CRISPRimmunity

Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP051775	Rhodospirillaceae bacterium B3 chromosome, complete genome	4 crisprs	DEDDh,csa3	0	3	1	0

1. NZ_CP051775

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP051775_2

• CRISPR_ID: NZ_CP051775_2
• CRISPR_location: 485361-485433
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP051775_2

Consensus_repeat	Method
GGCGCCCACCAGCTTGGCCTCGTTCAGG	CRISPRCasFinder

spacers of NZ_CP051775_2

>2.1|485389|17|NZ_CP051775|CRISPRCasFinder
ACGGTGCAGTGGAGCAG

CRISPR arrays and Neighbor proteins around NZ_CP051775_2

CRISPR arrays

The CRISPR arrays of NZ_CP051775_2

>merge|NZ_CP051775|2|485361-485433|CRISPRCasFinder
GGCGCCGGCCAGCTTCGCCCCCTTCAGCACGGTGCAGTGGAGCAGGGCGGCGGACAGGTTGGCCCCGGTCAGG

>NZ_CP051775|2|2|485361-485433|CRISPRCasFinder
GGCGCCGGCCAGCTTCGCCCCCTTCAGC	ACGGTGCAGTGGAGCAG
GGCGGCGGACAGGTTGGCCCCGGTCAGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	unknown	unknown	gnl|CDD|368240
NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator	unknown	unknown	gnl|CDD|226420
NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19	unknown	unknown	gnl|CDD|235418
NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|226628
NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	unknown	unknown	gnl|CDD|234581
NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter	unknown	unknown	gnl|CDD|223769
NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein	unknown	unknown	gnl|CDD|236780
NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit	unknown	unknown	gnl|CDD|181841
NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein	unknown	unknown	gnl|CDD|319923
NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|224584
NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16	unknown	unknown	gnl|CDD|234588
NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor	unknown	unknown	gnl|CDD|238657
NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein	unknown	unknown	gnl|CDD|226654
NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|182641

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	gnl|CDD|368240	pfam05016, ParE_toxin, ParE toxin of type II toxin-antitoxin system, parDE. ParE is the toxin family of a type II toxin-antitoxin family. It is toxic towards DNA gyrase, but is neutralized by the antitoxin ParD. The family also encompasses RelE/ParE described in.	8.7066e-15
NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator	gnl|CDD|226420	COG3905, COG3905, Predicted transcriptional regulator [Transcription].	3.44667e-06
NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19	gnl|CDD|235418	PRK05338, rplS, 50S ribosomal protein L19; Provisional.	1.80344e-71
NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein	gnl|CDD|226628	COG4148, ModC, ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism].	3.09437e-149
NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	gnl|CDD|234581	PRK00026, trmD, tRNA (guanine-N(1)-)-methyltransferase; Reviewed.	4.89807e-141
NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter	gnl|CDD|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	1.36559e-12
NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein	gnl|CDD|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit	gnl|CDD|181841	PRK09421, modB, molybdate ABC transporter permease subunit.	8.32723e-123
NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein	gnl|CDD|319923	cd07262, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	2.67281e-45
NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase	gnl|CDD|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	9.27405e-38
NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16	gnl|CDD|234588	PRK00040, rpsP, 30S ribosomal protein S16; Reviewed.	1.32363e-43
NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor	gnl|CDD|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	8.75619e-52
NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein	gnl|CDD|226654	COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms].	1.4923e-08
NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein	gnl|CDD|182641	PRK10677, modA, molybdate transporter periplasmic protein; Provisional.	2.01971e-87

Protein sequences

>NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein
MRIALAALVALSLALPAGAEVVFRRGIGPSPDTLDPTKGELQPSARMTYDLFEGLFSLDGQGQRRNAMAESHEVSPDGLTYTFKLREAKWSDGTPVTADDFVFGWRRLADPKHASPYGYYMWPVLNGQAIGEGKKKPEELGVQAVDARTLKVTLAEPTGYFLATLQHPSTFPVNRASVEKHGEAFVQPGKLVSNGPYMLVESVPQSHLKAVKNPHYYDAANVQVDTVMSYPIDNNDTEFKRFRAGELDATETLPVTQNDFAKQNLPDAFTSGSTYSTYYLSFNMTNPFWRDNPKLRAALYLAIDRDVIATKVMNGSGQPAWTFTPPGKVGGYEPPLPAAAKQTQAERDKLAKQLLAEAGFGPGGKPLPPVDLLYSTSENNRRVLVAVAAMWKQKLGVETQLNNQEFRVVASIGNEKAYKDIIFYAWIGDYPDPYTFLQLLRGDVGQQNFPGYKSAEYDRLTTEANRLTDPEKRLSLLAQAEAVALADYPVAPVFHNVRRRLVSPAVKGWTPNPPDFNLPRFLTVGK
>NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein
MGLALRRLALATLLSFGTATLAAAVPQPAAAEKVFRRGIGSGPGTIDPHKADVVSEAMVIYELFEGLMSLDAKGEPRYALAERHEMTADGLTYTFTLRANAKFSDGTPITAEDVVYSYRRLADPKTASPYGYFTWPIANGPEVNTGKKPLEQLGIEAVDPRTVRITLSQPAGYFLGQVSHQAMSVVQKASVEKHGQDWTRPGNLVGTGAYVLKETVPQSSFTMTRNPHYYDADQVKIDKVILYVTESTDTEFKQFRAGELEATYTTPLPQLGWVRQNMPDALKPTPLFATFYIAFNLQNEPWKSNPKLRQAMSLVIDRDVVAKKVMDPEVRPAVTFVPPNSVPGYASPIPAWAKQTQAERDAQARKLLAEAGYGPGGKPLPPVEVLYTTNENNRRILIAVAAMWKQKLGIEANLANQEGRVVAEIAQNRQFKDLLLFGWVGDYTDPNTFLKIMRSDVVLQNYPSFVSADYDRLLEEGNASLDPAARFAKLAQAEAIFLDSHAIMTAIHTTRFKLVSSKVKGWVPNPRDHYPTRYLDIAP
>NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein
MRLSPRLALIPVLAVMAAALAPPALAEKVLRRGIGSSPGTVDPNKAELHQESILIYDLFEGITAPDANGQPRPAMASRWEISPDGLTYTFHLRDGAKWSDGTPVTAADFAYSWRRLADPKTASPYAYYVWPILNGPEATAGKKPTSELGVEAVDAKTLKVTLGKPTSYFLASLVHQSMFPVQQKNVEGAQGNFTAAGVLVSNGAYKLAEAVPQSHYKLVRNDQYYDAKAVKIDTVMHYVTENLETELKRYRAGELDITYQIPITQVKWARENEPKAYTPTPTFSTQYMGANLNNEPWRSNPKLRAALSMAIDREVIAGKVLEGDMLPAWTFTPPIKGGAYQPPKPDWANLTQAQRDEMAKKLLAEAGYGPGGKPLPPVEVIHSTSENSRRVMIAVAAMWKQKLGLNVTLNNQEFRVVAQIANQKSYKDLLLYGWIGDFPDAVNFLKLLRSDVDQQNLSAYKNPAYDKLLDEANAATDPEKRLDLMRQAEALAQADFPVIPVYHNNRRRLVNPVVQGWVSNTMDQNPARWLDVVR
>NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator
MTMGKPLTLTLPPEVEATLGDLAARRGLSTAALATDIVSSFVADQEEFIRAVADGMADAEAGNLIDHEDVVAAIRRRRAAAA
>NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin
MRLRWTKLALADLEAIWRHIVKDNPQAADGVEDRIVDAAANLRQFPGLGRVGLVEGTRELVVPGLPYIIVYAAKPGGSSSTGCATASACGHPHDPHPSPDAVGTGATKGRVRVKRVPWPRRLATSMRPPRVLVTML
>NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein
MDGENGKQGQGRAARLLLDSLDGYADPFVLCDPDDRVLYTNARYHELFPAAPPQGEIRGWGFEALLRRVLAGGETPDPGIPDPEEFIRLRLAQRAALAGRSLSEATIGGRLFRRVEERTPNGCVITSYSDITDLKQAQEAAERNAARLAAAVEAIPGGFMMMDEGLNYLVWNSRYPGIGGTTDAVIRSHGNVRETLWLQARRGDYDDLRLDPGAFTAGQVADTPCLATLLRCQAARPPGQRPTEEEMEAQVEWHLLRFRPGGRVDGDNAEREGTFRVAGSGAVIEFRRTYTPGLGWVSLYTDVTERMREAEETAAARAAAERALADLRAAQASLVQAEKLASLGGLVAGIAHELNTPIGITYTAATHLKDQAARFRARLEGGQLRRAELDEFLDLVAEGAALLEANAGRASQLVQSFKNVSADRTHDERRRFELGPALEELVVSLGPAGARPGTCSAWIARRG
>NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein
MAEGLSVSLRHRQGDFTVEADFRAGPGVTALFGRSGAGKTTLLRAVAGLLRPQQGRITLGGRVFVDTGTGAWLPPHRRRVGYVFQDARLFPHLTVRQNLAYGRWFAGRGGATTVPFDDIVGMLGIVPLLGRRPGGLSGGERQRVAIGRALLAGAEVLLLDEPLASLDAARRAEILPYLERLRDGLDLPILHVSHSLAEVVRLATALVLVEQGRVVASGPLAAMLARPDLAALFGRFGTATLLEGTVEGHDPAWELTRVATPAGPLLLPRLDRPVGAAVRLRVLARDVLLSTRPPRDLSARNVLPGMVTALLPGTGAEMEASLDMAGQPLTASLTRLAAAELGLAPGQPVWAVVKAVAVVDGGTGLD
>NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit
MLDAFTPDELAAIRLSLRVAFWATLGSLPLGIGVAWLLARGRFPGKVLLDGLVHMPLVLPPVVTGYVLLLLFGRNGPLGKLLGEVGIVLAFDWKGAALACAVMGFPLLVRAVRLGLEAVDQGLEEAAATLGAAPPLVFLTVTLPLMLPGIVAGAILCFAKALGEFGATITFVSNIPGRTQTLPSALYSYTQVPGGDAGALRLTIVAAVLAVAALVASEMLARRVRRRVEGRDG
>NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein
MSPAFLRPVRRLLGAALLALGLAGGPPALAQAPPADQTVVFAAASLRNALDGIARQYQGETGKAVAISYAASSALARQIEAAAPAHIFIAADLDWMDYLEGKGLLAPGSRRTLLGNRLVLVAPKDSTAAVALGPGLDLTPVLGRDGRLALGDPASVPAGKYARAALEKLGAWDTVKGRLAPAENVRAALLLVSRGEAPAGIVYATDARADPSLKVLGTFPADSHPAILYPAALTAAGGKSADAAAFLAYLAGPKAKPLFEKEGFVILGN
>NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein
MLGHLSFGVRDLDASVSFYDAALAPLGLVLVWRSGRGAGYGPPGGEDILALFQEPGAHPPGPGFHLAFDAPDRTAVDRFHAAALSKGGRDQGPPGLRPQYHAHYYAAFVLDPDGHKLEAVHQPRRSD
>NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein
MFEGLTGRLGDIFDRLRKRGALSEDDVNAALREVRVALLEADVALPAVKAFVNGVKERAVGQEVLRGINPGQQVIKIVHDHLVELLGSASEEINLNANPPVPVLMLGLQGSGKTTTSAKIALRLKNREKKKVLMASLDTRRPAAQEQLKVLGEQVGVATLPIVPGQTPVQIARRALEEGRLGGFDVVMLDTAGRLAIDDELMREVVEIRDATKPVESLLVVDAMTGQDAVTVATNFNERVGITGIVMTRIDGDARGGAALSMRHVTGKPIKLLGVGEKVDALEAFHPDRIAGRILGMGDVVSLVEKAAETIDREEAEKLAKKLEKGGFDLDDMLSQLRQIRKMGGMGGMMGLLPGIGKIKDQLKNANIDEGILKKQEAIILSMTKKERRNPQVLNASRRRRIALGSGTTVADVNRLVKQHQDMAEMMKKMKKLGQKGLMRQGLGALLPKGFR
>NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase
MTDAAAIPAQAQTPPPPTTLVTARLVLRPLQVEDAEDLFPVFNDPESMRYWSHLPHKDVAETRAKLERVVEEDGTSRTWAVTRDGGRCQGWVSLFGAQDRLVWLGYILLPETRGQGLATEAVHAALDFAFGPWDMHRVEANLDPRNARSERLLKRLGFTREGVRREDFLLGGRYYDTLIYGLLAAEWRSARAAA
>NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16
MSVKIRLTRGGAKKRPYYSIVVADSRAPRDGAFIEKVGTYNPMLPAEHPERVTLKDERLKYWLSNGAQPTERVAKFLGKANLIEMPKFRDTPKKSAPKAKAQERAKLAAKAAEA
>NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD
MSDAPDPAGAEPPAGPLWSVTVLTLFPEMFPGPLGHSLAGRALEHGTWALETLDIRSFARDKHRSVDDTPFGGGPGMVMRPDVLDAALEAATAQAVAARGERGRAIYLSPRGRVLDQDLVKELAGERSLILLCGRYEGVDERVLEKHALEEVSLGDFVLSGGEPAALCLIDAVVRLLPGVMGNVETAGEESFERGLLEYPHYTRPAFWDGRQVPAVLLSGDHGKVRAWRLEQAEAITEARRPDLWSRYLESRPAPKVKKRRATKAAAQPSNPADDPAGTAGSNEDS
>NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19
MNILQQLEAEQVAKLTQGKTIPEFSPGDTVKVNVKVVEGTRERIQAYEGVVIARKNAGLNSAFTVRKISYGEGVERVFPLYSPRIDSIELVRKGAVRRAKLYYLRGRTGKSARIAERTTGRGMNDKGE
>NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor
MMGSNFRRSALLGATAMMAVCALGATGTAALAQSTQTAELDEIVVTATKRVQNLQEVPVSVAAVSPEQFENFSAAGEDIRFLSARVPSLTVESSFGRTFPRFYIRGLGNTDFDLNASQPVSLVYDEVVLENPIMKGFPVFDIERIEVLRGPQGTLFGRNTPAGIISVVSKKPTQKTEGYASLSYGRWNAIEAEAAVGGALVEDKLAARVSVIHQRRDGYVDNTFTGEKDALEGYEDTAARLQLLYTPTERFTALLNGHFRDLNGTARVFRANIIKPGTNELVDGFTPYKAYVDGQNDQEVSARGASLNAQYEFDGVTFTSITAYEYVDAFSRGDVDGGVARGIGNPLTGPGRVPFSVESASEVAGIDQWTQEFRLSSSGEGPLQWQVGAFYFDEKAPFANIGYGTATTDPRGRTTLASSVQNNETWAVFGQGSYKVTEQLTLTGGLRYTEDEKDLVRRQISVNGTNAPTVTSRASTEDERISWDVSADYAFTADVRGFVRVASGFRAPTIQPRSVTITTADSEKVMSYEAGVKSDLFGNRARVNVTAFYYRVKDQQFTAVGGVDNTNRLLNADKGVGKGFEADLEFLPLENLLLTVGTSYNDTEIKDADLRVPACGGGCTVTDAITVVGTSRLANIDGNPFPQAPKWIFNATARYGIPVGDAGEVYAFTDWSYKSSQNFFLYESVEFKSDARWQGGLRLGYSHDNGRFDVSAFVRNITNEQGLEGGIDFNNLTGFVIEPRTYGVTARMKF
>NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein
MRKGWFMGIRAWVAAFLTVLLLAAPATAQKVLHRGNGSEPETLDPHKSTGEPEGWIQYDLFEGLMTVDGAGNLIPGAAESYTVSPDGLTYTFKLRDTVWSDGTPVTAEDFAFSWRRLLDPKTGSRYAFFLWPVKNAEKANKGEVPLSEVGVAAPDPRTFVVTLEAPTSYFASALQHNATYAISKKSYEKHGEDFIKPGNLVSNGAFMLVEAVPQGYVRVRKNPRYWDAANVRLDEVVFHATENRDTELKRFRAGELHLTYDVPDPQIPWLKQNMPAELRIAPFFSTYYYAFNLTREPWKSNPDLRKALALAIDRTIITEKITLSGEVPAYQLVPDGTANYASPKPEWASWTQSQRDTEARRLVEAAGYGKGGKPLEVELFYNTSENHKKVAVAVASMWQQKLGVRTVMNNQEWKVFLQTRSRKQYRDIALGRWVGDYNDAYTFLGLFLSDLGPSNYSGYASPEYDRLVRAASSEVDAEKRRDLLQRAEAVLLADLPIIPVYIYTTQNMVSPRVKGWVPNIRNLHPSRFLDLN
>NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein
MKTLFNRARAIALGALLAAGSLAVSAVPAEAQKILHRGNGSEPETLDPHKSTGVPESYIQYDLFEGLVVPDGKGNLIPGAAESWSSNADGTVFTFKLRKNAKWSDGTPVTADDWVYSWRRVVDPKTMSKYAWYLWPVKNGEAVSNGKLPPDQFGVRALDPLTFEVTLEGPTPYFVSMLQHHATYAVNRASIEKHGDEFIRPGNYVTNGPYMLAEAVPQSHIKVVKNPHFHDAANVKIDTVMFYPTENIEAELKRFRAGELDITYEIPVSQMDWVRQNMAKQARLAPYFGTYFFAPNLTKEPWKSNKDLRLALNLAIDRQTLVDKINKRGEQPAYSWLPPGTENYTQQVPEYANWTQEQREAKAKELVKKAGYGPGGKPLEVEVLFNTSENHRKMAIAVASMWQKVLGAKVTLNNQEWKVFLSTRDEKKFKDVVRHGWIGDYLDANNFLALFRSDVGKQNPSGYNNPEFDRLVSEANKLADVEKRRALLQQAERLMIEDVAFFPLHFYSSRHMVSDRVIGWGDNLQDLHPSRFLDVK
>NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein
MRFVRRLAPAIAAAALAATLTAAPAFAEMVLNRGNQAEPSSLDPHKGTDMQSARIGYDLFEGLLTFAPDGKAIPGVAERWEISADGLTYTFFLRKDAKWSDGTPVTAEDFVFSWRRLVDPKTASDYAYFLWPVKNGEAISNGKAPLDSMGVVAKDPHTLVVTLERPTGYFLSSLIHRMTYPVSKANVEKFGPDFVKPGNMVSNGAYRMVEAVPQAYVKAVKNPHFREASTVKIDTVLYHHTDSQETELRRFRAGELDTLQMAPVTQIDWLKQNMPDVMEFYPVLGIRYLGVNMVKGPLANEPKVRLALALAVDRETLTEKVTKAGEPPKMTFIPDGIPGYQSPDLPFLKMTQAERDAMAKKLVAEAGYGPGGKPLAFEIMHATNESTRKTMVAIASMWQQKLGAKVSLNNQEWKVVLQKAGEKDYNGLVELGWIGDFPDPYTFMKLFLGSVGKMNRSGYKNADYDALLDKANATVDPAERLKLMAQAEAMLLQDAPLVVQFHATYRNLVHKHVKGWFESPMGVQPTRYLSIQK
>NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter
MPPAPRPDNKALGILLAVLAFALYSVTDATVKALSARMSVPQIIVGNGLFSLVPIIGYAAWSGGLRFLRPRRPLLHLARATCGLFSGFLAYYGYSQMPIADAYALSFTAPLFITALSVPMLGEKVGWRRWTAVAVGFLGVMVMLRPGSGSLNPAALGILAGAALYSMGMMITRLARATDSAVSFAFSTTIVGLAVWGATLPWLAVAPTMDDLVLHALGGTCVGIAIVLLLSGFRLAPAAVVAPFQYTQILWGVALGWLLFGDRPTAPMLLGAGIVIASGLYILYRETVLGRQRAAAAPPREAA

Crispr_ID: NZ_CP051775_1

• CRISPR_ID: NZ_CP051775_1
• CRISPR_location: 484980-485269
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 4 spacers

Consensus repeat of NZ_CP051775_1

Consensus_repeat	Method
GGCGCCCACCAGCTTGGCCTCGTTCAGG	CRISPRCasFinder

spacers of NZ_CP051775_1

>1.1|485008|47|NZ_CP051775|CRISPRCasFinder
TCGGCGCCGGTCAGGACGGCGCCGGTGCATCGGGCATCGGTCAGGTC
>1.2|485083|17|NZ_CP051775|CRISPRCasFinder
CGGGTCTCATGCAGGTC
>1.3|485128|32|NZ_CP051775|CRISPRCasFinder
ATGGCGCGGCGCAGGTCGGCCCTGGACAGGTC
>1.4|485188|53|NZ_CP051775|CRISPRCasFinder
TTCGCGCTCCACAGCCGGCCGCTGCCGGACTGGATCTGGACCGGGCCCACCAG

CRISPR arrays and Neighbor proteins around NZ_CP051775_1

CRISPR arrays

The CRISPR arrays of NZ_CP051775_1

>merge|NZ_CP051775|1|484980-485269|CRISPRCasFinder
GGCGCCCACCAGCTTGGCCTCGTTCAGGTCGGCGCCGGTCAGGACGGCGCCGGTGCATCGGGCATCGGTCAGGTCGGCGCCCACCAGCTTGGCGTCGTTCAGGCGGGTCTCATGCAGGTCGGCACCCACGAGGGTGGCCTGGTTCAGGATGGCGCGGCGCAGGTCGGCCCTGGACAGGTCGGCCCCGTCCAGCCGGGCCCGTTGCAGGTTCGCGCTCCACAGCCGGCCGCTGCCGGACTGGATCTGGACCGGGCCCACCAGGGCGCCGGACAGCTTGGCCCGGGACAGGG

>NZ_CP051775|1|1|484980-485269|CRISPRCasFinder
GGCGCCCACCAGCTTGGCCTCGTTCAGG	TCGGCGCCGGTCAGGACGGCGCCGGTGCATCGGGCATCGGTCAGGTC
GGCGCCCACCAGCTTGGCGTCGTTCAGG	CGGGTCTCATGCAGGTC
GGCACCCACGAGGGTGGCCTGGTTCAGG	ATGGCGCGGCGCAGGTCGGCCCTGGACAGGTC
GGCCCCGTCCAGCCGGGCCCGTTGCAGG	TTCGCGCTCCACAGCCGGCCGCTGCCGGACTGGATCTGGACCGGGCCCACCAG
GGCGCCGGACAGCTTGGCCCGGGACAGGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	unknown	unknown	gnl|CDD|368240
NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator	unknown	unknown	gnl|CDD|226420
NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19	unknown	unknown	gnl|CDD|235418
NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|226628
NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	unknown	unknown	gnl|CDD|234581
NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter	unknown	unknown	gnl|CDD|223769
NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein	unknown	unknown	gnl|CDD|236780
NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit	unknown	unknown	gnl|CDD|181841
NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein	unknown	unknown	gnl|CDD|319923
NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|224584
NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16	unknown	unknown	gnl|CDD|234588
NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor	unknown	unknown	gnl|CDD|238657
NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein	unknown	unknown	gnl|CDD|226654
NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173869
NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|182641

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin	gnl|CDD|368240	pfam05016, ParE_toxin, ParE toxin of type II toxin-antitoxin system, parDE. ParE is the toxin family of a type II toxin-antitoxin family. It is toxic towards DNA gyrase, but is neutralized by the antitoxin ParD. The family also encompasses RelE/ParE described in.	8.7066e-15
NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator	gnl|CDD|226420	COG3905, COG3905, Predicted transcriptional regulator [Transcription].	3.44667e-06
NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19	gnl|CDD|235418	PRK05338, rplS, 50S ribosomal protein L19; Provisional.	1.80344e-71
NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein	gnl|CDD|226628	COG4148, ModC, ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism].	3.09437e-149
NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	gnl|CDD|234581	PRK00026, trmD, tRNA (guanine-N(1)-)-methyltransferase; Reviewed.	4.89807e-141
NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter	gnl|CDD|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	1.36559e-12
NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein	gnl|CDD|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit	gnl|CDD|181841	PRK09421, modB, molybdate ABC transporter permease subunit.	8.32723e-123
NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein	gnl|CDD|319923	cd07262, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	2.67281e-45
NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase	gnl|CDD|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	9.27405e-38
NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16	gnl|CDD|234588	PRK00040, rpsP, 30S ribosomal protein S16; Reviewed.	1.32363e-43
NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor	gnl|CDD|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	8.75619e-52
NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein	gnl|CDD|226654	COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms].	1.4923e-08
NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein	gnl|CDD|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	0
NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein	gnl|CDD|182641	PRK10677, modA, molybdate transporter periplasmic protein; Provisional.	2.01971e-87

Protein sequences

>NZ_CP051775.1|WP_075771943.1|481327_482908_+|peptide-ABC-transporter-substrate-binding-protein
MRIALAALVALSLALPAGAEVVFRRGIGPSPDTLDPTKGELQPSARMTYDLFEGLFSLDGQGQRRNAMAESHEVSPDGLTYTFKLREAKWSDGTPVTADDFVFGWRRLADPKHASPYGYYMWPVLNGQAIGEGKKKPEELGVQAVDARTLKVTLAEPTGYFLATLQHPSTFPVNRASVEKHGEAFVQPGKLVSNGPYMLVESVPQSHLKAVKNPHYYDAANVQVDTVMSYPIDNNDTEFKRFRAGELDATETLPVTQNDFAKQNLPDAFTSGSTYSTYYLSFNMTNPFWRDNPKLRAALYLAIDRDVIATKVMNGSGQPAWTFTPPGKVGGYEPPLPAAAKQTQAERDKLAKQLLAEAGFGPGGKPLPPVDLLYSTSENNRRVLVAVAAMWKQKLGVETQLNNQEFRVVASIGNEKAYKDIIFYAWIGDYPDPYTFLQLLRGDVGQQNFPGYKSAEYDRLTTEANRLTDPEKRLSLLAQAEAVALADYPVAPVFHNVRRRLVSPAVKGWTPNPPDFNLPRFLTVGK
>NZ_CP051775.1|WP_075771942.1|479613_481233_+|peptide-ABC-transporter-substrate-binding-protein
MGLALRRLALATLLSFGTATLAAAVPQPAAAEKVFRRGIGSGPGTIDPHKADVVSEAMVIYELFEGLMSLDAKGEPRYALAERHEMTADGLTYTFTLRANAKFSDGTPITAEDVVYSYRRLADPKTASPYGYFTWPIANGPEVNTGKKPLEQLGIEAVDPRTVRITLSQPAGYFLGQVSHQAMSVVQKASVEKHGQDWTRPGNLVGTGAYVLKETVPQSSFTMTRNPHYYDADQVKIDKVILYVTESTDTEFKQFRAGELEATYTTPLPQLGWVRQNMPDALKPTPLFATFYIAFNLQNEPWKSNPKLRQAMSLVIDRDVVAKKVMDPEVRPAVTFVPPNSVPGYASPIPAWAKQTQAERDAQARKLLAEAGYGPGGKPLPPVEVLYTTNENNRRILIAVAAMWKQKLGIEANLANQEGRVVAEIAQNRQFKDLLLFGWVGDYTDPNTFLKIMRSDVVLQNYPSFVSADYDRLLEEGNASLDPAARFAKLAQAEAIFLDSHAIMTAIHTTRFKLVSSKVKGWVPNPRDHYPTRYLDIAP
>NZ_CP051775.1|WP_075771941.1|477890_479495_+|peptide-ABC-transporter-substrate-binding-protein
MRLSPRLALIPVLAVMAAALAPPALAEKVLRRGIGSSPGTVDPNKAELHQESILIYDLFEGITAPDANGQPRPAMASRWEISPDGLTYTFHLRDGAKWSDGTPVTAADFAYSWRRLADPKTASPYAYYVWPILNGPEATAGKKPTSELGVEAVDAKTLKVTLGKPTSYFLASLVHQSMFPVQQKNVEGAQGNFTAAGVLVSNGAYKLAEAVPQSHYKLVRNDQYYDAKAVKIDTVMHYVTENLETELKRYRAGELDITYQIPITQVKWARENEPKAYTPTPTFSTQYMGANLNNEPWRSNPKLRAALSMAIDREVIAGKVLEGDMLPAWTFTPPIKGGAYQPPKPDWANLTQAQRDEMAKKLLAEAGYGPGGKPLPPVEVIHSTSENSRRVMIAVAAMWKQKLGLNVTLNNQEFRVVAQIANQKSYKDLLLYGWIGDFPDAVNFLKLLRSDVDQQNLSAYKNPAYDKLLDEANAATDPEKRLDLMRQAEALAQADFPVIPVYHNNRRRLVNPVVQGWVSNTMDQNPARWLDVVR
>NZ_CP051775.1|WP_169654605.1|476652_476901_-|CopG-family-transcriptional-regulator
MTMGKPLTLTLPPEVEATLGDLAARRGLSTAALATDIVSSFVADQEEFIRAVADGMADAEAGNLIDHEDVVAAIRRRRAAAA
>NZ_CP051775.1|WP_169654603.1|476245_476656_-|type-II-toxin-antitoxin-system-RelE/ParE-family-toxin
MRLRWTKLALADLEAIWRHIVKDNPQAADGVEDRIVDAAANLRQFPGLGRVGLVEGTRELVVPGLPYIIVYAAKPGGSSSTGCATASACGHPHDPHPSPDAVGTGATKGRVRVKRVPWPRRLATSMRPPRVLVTML
>NZ_CP051775.1|WP_169654601.1|474600_475992_+|hypothetical-protein
MDGENGKQGQGRAARLLLDSLDGYADPFVLCDPDDRVLYTNARYHELFPAAPPQGEIRGWGFEALLRRVLAGGETPDPGIPDPEEFIRLRLAQRAALAGRSLSEATIGGRLFRRVEERTPNGCVITSYSDITDLKQAQEAAERNAARLAAAVEAIPGGFMMMDEGLNYLVWNSRYPGIGGTTDAVIRSHGNVRETLWLQARRGDYDDLRLDPGAFTAGQVADTPCLATLLRCQAARPPGQRPTEEEMEAQVEWHLLRFRPGGRVDGDNAEREGTFRVAGSGAVIEFRRTYTPGLGWVSLYTDVTERMREAEETAAARAAAERALADLRAAQASLVQAEKLASLGGLVAGIAHELNTPIGITYTAATHLKDQAARFRARLEGGQLRRAELDEFLDLVAEGAALLEANAGRASQLVQSFKNVSADRTHDERRRFELGPALEELVVSLGPAGARPGTCSAWIARRG
>NZ_CP051775.1|WP_075771937.1|473365_474466_+|molybdenum-ABC-transporter-ATP-binding-protein
MAEGLSVSLRHRQGDFTVEADFRAGPGVTALFGRSGAGKTTLLRAVAGLLRPQQGRITLGGRVFVDTGTGAWLPPHRRRVGYVFQDARLFPHLTVRQNLAYGRWFAGRGGATTVPFDDIVGMLGIVPLLGRRPGGLSGGERQRVAIGRALLAGAEVLLLDEPLASLDAARRAEILPYLERLRDGLDLPILHVSHSLAEVVRLATALVLVEQGRVVASGPLAAMLARPDLAALFGRFGTATLLEGTVEGHDPAWELTRVATPAGPLLLPRLDRPVGAAVRLRVLARDVLLSTRPPRDLSARNVLPGMVTALLPGTGAEMEASLDMAGQPLTASLTRLAAAELGLAPGQPVWAVVKAVAVVDGGTGLD
>NZ_CP051775.1|WP_075771936.1|472671_473373_+|molybdate-ABC-transporter-permease-subunit
MLDAFTPDELAAIRLSLRVAFWATLGSLPLGIGVAWLLARGRFPGKVLLDGLVHMPLVLPPVVTGYVLLLLFGRNGPLGKLLGEVGIVLAFDWKGAALACAVMGFPLLVRAVRLGLEAVDQGLEEAAATLGAAPPLVFLTVTLPLMLPGIVAGAILCFAKALGEFGATITFVSNIPGRTQTLPSALYSYTQVPGGDAGALRLTIVAAVLAVAALVASEMLARRVRRRVEGRDG
>NZ_CP051775.1|WP_075771935.1|471819_472629_+|molybdate-ABC-transporter-substrate-binding-protein
MSPAFLRPVRRLLGAALLALGLAGGPPALAQAPPADQTVVFAAASLRNALDGIARQYQGETGKAVAISYAASSALARQIEAAAPAHIFIAADLDWMDYLEGKGLLAPGSRRTLLGNRLVLVAPKDSTAAVALGPGLDLTPVLGRDGRLALGDPASVPAGKYARAALEKLGAWDTVKGRLAPAENVRAALLLVSRGEAPAGIVYATDARADPSLKVLGTFPADSHPAILYPAALTAAGGKSADAAAFLAYLAGPKAKPLFEKEGFVILGN
>NZ_CP051775.1|WP_075771934.1|471287_471671_-|VOC-family-protein
MLGHLSFGVRDLDASVSFYDAALAPLGLVLVWRSGRGAGYGPPGGEDILALFQEPGAHPPGPGFHLAFDAPDRTAVDRFHAAALSKGGRDQGPPGLRPQYHAHYYAAFVLDPDGHKLEAVHQPRRSD
>NZ_CP051775.1|WP_075771945.1|486677_488036_+|signal-recognition-particle-protein
MFEGLTGRLGDIFDRLRKRGALSEDDVNAALREVRVALLEADVALPAVKAFVNGVKERAVGQEVLRGINPGQQVIKIVHDHLVELLGSASEEINLNANPPVPVLMLGLQGSGKTTTSAKIALRLKNREKKKVLMASLDTRRPAAQEQLKVLGEQVGVATLPIVPGQTPVQIARRALEEGRLGGFDVVMLDTAGRLAIDDELMREVVEIRDATKPVESLLVVDAMTGQDAVTVATNFNERVGITGIVMTRIDGDARGGAALSMRHVTGKPIKLLGVGEKVDALEAFHPDRIAGRILGMGDVVSLVEKAAETIDREEAEKLAKKLEKGGFDLDDMLSQLRQIRKMGGMGGMMGLLPGIGKIKDQLKNANIDEGILKKQEAIILSMTKKERRNPQVLNASRRRRIALGSGTTVADVNRLVKQHQDMAEMMKKMKKLGQKGLMRQGLGALLPKGFR
>NZ_CP051775.1|WP_075771946.1|488043_488628_+|GNAT-family-N-acetyltransferase
MTDAAAIPAQAQTPPPPTTLVTARLVLRPLQVEDAEDLFPVFNDPESMRYWSHLPHKDVAETRAKLERVVEEDGTSRTWAVTRDGGRCQGWVSLFGAQDRLVWLGYILLPETRGQGLATEAVHAALDFAFGPWDMHRVEANLDPRNARSERLLKRLGFTREGVRREDFLLGGRYYDTLIYGLLAAEWRSARAAA
>NZ_CP051775.1|WP_075771947.1|488753_489098_+|30S-ribosomal-protein-S16
MSVKIRLTRGGAKKRPYYSIVVADSRAPRDGAFIEKVGTYNPMLPAEHPERVTLKDERLKYWLSNGAQPTERVAKFLGKANLIEMPKFRDTPKKSAPKAKAQERAKLAAKAAEA
>NZ_CP051775.1|WP_075771949.1|489967_490828_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD
MSDAPDPAGAEPPAGPLWSVTVLTLFPEMFPGPLGHSLAGRALEHGTWALETLDIRSFARDKHRSVDDTPFGGGPGMVMRPDVLDAALEAATAQAVAARGERGRAIYLSPRGRVLDQDLVKELAGERSLILLCGRYEGVDERVLEKHALEEVSLGDFVLSGGEPAALCLIDAVVRLLPGVMGNVETAGEESFERGLLEYPHYTRPAFWDGRQVPAVLLSGDHGKVRAWRLEQAEAITEARRPDLWSRYLESRPAPKVKKRRATKAAAQPSNPADDPAGTAGSNEDS
>NZ_CP051775.1|WP_075771950.1|490829_491216_+|50S-ribosomal-protein-L19
MNILQQLEAEQVAKLTQGKTIPEFSPGDTVKVNVKVVEGTRERIQAYEGVVIARKNAGLNSAFTVRKISYGEGVERVFPLYSPRIDSIELVRKGAVRRAKLYYLRGRTGKSARIAERTTGRGMNDKGE
>NZ_CP051775.1|WP_169654607.1|491521_493774_-|TonB-dependent-receptor
MMGSNFRRSALLGATAMMAVCALGATGTAALAQSTQTAELDEIVVTATKRVQNLQEVPVSVAAVSPEQFENFSAAGEDIRFLSARVPSLTVESSFGRTFPRFYIRGLGNTDFDLNASQPVSLVYDEVVLENPIMKGFPVFDIERIEVLRGPQGTLFGRNTPAGIISVVSKKPTQKTEGYASLSYGRWNAIEAEAAVGGALVEDKLAARVSVIHQRRDGYVDNTFTGEKDALEGYEDTAARLQLLYTPTERFTALLNGHFRDLNGTARVFRANIIKPGTNELVDGFTPYKAYVDGQNDQEVSARGASLNAQYEFDGVTFTSITAYEYVDAFSRGDVDGGVARGIGNPLTGPGRVPFSVESASEVAGIDQWTQEFRLSSSGEGPLQWQVGAFYFDEKAPFANIGYGTATTDPRGRTTLASSVQNNETWAVFGQGSYKVTEQLTLTGGLRYTEDEKDLVRRQISVNGTNAPTVTSRASTEDERISWDVSADYAFTADVRGFVRVASGFRAPTIQPRSVTITTADSEKVMSYEAGVKSDLFGNRARVNVTAFYYRVKDQQFTAVGGVDNTNRLLNADKGVGKGFEADLEFLPLENLLLTVGTSYNDTEIKDADLRVPACGGGCTVTDAITVVGTSRLANIDGNPFPQAPKWIFNATARYGIPVGDAGEVYAFTDWSYKSSQNFFLYESVEFKSDARWQGGLRLGYSHDNGRFDVSAFVRNITNEQGLEGGIDFNNLTGFVIEPRTYGVTARMKF
>NZ_CP051775.1|WP_169654609.1|494002_495601_-|peptide-ABC-transporter-substrate-binding-protein
MRKGWFMGIRAWVAAFLTVLLLAAPATAQKVLHRGNGSEPETLDPHKSTGEPEGWIQYDLFEGLMTVDGAGNLIPGAAESYTVSPDGLTYTFKLRDTVWSDGTPVTAEDFAFSWRRLLDPKTGSRYAFFLWPVKNAEKANKGEVPLSEVGVAAPDPRTFVVTLEAPTSYFASALQHNATYAISKKSYEKHGEDFIKPGNLVSNGAFMLVEAVPQGYVRVRKNPRYWDAANVRLDEVVFHATENRDTELKRFRAGELHLTYDVPDPQIPWLKQNMPAELRIAPFFSTYYYAFNLTREPWKSNPDLRKALALAIDRTIITEKITLSGEVPAYQLVPDGTANYASPKPEWASWTQSQRDTEARRLVEAAGYGKGGKPLEVELFYNTSENHKKVAVAVASMWQQKLGVRTVMNNQEWKVFLQTRSRKQYRDIALGRWVGDYNDAYTFLGLFLSDLGPSNYSGYASPEYDRLVRAASSEVDAEKRRDLLQRAEAVLLADLPIIPVYIYTTQNMVSPRVKGWVPNIRNLHPSRFLDLN
>NZ_CP051775.1|WP_075773040.1|495874_497485_-|peptide-ABC-transporter-substrate-binding-protein
MKTLFNRARAIALGALLAAGSLAVSAVPAEAQKILHRGNGSEPETLDPHKSTGVPESYIQYDLFEGLVVPDGKGNLIPGAAESWSSNADGTVFTFKLRKNAKWSDGTPVTADDWVYSWRRVVDPKTMSKYAWYLWPVKNGEAVSNGKLPPDQFGVRALDPLTFEVTLEGPTPYFVSMLQHHATYAVNRASIEKHGDEFIRPGNYVTNGPYMLAEAVPQSHIKVVKNPHFHDAANVKIDTVMFYPTENIEAELKRFRAGELDITYEIPVSQMDWVRQNMAKQARLAPYFGTYFFAPNLTKEPWKSNKDLRLALNLAIDRQTLVDKINKRGEQPAYSWLPPGTENYTQQVPEYANWTQEQREAKAKELVKKAGYGPGGKPLEVEVLFNTSENHRKMAIAVASMWQKVLGAKVTLNNQEWKVFLSTRDEKKFKDVVRHGWIGDYLDANNFLALFRSDVGKQNPSGYNNPEFDRLVSEANKLADVEKRRALLQQAERLMIEDVAFFPLHFYSSRHMVSDRVIGWGDNLQDLHPSRFLDVK
>NZ_CP051775.1|WP_075773041.1|497666_499268_-|peptide-ABC-transporter-substrate-binding-protein
MRFVRRLAPAIAAAALAATLTAAPAFAEMVLNRGNQAEPSSLDPHKGTDMQSARIGYDLFEGLLTFAPDGKAIPGVAERWEISADGLTYTFFLRKDAKWSDGTPVTAEDFVFSWRRLVDPKTASDYAYFLWPVKNGEAISNGKAPLDSMGVVAKDPHTLVVTLERPTGYFLSSLIHRMTYPVSKANVEKFGPDFVKPGNMVSNGAYRMVEAVPQAYVKAVKNPHFREASTVKIDTVLYHHTDSQETELRRFRAGELDTLQMAPVTQIDWLKQNMPDVMEFYPVLGIRYLGVNMVKGPLANEPKVRLALALAVDRETLTEKVTKAGEPPKMTFIPDGIPGYQSPDLPFLKMTQAERDAMAKKLVAEAGYGPGGKPLAFEIMHATNESTRKTMVAIASMWQQKLGAKVSLNNQEWKVVLQKAGEKDYNGLVELGWIGDFPDPYTFMKLFLGSVGKMNRSGYKNADYDALLDKANATVDPAERLKLMAQAEAMLLQDAPLVVQFHATYRNLVHKHVKGWFESPMGVQPTRYLSIQK
>NZ_CP051775.1|WP_083699524.1|499524_500436_+|DMT-family-transporter
MPPAPRPDNKALGILLAVLAFALYSVTDATVKALSARMSVPQIIVGNGLFSLVPIIGYAAWSGGLRFLRPRRPLLHLARATCGLFSGFLAYYGYSQMPIADAYALSFTAPLFITALSVPMLGEKVGWRRWTAVAVGFLGVMVMLRPGSGSLNPAALGILAGAALYSMGMMITRLARATDSAVSFAFSTTIVGLAVWGATLPWLAVAPTMDDLVLHALGGTCVGIAIVLLLSGFRLAPAAVVAPFQYTQILWGVALGWLLFGDRPTAPMLLGAGIVIASGLYILYRETVLGRQRAAAAPPREAA

Crispr_ID: NZ_CP051775_3

• CRISPR_ID: NZ_CP051775_3
• CRISPR_location: 682989-683185
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 3 spacers

Consensus repeat of NZ_CP051775_3

Consensus_repeat	Method
ACGTCGCCGGAACCGTTGATCTC	CRISPRCasFinder

spacers of NZ_CP051775_3

>3.1|683012|37|NZ_CP051775|CRISPRCasFinder
GACCGCCAGCGGGTCGGCCATGCCGGCCTTCAGCGTG
>3.2|683072|34|NZ_CP051775|CRISPRCasFinder
CACCTTCACAGGCCCGTCCACCCGGGCCACCTCC
>3.3|683129|34|NZ_CP051775|CRISPRCasFinder
AACCTCCAGTTGGCCGCTGGTCCGGCCAGTGCGG

CRISPR arrays and Neighbor proteins around NZ_CP051775_3

CRISPR arrays

The CRISPR arrays of NZ_CP051775_3

>merge|NZ_CP051775|3|682989-683185|CRISPRCasFinder
ACGTCGCCCGATCCCCTGATGGCGACCGCCAGCGGGTCGGCCATGCCGGCCTTCAGCGTGACGTCGCCGGACCCGTTGACCTCCACCTTCACAGGCCCGTCCACCCGGGCCACCTCCACGTCGCCGGAACCGTTGATCTCAACCTCCAGTTGGCCGCTGGTCCGGCCAGTGCGGACGTCGCCGGAGCCGTTGATCTC

>NZ_CP051775|3|3|682989-683185|CRISPRCasFinder
ACGTCGCCCGATCCCCTGATGGC	GACCGCCAGCGGGTCGGCCATGCCGGCCTTCAGCGTG
ACGTCGCCGGACCCGTTGACCTC	CACCTTCACAGGCCCGTCCACCCGGGCCACCTCC
ACGTCGCCGGAACCGTTGATCTC	AACCTCCAGTTGGCCGCTGGTCCGGCCAGTGCGG
ACGTCGCCGGAGCCGTTGATCTC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051775.1|WP_075773322.1|691310_691571_-|DUF2283-domain-containing-protein	unknown	unknown	gnl|CDD|378367
NZ_CP051775.1|WP_075772106.1|671923_672682_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075773323.1|690895_691171_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_169654682.1|682095_682866_-|hypothetical-protein	unknown	unknown	gnl|CDD|371327
NZ_CP051775.1|WP_075772108.1|675071_675512_+|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl|CDD|378915
NZ_CP051775.1|WP_169654692.1|687230_687767_-|2OG-Fe(II)-oxygenase	unknown	unknown	gnl|CDD|379309
NZ_CP051775.1|WP_169654690.1|684770_687161_+|tetratricopeptide-repeat-protein	unknown	unknown	gnl|CDD|274350
NZ_CP051775.1|WP_075773324.1|690659_690890_-|DUF2283-domain-containing-protein	unknown	unknown	gnl|CDD|227715
NZ_CP051775.1|WP_075772109.1|676503_676788_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_169654686.1|683286_683682_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075772105.1|671106_671838_+|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|212491
NZ_CP051775.1|WP_075773330.1|691567_691771_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075773325.1|690089_690611_-|2'-5'-RNA-ligase-family-protein	unknown	unknown	gnl|CDD|379265
NZ_CP051775.1|WP_083699260.1|675597_676443_+|pantoate--beta-alanine-ligase	unknown	unknown	gnl|CDD|234741
NZ_CP051775.1|WP_075772113.1|679959_682083_+|ammonium-transporter	unknown	unknown	gnl|CDD|273292
NZ_CP051775.1|WP_075772112.1|678337_679783_+|NADP-dependent-isocitrate-dehydrogenase	unknown	unknown	gnl|CDD|236416
NZ_CP051775.1|WP_075772107.1|674292_675075_+|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl|CDD|187608
NZ_CP051775.1|WP_169654688.1|683931_684786_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075773326.1|687870_690003_-|NAD-dependent-DNA-ligase-LigA	unknown	unknown	gnl|CDD|236137
NZ_CP051775.1|WP_075772111.1|677663_678083_-|lactoylglutathione-lyase	unknown	unknown	gnl|CDD|272886

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP051775.1|WP_075773325.1|690089_690611_-|2'-5'-RNA-ligase-family-protein	gnl|CDD|379265	pfam13563, 2_5_RNA_ligase2, 2'-5' RNA ligase superfamily. This family contains proteins related to pfam02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity.	8.18146e-24
NZ_CP051775.1|WP_169654682.1|682095_682866_-|hypothetical-protein	gnl|CDD|371327	pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).	2.21223e-11
NZ_CP051775.1|WP_169654690.1|684770_687161_+|tetratricopeptide-repeat-protein	gnl|CDD|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	2.01704e-18
NZ_CP051775.1|WP_075772108.1|675071_675512_+|nuclear-transport-factor-2-family-protein	gnl|CDD|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	5.9703e-09
NZ_CP051775.1|WP_169654692.1|687230_687767_-|2OG-Fe(II)-oxygenase	gnl|CDD|379309	pfam13640, 2OG-FeII_Oxy_3, 2OG-Fe(II) oxygenase superfamily. This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.	1.14205e-14
NZ_CP051775.1|WP_075773324.1|690659_690890_-|DUF2283-domain-containing-protein	gnl|CDD|227715	COG5428, COG5428, Uncharacterized conserved small protein [Function unknown].	4.91925e-08
NZ_CP051775.1|WP_075773322.1|691310_691571_-|DUF2283-domain-containing-protein	gnl|CDD|378367	pfam10049, DUF2283, Protein of unknown function (DUF2283). Members of this family of hypothetical bacterial proteins have no known function.	8.83394e-05
NZ_CP051775.1|WP_075772105.1|671106_671838_+|SDR-family-oxidoreductase	gnl|CDD|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	2.70488e-42
NZ_CP051775.1|WP_083699260.1|675597_676443_+|pantoate--beta-alanine-ligase	gnl|CDD|234741	PRK00380, panC, pantoate--beta-alanine ligase; Reviewed.	1.66609e-150
NZ_CP051775.1|WP_075772113.1|679959_682083_+|ammonium-transporter	gnl|CDD|273292	TIGR00836, Ammonium_transporter, ammonium transporter. The Ammonium Transporter (Amt) Family (TC 2.A.49) All functionally characterized members of the Amt family are ammonia or ammonium uptake transporters. Some, but not others, also transport methylammonium. The mechanism of energy coupling, if any, to methyl-NH2 or NH3 uptake by the AmtB protein of E. coli is not entirely clear. NH4+ uniport driven by the pmf, energy independent NH3 facilitation, and NH4+/K+ antiport have been proposed as possible transport mechanisms. In Corynebacterium glutamicum and Arabidopsis thaliana, uptake via the Amt1 homologues of AmtB has been reported to be driven by the pmf. [Transport and binding proteins, Cations and iron carrying compounds].	7.65651e-134
NZ_CP051775.1|WP_075772112.1|678337_679783_+|NADP-dependent-isocitrate-dehydrogenase	gnl|CDD|236416	PRK09222, PRK09222, NADP-dependent isocitrate dehydrogenase.	0
NZ_CP051775.1|WP_075772107.1|674292_675075_+|SDR-family-NAD(P)-dependent-oxidoreductase	gnl|CDD|187608	cd05350, SDR_c6, classical (c) SDR, subgroup 6. These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	3.56678e-74
NZ_CP051775.1|WP_075773326.1|687870_690003_-|NAD-dependent-DNA-ligase-LigA	gnl|CDD|236137	PRK07956, ligA, NAD-dependent DNA ligase LigA; Validated.	0
NZ_CP051775.1|WP_075772111.1|677663_678083_-|lactoylglutathione-lyase	gnl|CDD|272886	TIGR00068, Lactoylglutathione_lyase, lactoylglutathione lyase. Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other].	2.73887e-39

Protein sequences

>NZ_CP051775.1|WP_169654682.1|682095_682866_-|hypothetical-protein
MRALPAFTLFLALAGTPALAAPQSFTADSVRVTDIVGTVQVVVDPAARAVTADVTGQQRWVDTVRLEQSGDTLSIIQDRSSQRGRIGKDDMVTVSVTLPPGTALELGNLVGDARVGDLDGTLRLRGSGAADVKVGRVAGVDLDLSGAGDVTLGEVRGPLRGSLSGAGSVEAGPVRGELSLDVSGFGDVDVDAVHGPVKVRLSGVGDVHIKGGHTPLLDANASGVGSIRFDGSADDYRVDHSGIGSVRINGKKAGRS
>NZ_CP051775.1|WP_075772113.1|679959_682083_+|ammonium-transporter
MSAEPVALVWVLAATALVFAMQLGFCLLEAGFVRAKNSINVAVKNVMDFCIAAFLFWLFGYALMFGPSWNGLVGTGGFMPGHGWPPGLLVFVLFQVMFCGTATTIVSGAVAERMGLRSYIAASALLSGLIYPIFGHWAWGGMAEGTPTGWLGRMGFIDFAGSTVVHSVGGWLALAGCLIIGPRLGRFGDGARPMASANLTLAAAGVLLLWFGWIGFNGGSALGLSESVPGILLNTVLAGCTGGLAAHGLSTLLNGKPKIEHFLNGILAGLVAITAGCNVMGTPAAACVGAVGGALVLAGERLLERFRVDDAVGAVPVHLMAGVWGTLAVALLGDPALWGTGHTRLEQLGVQAVGVLACGAYAFGLGFLLLKLLDRVHPLRIPAEDERIGLNVAEHDARSPMLELVAEMDRHRQDGQLDRPVHVEPESEVELIAAQYNRVIDKVGDQMRQQKLLLDELSHAKVEAETLNLSKSRFLATMSHELRTPLNAVIGFSHLIKDQAYGQIDPRYVEHAADIHDGGKHLLALVNDVLDYSRIEAGKFQLNEQPLDLARILRGVLRLMQPMAEAASVGLLLRVPDDLPALVGDERAVRQVLINLVGNAVKFTRPGGHVTLSAELEPDGRLRLTVADTGIGMDPRLVPKALEPFSQLENGLDKSHAGAGLGLSLVNALTRLHGGTLVIQTAPGQGTAVHVRFPRDRLPASLSKAVV
>NZ_CP051775.1|WP_075772112.1|678337_679783_+|NADP-dependent-isocitrate-dehydrogenase
MVKPVPVTVAYGDGIGPEIMEASLRVLEAGGAKLDMEVIEIGEKVYKRGHTSGIEPQAWDSLRRTKLFYKAPITTPQGGGYKSLNVTIRKTLGLFANVRPCASLHPFVATKHPTMDVVIVRENEEDLYAGIEHRQTDEVFQCLKLITRPGCERIVRYAFEYARTYGRKKVTCFSKDNIMKLTDGLFHKVFDEVGAEYPDLEKEHWIVDIGAARLADTPEVFDVIVMPNLYGDILSDVAAQITGSVGLAGSANIGEHVSMFEAIHGSAPMIAGQDKANPSGLLLSGVMMLNHVGQAEAATRIHNAWLRTLEDGVHTADIAKGGKTEATVGTRAFAQAVIDRLGEGPRHFKPVAYQGRAGGMPVPKASPTRKARKEMVGVDMFVQWSGGTPDDLAAILKRGDGKGLSLQMVTNRGVKVWPGYMPETFLVDHWRCRFMATAGSVTGLQVVDLMSRLVEAGLDVIKTETLCTFDGVAGYSLGQGQ
>NZ_CP051775.1|WP_075772111.1|677663_678083_-|lactoylglutathione-lyase
MKYLHTMVRVTNLEQSLDFYCDKLGLKEIRRMENQAGRYTLVFLAAEETPDAQVELTYNWDPEEYTGGRNFGHLAFAVDDIYATCQRLMDKGVTINRPPRDGHMAFVRSPDNISIELLQKGGSLPPAEPWKSMPNTGVW
>NZ_CP051775.1|WP_075772109.1|676503_676788_-|hypothetical-protein
MYDSGGVDGQVIWAFFMVLAIPIAAGIFTFFATRADKKRRAVAEQANRPDLLPPDAAEANQREATLPEAHPDNRPPRIEPVHLVDPAGKTARQG
>NZ_CP051775.1|WP_083699260.1|675597_676443_+|pantoate--beta-alanine-ligase
MSLPTVRTVADLRAQVAAWRGQGLRVALVPTMGALHDGHLTLVRRGRALADKVVASVFVNPTQFGPSEDFARYPRDEGGDAAKLASAGCDLLFAPDVSVMYPDGFATSIDVGPVTRRWEGAFRPGHFNGVATVVTKLLLQGLPDVALFGEKDYQQLQTIRRLVRDLDIPVSIEGVPTVREADGLALSSRNAYLTAEQRAVAASLNRVLRDVVERVRAEPGTVADAVAAGERALLAAGFDAVDYLAVVDVASLEPLERLDGPARVVCTARLGKTRLLDNFPV
>NZ_CP051775.1|WP_075772108.1|675071_675512_+|nuclear-transport-factor-2-family-protein
MNAPVPVEQAVEAYIRFYQDLRPETVNRLDRLAVPDVHFKDPFNDFRSRDRMKHVFQNMYQRVEQPRFIVRDHATSGQTAFLRWGFTFRVKGQARPLTIEGMSEVRFDHAGMVQSHIDHWDAAEQFYERLPVLGWVLRAIKKRMAD
>NZ_CP051775.1|WP_075772107.1|674292_675075_+|SDR-family-NAD(P)-dependent-oxidoreductase
MSFPIRTPMPADGVAWVTGASSGIGEHVALRLAGEGWTVVASARRADALEALAARARGPGRIVPWPVDLVDLEATRAAVAGIKAAHGPVALAVLNAGTFKPDSARTLKAEEYRQTVDINLMGTIHCLDALLPDMIGRQLGHLAIVSSVAGYRGLPRSLAYGATKAALINLAESLKLDVERYGVKVQLVSPGFIKTPLTDKNDFPMPFLMPVEEAAERLVSGLKGEGFEITFPRRFTFWLQRLRCLPYPAYFNIVRRTVPK
>NZ_CP051775.1|WP_075772106.1|671923_672682_+|hypothetical-protein
MVPALSRRGFVAGAAGVAALGWAGLPGRAGAATIPGTGQIPFSVFRNGDDAMGYHRLRFSREGDRFIVDKEIGFEVKVAFITAYRYKHTNREVWQDGRLVSLDTRTNDDGDKHWVKGQAKDGAFAVESSRGSLFAPPDIIPTSYWNIATLKAPRLLDTQRGLLMDVAIDDKGEQVIRAGGQDIPARHHTIRLLTNPPGATNAIEIWYDRNDAWVKLAFKAKGQDIGYVLDPEGLVRPGQAAEVVFGQAGARN
>NZ_CP051775.1|WP_075772105.1|671106_671838_+|SDR-family-oxidoreductase
MAAPIIVIGATGGIGEALARRLSAQKRPLFLVARNGDKLGPLAESLGAVGSAAADVLDDQALTTAVQQADSGDGIAGLAYCVGTITIKPLKAASAEDFMEAYRLNVAGAVTALKAAEKGLKAAKGSVVLFSTVAVEQGFPNHSVIASAKGAVAGLARSLAAEWAPAVRVNLVAPSLTRTPLAHPLLTSDQFAQGIANMHPIPRLGEADDQAAAAAFLLSEDASWITGQTLGVDGGRSTLRNKG
>NZ_CP051775.1|WP_169654686.1|683286_683682_-|hypothetical-protein
MIRRTTILTTAALALLGTPALAFGPQDFTARAVEVDGVFGSLEVVVDKSATKVTASVTGPERWLQEVTVRQQGDRLVVEQKDQPDGMRRWDDRKDWIAVKLTVPPGPPWRWRTSPARARWATWVPPWSWTT
>NZ_CP051775.1|WP_169654688.1|683931_684786_+|hypothetical-protein
MESFPCSKCRNPCPWDAVLCPVCNEMVGVPNVRLAERAQEKEALRKRYEEAKVAAEARGVKDRLAEFERAVSMAGAVINISIDNADSLLANDKTLYSNYRLQVDGEVRMVAELENDVKRTAVECSFFGSTAKDIRYAALSLDGVGLRSYGEISLRLKEIAVETRASLLECNTYTFVKRHPFWAGSMPEAGYRATWQGKAELAVAKCGAMIERQTTQAAFARLVLRSSGSREDDEFIEIHIHGKISLQAFEAAVLPKAGGTPTKDQKLNVIRDRLDKLGIRCTSI
>NZ_CP051775.1|WP_169654690.1|684770_687161_+|tetratricopeptide-repeat-protein
MHEHLIQGGFLVPGAGLAMVVGPDRIKVLRGVGANALDDLRPGEIGLILDSGHEVHQIPSRHRNLDWVRANLRRLGDGETLLRLLLQGLDHDLSERSRKWSIDLAEPMLTSGAAADFASRRLLGCPVPEDADLDGGSRLARSANCSRVVALYADMVRLRPALADLHDAWKATCANQTPDFPGQALRRQLIDAGIFERCARSLMARDRLAISTLPLDATLLASLIGAVQQPAKFLVGFSNMLIGKLSDKGNSVPIDSVEKEKNKDSERDDDPIISLIQNGVEEASLSQRETPRTYSGDLIEKIENQKKNIVKEFARGREERAWRFVRELVEYQLANSRPEHLAKSLCDIAARLNGGFFADAALRIYCYAREANYNEYFPLVGRAEVLKAMGRLGEALAAYEDAVAQFPNDVVPRNGRAEALKAMGRLGEALAAYEDAVAQFPNDVVARNGRAEALKAMGRLGEALAAYEDGVAQFPNDVVARNGRAEVLKAMGRLGEALAAYEDAVAQFPNDVVARNGRAEVLKAMGRLGEALAAYEDAVAQFPNDVVARNGRAEVLKAMGRLGEALAAYEDVVAQFPNDVVARTGRAEVLKAMGQLGEALAAYSDVLAAFPRQEFARNGKASTLVSIGRTQEVIEDFKAIQPITRGDWISCHILAMAYLRSEAPEEARHLLEMGAESCPFPDCHWYFAMTLAYLDVAHGFSGQAAQRLRPAMAGSPTAATVILFSHALAASGNKRDAATSLDRLGSSHVPAQVLSLKDALTKRYGLRGHGELPKAQREALDKQIAEGEFALLLEAA
>NZ_CP051775.1|WP_169654692.1|687230_687767_-|2OG-Fe(II)-oxygenase
MTTLLANPVMLPHHVYRNVMGDEFVDGLLDYVYANRDRFEVAKVGGKDEATLSVRVASILNDTGPYRALFEAKVREMLPQVTKDLGVPAVDPKRIEVQLAAHGDGAFYARHLDIQTGSQEGPRRLVSMVYYFYRLPKAFTGGALRLYALGPNAPTQDVEPARDSLLAFPAWAPTPSSR
>NZ_CP051775.1|WP_075773326.1|687870_690003_-|NAD-dependent-DNA-ligase-LigA
MPDLRATPVDTLTLDQAKEEHDALVREVRHHRELYYRKDAPEISDADYDALEKRLNLVEARFPELVTADSPTQTVGAAPGTGFRKLRHTVPMLSLDNAFAAEDVDGFIEQIVRFLNLKTVDGLEFVAEPKIDGASLSIRYEDGELVQAATRGDGTEGEDVTANVRTIAEIPNRLSGPAPKVLEVRGEVYMTRDSFFELNKRQAEAGEKVFANPRNAAAGSLRQLDARITAKRPLCFFAYTWGELSEPLAATQWDSLQRLKALGLQVPKQSTLCRSRDELLAYYEQIGKERSSLPFDIDGVVYKVNDLALQERLGFRTRTPRWATAHKFPAEQARTLLKSITIQVGRTGALTPVAELEPITVGGVVVSRATLHNADEIRRKDIRVGDTVIIQRAGDVIPQVVSVIPEARPADSAEFTFPDHCPECGSQAVREDGGVVSRCTGGLVCPAQAVERLRHFTSRNAFDIEGLGIERIQLFFDQGRIRTPADIFTLEAREEQRLDRLVTMTGFGKKSVENLFRAIEARRTIGLDRFIFALGIRQVGEATAKLLARNYRTAENWRDRMLEAAGERAAAPNQPKAELVGDAYADLCRIEQIGMSVADDIVQFFGEEHNLKALDDLLAQVTVQEFVPPRVTASPVLGKTVVFTGTLTTMGRSEAKAKAEALGAKVSGSVSAKTDYLVVGEDAGSKAAKARELGVTTLTEQEWLALIGQS
>NZ_CP051775.1|WP_075773325.1|690089_690611_-|2'-5'-RNA-ligase-family-protein
MDPIYAPLILTLRLDQASFQHFQALRQRHFPPERNFIPAHVTLFHHLPGPQVQSILADLRRTTRDTAPFPVEVFAVKSIGRGAAFYLRSRPLEELRERLADLWAPWLIPQDQQGFRPHVTVQNKVQAGEAKATLEALQRTFTPMTARGEGLLLWAYKGGPWEQLADLGFTAKP
>NZ_CP051775.1|WP_075773324.1|690659_690890_-|DUF2283-domain-containing-protein
MTTRSPIFYDPSTDSMYVRFTDGNQWDQKVDDDRDLVIDYDEHGNLVGYDIQYASQHMDVVAEAMAILRGHMPKAA
>NZ_CP051775.1|WP_075773323.1|690895_691171_-|hypothetical-protein
MRLTPTGEPKRLPPPPFWRTEYFANEVLGKPGRCRIDPLDIKRIIANPDRKRRQPDGRIQFWGWVPSLNSDVRVVTLADGETVHNAFRDRT
>NZ_CP051775.1|WP_075773322.1|691310_691571_-|DUF2283-domain-containing-protein
MTDNAALSYDPAADMLRVELRPWPAPRAGDDPASVGGEEQEPDLVVHFATDGKPWAWEIEHASRRPDLVARALAALRASHGLKDAA
>NZ_CP051775.1|WP_075773330.1|691567_691771_-|hypothetical-protein
MARPDRALVRHDDIAATLSAPTRTLRQEDGRVRYWGWVEREGRWLRVVVEPDGETVLNAFWDRGFKP

Crispr_ID: NZ_CP051775_4

• CRISPR_ID: NZ_CP051775_4
• CRISPR_location: 2075991-2076387
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 5 spacers

Consensus repeat of NZ_CP051775_4

Consensus_repeat	Method
CNGANCTGTCCNGNNCNGANCAGGANGCNGCGGAGCTGTC	CRT

spacers of NZ_CP051775_4

>4.1|2076031|50|NZ_CP051775|CRT
GTCGAGCGAGCAGGACGCGGCGGAGCTGTCGTCCAACGAACAGGACGCGG
>4.2|2076121|47|NZ_CP051775|CRT
CAGCAGCGTGACCACGGTGGAGCTGTCGACATCGGAACTCTCCTCCT
>4.3|2076208|20|NZ_CP051775|CRT
CAGTGCCGAGCAGGATGCTG
>4.4|2076268|20|NZ_CP051775|CRT
GACTTCGGAACTCTCCTCCT
>4.5|2076328|20|NZ_CP051775|CRT
GAGCACGGAGCAGGATGCCG

CRISPR arrays and Neighbor proteins around NZ_CP051775_4

CRISPR arrays

The CRISPR arrays of NZ_CP051775_4

>merge|NZ_CP051775|4|2075991-2076387|CRT
CCGAACTGTCCTCCACCGAGCAGGATGCCGCCGAGCTGTCGTCGAGCGAGCAGGACGCGGCGGAGCTGTCGTCCAACGAACAGGACGCGGCGGAGCTGTCCGGGCCGGAGCAGGATGCCGCGGAACTGTCCAGCAGCGTGACCACGGTGGAGCTGTCGACATCGGAACTCTCCTCCTCGGAGCTGTCCAGCGCTGAACAGGACGCGGCGGAGCTGTCCAGTGCCGAGCAGGATGCTGCTGAGCTGTCGAGCGCCGAACAGGACGCGGCGGAGCTGTCGACTTCGGAACTCTCCTCCTCGGAGCTGTCCAGCGTCGAACAGGACGCCGCGGAGCTGTCGAGCACGGAGCAGGATGCCGCGGAACTGTCCAGTGCCGAACAGGACGCGGCGGAGCTGTC

>NZ_CP051775|4|1|2075991-2076387|CRT
CCGAACTGTCCTCCACCGAGCAGGATGCCGCCGAGCTGTC	GTCGAGCGAGCAGGACGCGGCGGAGCTGTCGTCCAACGAACAGGACGCGG
CGGAGCTGTCCGGGCCGGAGCAGGATGCCGCGGAACTGTC	CAGCAGCGTGACCACGGTGGAGCTGTCGACATCGGAACTCTCCTCCT
CGGAGCTGTCCAGCGCTGAACAGGACGCGGCGGAGCTGTC	CAGTGCCGAGCAGGATGCTG
CTGAGCTGTCGAGCGCCGAACAGGACGCGGCGGAGCTGTC	GACTTCGGAACTCTCCTCCT
CGGAGCTGTCCAGCGTCGAACAGGACGCCGCGGAGCTGTC	GAGCACGGAGCAGGATGCCG
CGGAACTGTCCAGTGCCGAACAGGACGCGGCGGAGCTGTC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051775.1|WP_075768556.1|2082721_2083192_-|DUF2948-family-protein	unknown	unknown	gnl|CDD|371401
NZ_CP051775.1|WP_075768552.1|2086997_2088260_+|tyrosine--tRNA-ligase	unknown	unknown	gnl|CDD|235645
NZ_CP051775.1|WP_075768559.1|2080044_2080527_-|UPF0262-family-protein	unknown	unknown	gnl|CDD|235077
NZ_CP051775.1|WP_169654468.1|2063495_2064308_-|hypothetical-protein	unknown	unknown	gnl|CDD|133028
NZ_CP051775.1|WP_075768558.1|2080600_2081899_-|histidinol-dehydrogenase	unknown	unknown	gnl|CDD|234853
NZ_CP051775.1|WP_169655076.1|2085299_2085458_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075768567.1|2067859_2068930_+|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|212494
NZ_CP051775.1|WP_075768568.1|2066990_2067809_+|glucose-1-phosphate-cytidylyltransferase	unknown	unknown	gnl|CDD|133015
NZ_CP051775.1|WP_075768555.1|2083253_2084540_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl|CDD|236486
NZ_CP051775.1|WP_075769129.1|2072936_2073263_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075768553.1|2085840_2086914_-|anhydro-N-acetylmuramic-acid-kinase	unknown	unknown	gnl|CDD|236579
NZ_CP051775.1|WP_075768554.1|2084640_2085195_-|dCTP-deaminase	unknown	unknown	gnl|CDD|234753
NZ_CP051775.1|WP_169655074.1|2064304_2064541_-|glycosyltransferase	unknown	unknown	gnl|CDD|133028
NZ_CP051775.1|WP_075768564.1|2070974_2072237_+|methyltransferase-domain-containing-protein	unknown	unknown	gnl|CDD|378005
NZ_CP051775.1|WP_075768569.1|2064855_2066409_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP051775.1|WP_075768561.1|2076651_2079471_+|tetratricopeptide-repeat-containing-sensor-histidine-kinase	unknown	unknown	gnl|CDD|223715
NZ_CP051775.1|WP_075768560.1|2079598_2080036_-|arsenate-reductase-ArsC	unknown	unknown	gnl|CDD|319973
NZ_CP051775.1|WP_075768565.1|2069490_2070813_+|DUF4910-domain-containing-protein	unknown	unknown	gnl|CDD|374456
NZ_CP051775.1|WP_075768566.1|2068926_2069487_+|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein	unknown	unknown	gnl|CDD|380337
NZ_CP051775.1|WP_075768563.1|2073268_2074636_+|hypothetical-protein	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP051775.1|WP_075768552.1|2086997_2088260_+|tyrosine--tRNA-ligase	gnl|CDD|235645	PRK05912, PRK05912, tyrosyl-tRNA synthetase; Validated.	0
NZ_CP051775.1|WP_169655074.1|2064304_2064541_-|glycosyltransferase	gnl|CDD|133028	cd04185, GT_2_like_b, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	2.95551e-18
NZ_CP051775.1|WP_169654468.1|2063495_2064308_-|hypothetical-protein	gnl|CDD|133028	cd04185, GT_2_like_b, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	1.09404e-27
NZ_CP051775.1|WP_075768558.1|2080600_2081899_-|histidinol-dehydrogenase	gnl|CDD|234853	PRK00877, hisD, bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed.	0
NZ_CP051775.1|WP_075768567.1|2067859_2068930_+|SDR-family-oxidoreductase	gnl|CDD|212494	cd08946, SDR_e, extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	2.84567e-60
NZ_CP051775.1|WP_075768564.1|2070974_2072237_+|methyltransferase-domain-containing-protein	gnl|CDD|378005	pfam08484, Methyltransf_14, C-methyltransferase C-terminal domain. This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.	7.21542e-80
NZ_CP051775.1|WP_075768555.1|2083253_2084540_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl|CDD|236486	PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated.	0
NZ_CP051775.1|WP_075768553.1|2085840_2086914_-|anhydro-N-acetylmuramic-acid-kinase	gnl|CDD|236579	PRK09585, anmK, anhydro-N-acetylmuramic acid kinase; Reviewed.	6.92816e-173
NZ_CP051775.1|WP_075768554.1|2084640_2085195_-|dCTP-deaminase	gnl|CDD|234753	PRK00416, dcd, deoxycytidine triphosphate deaminase; Reviewed.	1.53959e-107
NZ_CP051775.1|WP_075768559.1|2080044_2080527_-|UPF0262-family-protein	gnl|CDD|235077	PRK02853, PRK02853, hypothetical protein; Provisional.	2.35559e-93
NZ_CP051775.1|WP_075768568.1|2066990_2067809_+|glucose-1-phosphate-cytidylyltransferase	gnl|CDD|133015	cd02524, G1P_cytidylyltransferase, G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose. Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.	2.81765e-147
NZ_CP051775.1|WP_075768556.1|2082721_2083192_-|DUF2948-family-protein	gnl|CDD|371401	pfam11164, DUF2948, Protein of unknown function (DUF2948). This family of proteins with unknown function appear to be restricted to Proteobacteria.	2.54976e-53
NZ_CP051775.1|WP_075768566.1|2068926_2069487_+|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein	gnl|CDD|380337	cd00438, cupin_RmlC, RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production. RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	2.22303e-74
NZ_CP051775.1|WP_075768560.1|2079598_2080036_-|arsenate-reductase-ArsC	gnl|CDD|319973	cd16345, LMWP_ArsC, Arsenate reductase of the LMWP family. Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).	2.00156e-40
NZ_CP051775.1|WP_075768565.1|2069490_2070813_+|DUF4910-domain-containing-protein	gnl|CDD|374456	pfam16254, DUF4910, Domain of unknown function (DUF4910).	0
NZ_CP051775.1|WP_075768561.1|2076651_2079471_+|tetratricopeptide-repeat-containing-sensor-histidine-kinase	gnl|CDD|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	7.34425e-34

Protein sequences

>NZ_CP051775.1|WP_075768563.1|2073268_2074636_+|hypothetical-protein
MARGGLPGEAVPWPSHDDWRKRLAWRQPFEKAEAEESIRAAYEAAGLPPPRTILWAGGPREARGILSRTGWRRAGPWLLMLVALLAIVASTLGLPAREGVAAVELPRGAFVVLGLAFVAFWTFALMLSGALQEAKSPLVLVGVPVAIAGALMAVGLLSSGPMVQVSPLAMLGGLLALPASILLAAQRGESRVGQPFLFGRSVAPRLSRTFHVLLDKARPAIRPRPYGLDLGDRLAAFVRLLAIACPPSFETPIAFYAVDRLVRVAPDPKAGGDAERKLAAFTDLVYRVDGLWAFAKVAVALEPPSEVHLDEFGRFHRTDGPALCWKDGSTLFAVDGRFAADPAILLGTEELTIFHIRQEPDPGIRRALLQTYGPDKVMRELGRKVGQDGTGELWRVDDFDGEPLVMVRVINSSPEPDGSYKPYWLRVPPATPSAHAGVSWTFGLVPSRYRPQVET
>NZ_CP051775.1|WP_075769129.1|2072936_2073263_+|hypothetical-protein
MPVQFRQGDVLITAVDGLPPTALPVRPDEGRVVLAYGEVTGHAHAMSPNRVVMFRDDGGGRSYIQVLGDQPTALSHEEHHTIEVPPGTYEVVRQREYEPKARPRAIAD
>NZ_CP051775.1|WP_075768564.1|2070974_2072237_+|methyltransferase-domain-containing-protein
MSRITECRSCGSPNLTPILDLGAQPLANALVEPDKAGQPEELFPLDVCFCGTCALVQVTETVPPEVLFGRDYPYFSSFSPALLAHSRSHALELIERRKLGPDNLVAEVASNDGYLLRNFAAAGIPVLGIDPASGPAAAARAIGIPTVEDFFNRTLGERLAAEGKAADVILAKNVLAHVDGINEFVAGFAALLKADGIAEFEFPYLRDLIEECAFDTIYHEHVFYYSLTALEPLFARHGLHLNDVVRLDIHGGSLRLTVSKNPGKSERLSALMAEERALGMHEARYYQDFARRVAGVKEALLALVDSLRGQGKRIAAYGAAAKGATLLNYAGLTAKELDFVVDRNTHKQGKLMPGAQLPIRPVEALLEERPDYLVVLAWNFADEIMEQQRAYAEAGGTFILPIPEPHLARPQAVEPGIAAA
>NZ_CP051775.1|WP_075768565.1|2069490_2070813_+|DUF4910-domain-containing-protein
MDGSFAKPPLTGEGMHALAAELYPICRSLTGDGVRRTLARVAREVPLEIVEVPTGTPVLDWEVPREWNIRAAWIETLDGRRVVDFADHALHILNYSRPIDMVVSREALAKHVHTLPQQPDLIPYRTAYYADTWGFCMAHRTWEAMTDPEYRVVVDSTLEPGRLTYGELHVPGTTEGDILVSLHVCHPQLANDNLSGLVVATALAQRLLNGPKRRLGVRFVFLPATIGAITWLARNEAAVDRVRHGLTLSCIGDPGPFHYKRSRREDAAIDRAVAHVLAARGVEHGILPFSPYGYDERQYCSPGYDLPVGCFMRGVHGTFPEYHTSADNLDFIRPEALAESLSVLAEVLDLLDADVTYARTDGGKGEPQLGRRGLYRQIAGQKDQGGLDQMAVLWVLNLADGKHRLLDMAERARMPFAKVRAAARACEEAGLLEVVPDTRR
>NZ_CP051775.1|WP_075768566.1|2068926_2069487_+|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein
MKFEDLPIHGAKLVRLTVHRDERGGFARTWCADSFREAGIDFTPVQGNSSVTHGRGTLRGMHFQRAPQQDAKVVRLTSGRVHDVIADLRPDSPTFRQSFAMELSAEAGVMLYLPPGLAHGFQLLGEEAGVEYLMGAAYVPDLYDGCRFDDPTLGLAWPLPVERISPKDLSWPPLAGRMPGFGVSAG
>NZ_CP051775.1|WP_075768567.1|2067859_2068930_+|SDR-family-oxidoreductase
MKVLVTGADGYIGAVLTPYLMKRGYDVVGLDAGFYRGGWLFDDLEDRPRVITRDIRRVTPKDLEGFDAVVHLAELSNDPLGAHNPEITYDINFRGSMNVAQSAKKAGVPRFVYASSCSVYGAGNDDIKTEESAPNPQTAYAECKVRCEQGLAELVEDSFVTTCLRNATAFGASPRMRFDIVLNNLSGLAWTTGKIAMTSDGKPWRPLVHVLDICQAIECTLRAPKEDVKGQIFNVGDERQNYRVSEIAEMVAAAFPGCTISFGAPGPDNRSYRVDFSKIRKHLPDFRCQWSAERGAAQLYQVFSRIGMTREMFEAPAFTRLNALKLLVGSGQLDPLFHWLDMPETPAAAASRQAAE
>NZ_CP051775.1|WP_075768568.1|2066990_2067809_+|glucose-1-phosphate-cytidylyltransferase
MKVVILAGGYGTRISEESQVRPKPLVEIGGRPIIWHIMKIYSHYGFNDFVILCGYKGEMLKQYFRDFMLTTGDVVFDLAQNSMKIVPREVEPWRVTLVDTGQETMTGGRLKRVAHLLDDTFCLTYGDGVADIDIGTLVRHHKEGGRWATVTAVEQPGRFGALHLLPHDPIVHGFREKGPEDGGLINGGFFVLEPKVIDFIDNDSTVWEREPLERLVAANQLQAFRHHGFWQPMDSLRDKMVLENLWKGGDAPWKVWGKEPAMPAAAPRMRAV
>NZ_CP051775.1|WP_075768569.1|2064855_2066409_+|hypothetical-protein
MPTPPDAGPIHRRQFIIDTDRHREAEGWMAERLGNGLWLSHCPRLRVRRLPDGQGGTALLLGTPLLADPDQDDFQLSPARAAQDLADAAYAWSGRWTLVTGDWLLADSTNLASIFYQPGPGGRTLVSTSLALIHGLRPELPVLKRRIGWYGMNWFPPPHSRIVGVRKLLPDQALRLSDGTVHRVSRWNPERFAGKPVGALAEMLLRSLGQCFKSAASVQDRLALALTAGLDSRTLLAAALEVGVRVDTMIQLFPLMPLADKVLPPEIARHCGLRWDAVPRGAFNLSRQRRFDAHTFRNMGDADRSFYARGMYDWMGPGTALVRGGGFEVGRERMEDRLRGLGWEEALADPDGLLESYGDFGSRPWLRTQMRDWLRWAVDGPRPYGLGNQFYRDQRLAGWLSAAEQSSDMLEGCALQVVNCGYHHDLMLAAPLEDRRTGTVQRQAIALAGRGLAEFPVNPPMETRMQRRLQRWSLKGRRTAGELRNMAMGLLDGPAVGVTPVRTAATATSPPRAAEGR
>NZ_CP051775.1|WP_169655074.1|2064304_2064541_-|glycosyltransferase
MSNQVAAVVVTYNRKAILCQCLAAIHGQTRRPDRIIIMDNGSADGTYEELAAQGLLTADTVFVRFPRTGAPPGPSGRA
>NZ_CP051775.1|WP_169654468.1|2063495_2064308_-|hypothetical-protein
MSQAYADGADWIWVMDDDIIPDPTALEVLLSTAGTEFPDPEKLAFLSSRVRGPEGQPMNTPEVAWRAALHDEYATWEEKLDLGLVQIRRASLTSTLFPRSTLRDVPPSAPDFWMWGEDSDFTMRATKNRRAYLVSGSKVVHLRAISRPLHPLTETDPSRLRRMFFMYRNLVYLRRHHYPPAEVLMSLIDGVRLTVKAVLSGKFAAARVVFTGTLAGFWFRPSIPATAEPSLMREAEVLHAEGQGLYRPQEVGETGAAPPAFTRAAGAYAR
>NZ_CP051775.1|WP_075768561.1|2076651_2079471_+|tetratricopeptide-repeat-containing-sensor-histidine-kinase
MVDLFGLPARVAELEGRCGRQDGDTAGRLSDLLHLAWYLRQRDTQRCLSLLGEVERLLDMAPLSEDTLALARARASLTRAECVARLHVDLGAAEGLVAAARAGFAALADPVGEGDSCFCSSDIALLRGDMPAATRRLEEARQLYRRGDDPVRAAIADAWLGRLESYGTLEQAEVRWTAPLREANTLEHPAVRAHVACFLGGIAFQRSDFTGCITHWQEAFDNAVVAGCRWLSITLAATTGAAYANLNDLPTALEWKEKAFALAEPTGWPEALGTALSSMAETTTSLGHHARARHLFEEALTYLAKVQGVRRYVITCIAYGDLCLAMGDAGTALPWYEKACTGAVRLGHPDTEHSAMRGMAAALLALDRLDEAKAAAERALSLFADRGDRFHQIRVLQVLAGIHRAQGDVRAAAGLLERAVAIGEEMAGYQLPPDLFAELSHDQELAGDLRKALAYERRARDALGNLYERQGRNRVQAMQVRFDTERARADAEHHRLLASAEAARAAALDHANTTLELLGRIGQEITATLDSESVFQALYRHIGDLLHAPSLFIGLLDKEGGKLDVRFRMEDGRRLPPRHDLLTSDTLAAQAVRENREIHKDFREDEPRLTIPGTRPMRTALYRPLVVGERVLGVLSVQSDRESAYGPRELQVFRTLCAYGAIALANAEAYRQLDRAVTDLRDALGRLVQQEKMAALGQLVAGVAHEVNTPLGVTLSAVSLLHDSMRQMQETLNGGVLTRTSLAEHLQTGVELAGLAQRNVVRAADMVRSFKEVAVDRSNDDRRIFDLGDYLKELLGLVRPRLVQAGVRVEFDGAPPIQMDTFPGALAQVVTNLLANVADHAYPPGKAGTARVTADALPDGGVEITVADDGAGIPADILPKVFDPFFTTRRAAGNMGLGLHVAFNQVTQRLRGSIEVESQPSQGTAVRVRIPADVMAAAP
>NZ_CP051775.1|WP_075768560.1|2079598_2080036_-|arsenate-reductase-ArsC
MAEIHPTRISSVLFACTHNAIRSPMAEGLLKKLQGTRLYVDSAGVREGDQDPFVTAVMAELGVDMSRHRCKTFDQLEDTSFDLVISLSPEAQHRAVEMTRTMACDVEFWHTFDPSIIEGTRETRLDAYRQVRDALMRRLKERFPA
>NZ_CP051775.1|WP_075768559.1|2080044_2080527_-|UPF0262-family-protein
MTHQPHHRVTHVQLVEKHVVRRNPEVEHERAVALFDLLEENRFRLAELPDQGPFRLYLSIEDNRLVFDVRGEDDGEVAKVVLPISPFRTIVRDYFLICDSYYKAIKTAAPSQIEAIDMGRRGLHNEGSELLRERLSGKIDLDLQTARRLFTLICVLHIRG
>NZ_CP051775.1|WP_075768558.1|2080600_2081899_-|histidinol-dehydrogenase
MPLRLSTADPRFEDGFRGLLHAKRETAEDLNAAVADILADVRARGDAAVLDYTKRWDRLDLTADTLRVTAAEVDAAVSACDPATLDALHLAAARIEDFHRRQVPDRQDYVDAAGVRLGARWTPVGAVGIYVPGGTAAYPSSVLMNAIPAKVAGVPRIAMVVPSPDGVLNPLVLAAARASGVTEIYRIGGAQAVGALAYGTETIAPVDKITGPGNAYVAAAKRQVFGTVGIDMIAGPSEILVVADGQNDPAWIAADLLSQAEHDTSAQSILITDDAAFADAVARAVELHLQTLPRTEIAGQSWAEHGAIILVDSLSQAVPLVDRLAPEHLELAVADPDALAAEIRNAGAIFLGRYTPEAIGDYVAGPNHVLPTARSARFSSGLNVLDFMKRTTLVGCTPDSLRAIGPAAVTLAEAEGLGAHALSVAIRLGQGT
>NZ_CP051775.1|WP_075768556.1|2082721_2083192_-|DUF2948-family-protein
MATGLKLRAQDADDLKVVSAMMQDAIIPICDVGYLPDEQAFVLVANRFKWECAERNGAKAATGPTPDEDCGFERTNCAIRFHNITRASYRNLDLRDRTQMLSLLSIEPGEGAVLLHFSGGHCVRLETAALDVRLEDIGEPWPTGARPCHDGQAATA
>NZ_CP051775.1|WP_075768555.1|2083253_2084540_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MDKLRIRGGRTLKGEIAISGAKNAALPLLAACLLTEETLTLRNLPHLADIVTMSNLLAQHGVGVVVNGKGTSYEGRDVHLDAANITNLTAHYDLVRKMRASVLVLGPLVARFGEAKVSLPGGCAIGPRPVDLHIKGLQAMGAEIDIEGGYILAKAPKGGLKGAEIVFPQVSVGATENLMMAAALADGETTLVNAAREPEIGDLARCLIAMGADIDGVGSDRLRIRGKKTLHGATHAILPDRIEAGTYAMAAAITGGDLELLGARLDDLRAMAKILAGAGVTFTETERGLRVARTGDLIGVDAMTEPFPGFPTDLQAQMMALMCVAKGASMITETIFENRFMHVPELARMGANITVHGASALVRGVPKLTGAPVMATDLRASVSLVLAGLAAEGETVVNRIYHLDRGYEHLEEKLIACGADMERLRDAS
>NZ_CP051775.1|WP_075768554.1|2084640_2085195_-|dCTP-deaminase
MPIMPDTWIRDMATTKGMIEPFTEAQKREGVISYGLSSYGYDARVADEFKIFTNVDNAVVDPKRFDETSFVDRKTDVCVIPPNSFALARTVEYFRIPRDVLVVCLGKSTYARCGLIVNVTPLEPEWEGHVTLEISNTTPLPAKVYANEGLCQFLFFQGATPCEVSYADRAGKYMGQKGVTLPRL
>NZ_CP051775.1|WP_169655076.1|2085299_2085458_-|hypothetical-protein
MTTPPKKSPPQKDDRKDRLAQALRDNLRKRKEQERGREVTDPAPVTPTEGAA
>NZ_CP051775.1|WP_075768553.1|2085840_2086914_-|anhydro-N-acetylmuramic-acid-kinase
MPDTTLAIGLMSGTSLDGIDAALLRTDGRGVAEAGAFLTVPYRRAFRDRLRAVLGGQGDVAGVERELTELHAAAVDSLLGMAGVEREEVGLVGFHGHTILHAPEQRRTWQIGDGALLATLTGIPVVNDFRSADVAAGGQGAPLVPLYHQALATDLDRPLAVLNIGGVANVTWLGAGELDVAAFDTGPGNALVDDWVLRHTGDPFDDGGRIAAKGTVDEGILAALLAHPYFTAPFPKSLDRDAWSADAVAGLSLEDGAATLTAFTAASIAAAAEHLPSRPARWLVTGGGRRNDTLMWMLARRLRAPVSPVDAVGWNGDSLEAEAFAYLAVRSRLGLPLSVPGTTGVPQPMTGGRYWAA
>NZ_CP051775.1|WP_075768552.1|2086997_2088260_+|tyrosine--tRNA-ligase
MTTPLPSSVKSDFLRVMLERGYYHQATDVEALDKALGAGGLVAYNGYDATADSLHVGHLLPTMMQRWLQKCGGKPILLMGGGTTKIGDPSGRDETRQLLTNEAIDANIAKIKTAFDRLFDFGPNGALLVNNADWLDRLEYIPFLRDVGRHFTINRMLTFDSVRLRLDREQPLTFLEFNYMILQAYDFVELNRRYGCVLQTGGSDQWGNIVNGVDLGRRIANKDLFGLTCPLLTTASGAKMGKTAAGAVWLNSDRLSDWDFWQYWRNTEDADVGRFLKLFTELPLDEIARLEALQGAEINEAKKILATEITKLVRGPEAAEAAAETARRTFEQGALAEGLPTVEVAGAELADGVTVFSLLARAGLVASNAEARRQIKQGAVKLNDQPVSDEFAKVTAADLVSDGAAKLSLGKKKHALVRAS

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP032340	Azospirillum brasilense strain MTCC4038 plasmid p1, complete sequence	645470-645501	4	0.875
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP012915	Azospirillum brasilense strain Sp 7 plasmid ABSP7_p1, complete sequence	1486914-1486945	4	0.875
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP025613	Niveispirillum cyanobacteriorum strain TH16 plasmid unnamed1, complete sequence	141885-141916	7	0.781
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	LN997843	Streptomyces reticuli genome assembly TUE45, plasmid : II	697558-697591	7	0.794
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NC_012527	Deinococcus deserti VCD115 plasmid 1, complete sequence	59319-59350	8	0.75
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NC_008826	Methylibium petroleiphilum PM1 plasmid RPME01, complete sequence	110725-110756	8	0.75
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP017563	Paraburkholderia sprentiae WSM5005 plasmid pl1WSM5005, complete sequence	467387-467418	9	0.719
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	5373301-5373332	9	0.719
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP014799	Salipiger profundus strain JLT2016 plasmid pTPRO3, complete sequence	6451-6482	9	0.719
NZ_CP051775_1	1.3|485128|32|NZ_CP051775|CRISPRCasFinder	485128-485159	32	NZ_CP004394	Celeribacter indicus strain P73 plasmid pP73A, complete sequence	13735-13766	9	0.719
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	JF957056	Mycobacterium phage Thora, complete genome	63734-63767	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279882	Mycobacterium phage Sophia, complete genome	63203-63236	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	KY965066	Mycobacterium phage BlackStallion, complete genome	63611-63644	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MN096366	Mycobacterium phage AbsoluteMadLad, complete genome	63699-63732	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279855	Mycobacterium phage Haleema, complete genome	63311-63344	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279873	Mycobacterium phage QueenBeane, complete genome	63546-63579	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MH651186	Mycobacterium phage Podrick, complete genome	63302-63335	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MH051264	Mycobacterium phage Cobra, complete genome	63772-63805	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MF919503	Mycobacterium phage Dingo, complete genome	62954-62987	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK112527	Mycobacterium phage Altwerkus, complete genome	63075-63108	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	NC_028691	Mycobacterium phage Apizium, complete genome	62903-62936	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279878	Mycobacterium phage Samaymay, complete genome	63546-63579	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK112551	Mycobacterium phage Riggan, complete genome	63727-63760	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279843	Mycobacterium phage CamL, complete genome	63546-63579	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	KM408320	Mycobacterium phage Lasso, complete genome	63472-63505	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK112555	Mycobacterium phage Zelda, complete genome	63835-63868	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	NC_028803	Mycobacterium phage OSmaximus, complete genome	64070-64103	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279870	Mycobacterium phage Omniscient, complete genome	64093-64126	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MG925346	Mycobacterium phage LeeLot, complete genome	63816-63849	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279859	Mycobacterium phage Kwadwo, complete genome	63231-63264	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	KP027197	Mycobacterium phage FluffyNinja, complete genome	63613-63646	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279897	Mycobacterium phage Bishoperium, complete genome	63761-63794	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MT310868	Mycobacterium phage Telesworld, complete genome	63357-63390	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	KC576784	Mycobacterium phage ShiVal, complete genome	63251-63284	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	GU247133	Mycobacterium phage Fang, complete genome	63743-63776	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MN369744	Mycobacterium phage Beaglebox, complete genome	63314-63347	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MG925356	Mycobacterium phage OliverWalter, complete genome	63690-63723	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	JF704109	Mycobacterium phage Oosterbaan, complete sequence	63630-63663	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MK279894	Mycobacterium phage YouGoGlencoco, complete genome	63504-63537	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MN585967	Mycobacterium phage Kloppinator, complete genome	63376-63409	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	GQ303259	Mycobacterium phage Colbert, complete genome	62670-62703	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MH479914	Mycobacterium phage FugateOSU, complete genome	64372-64405	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	MF919528	Mycobacterium phage Phunky, complete genome	63273-63306	10	0.706
NZ_CP051775_3	3.2|683072|34|NZ_CP051775|CRISPRCasFinder	683072-683105	34	KJ538723	Mycobacterium phage KingVeVeVe, complete genome	62940-62973	10	0.706
NZ_CP051775_3	3.3|683129|34|NZ_CP051775|CRISPRCasFinder	683129-683162	34	NZ_LT703506	Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 2	299091-299124	10	0.706

1. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP032340 (Azospirillum brasilense strain MTCC4038 plasmid p1, complete sequence) position: , mismatch: 4, identity: 0.875

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
caggcgccgcgcaggtcggccccggacaggtc	Protospacer
  ***** **************.*********

2. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP012915 (Azospirillum brasilense strain Sp 7 plasmid ABSP7_p1, complete sequence) position: , mismatch: 4, identity: 0.875

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
caggcgccgcgcaggtcggccccggacaggtc	Protospacer
  ***** **************.*********

3. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP025613 (Niveispirillum cyanobacteriorum strain TH16 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.781

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
atggcgcggcgcaggtcggcggtggaggcgcg	Protospacer
********************  **** . *. 

4. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to LN997843 (Streptomyces reticuli genome assembly TUE45, plasmid : II) position: , mismatch: 7, identity: 0.794

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
ctgctccacaggcccgtcgacccgggccacaccg	Protospacer
*  **.************ *********** .* 

5. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NC_012527 (Deinococcus deserti VCD115 plasmid 1, complete sequence) position: , mismatch: 8, identity: 0.75

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
gtcgcgcggcgcacgtcggcgctggactcctt	Protospacer
.* ********** ****** ******   *.

6. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NC_008826 (Methylibium petroleiphilum PM1 plasmid RPME01, complete sequence) position: , mismatch: 8, identity: 0.75

atggcgcggcgcaggtcggccctg-gacaggtc	CRISPR spacer
gtggcgcggcgcaggtcgcccttgtcgccgat-	Protospacer
.***************** **.**  .* *.* 

7. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP017563 (Paraburkholderia sprentiae WSM5005 plasmid pl1WSM5005, complete sequence) position: , mismatch: 9, identity: 0.719

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
ggtgcgcggcgcaggtcggcctgggaccagga	Protospacer
.  ******************. **** .*  

8. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 9, identity: 0.719

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
tggtcgcggcgcaggtcggccatgaactcgat	Protospacer
  * ***************** **.**  * .

9. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP014799 (Salipiger profundus strain JLT2016 plasmid pTPRO3, complete sequence) position: , mismatch: 9, identity: 0.719

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
attgcgcggcgcaggtccgccctctcggagtt	Protospacer
** ************** *****    ..**.

10. spacer 1.3|485128|32|NZ_CP051775|CRISPRCasFinder matches to NZ_CP004394 (Celeribacter indicus strain P73 plasmid pP73A, complete sequence) position: , mismatch: 9, identity: 0.719

atggcgcggcgcaggtcggccctggacaggtc	CRISPR spacer
gcggcggggcgcaggtcggtcctggcggggcg	Protospacer
..**** ************.*****  .**. 

11. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to JF957056 (Mycobacterium phage Thora, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

12. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279882 (Mycobacterium phage Sophia, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

13. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to KY965066 (Mycobacterium phage BlackStallion, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

14. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MN096366 (Mycobacterium phage AbsoluteMadLad, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

15. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279855 (Mycobacterium phage Haleema, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

16. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279873 (Mycobacterium phage QueenBeane, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

17. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MH651186 (Mycobacterium phage Podrick, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

18. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MH051264 (Mycobacterium phage Cobra, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

19. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MF919503 (Mycobacterium phage Dingo, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

20. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK112527 (Mycobacterium phage Altwerkus, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

21. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to NC_028691 (Mycobacterium phage Apizium, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

22. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279878 (Mycobacterium phage Samaymay, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

23. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK112551 (Mycobacterium phage Riggan, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

24. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279843 (Mycobacterium phage CamL, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

25. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to KM408320 (Mycobacterium phage Lasso, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

26. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK112555 (Mycobacterium phage Zelda, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

27. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to NC_028803 (Mycobacterium phage OSmaximus, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

28. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279870 (Mycobacterium phage Omniscient, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

29. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MG925346 (Mycobacterium phage LeeLot, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

30. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279859 (Mycobacterium phage Kwadwo, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

31. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to KP027197 (Mycobacterium phage FluffyNinja, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

32. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279897 (Mycobacterium phage Bishoperium, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

33. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MT310868 (Mycobacterium phage Telesworld, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

34. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to KC576784 (Mycobacterium phage ShiVal, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

35. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to GU247133 (Mycobacterium phage Fang, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

36. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MN369744 (Mycobacterium phage Beaglebox, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

37. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MG925356 (Mycobacterium phage OliverWalter, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

38. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to JF704109 (Mycobacterium phage Oosterbaan, complete sequence) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

39. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MK279894 (Mycobacterium phage YouGoGlencoco, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

40. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MN585967 (Mycobacterium phage Kloppinator, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

41. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to GQ303259 (Mycobacterium phage Colbert, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

42. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MH479914 (Mycobacterium phage FugateOSU, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

43. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to MF919528 (Mycobacterium phage Phunky, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

44. spacer 3.2|683072|34|NZ_CP051775|CRISPRCasFinder matches to KJ538723 (Mycobacterium phage KingVeVeVe, complete genome) position: , mismatch: 10, identity: 0.706

caccttcacaggcccgtccacccgggccacctcc	CRISPR spacer
cggtgacacaggcccgtcgacccggcccacgatc	Protospacer
*. .  ************ ****** ****  .*

45. spacer 3.3|683129|34|NZ_CP051775|CRISPRCasFinder matches to NZ_LT703506 (Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 2) position: , mismatch: 10, identity: 0.706

aacctccagttggccgctggtccggccagtgcgg	CRISPR spacer
cgcctccagtcggccgctggcccggcgcagccag	Protospacer
 .********.*********.*****  .  *.*

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site
DBSCAN-SWA_1	1394238 : 1400426	8	uncultured_Mediterranean_phage(83.33%)	protease	NA

Sequences of DBSCAN-SWA_1

Nucleotide sequences of DBSCAN-SWA_1

>NZ_CP051775|1394238:1400426|DBSCAN-SWA
ATTGTCCGGTAAGGCACCCCTGGCCATCGCCTTCGGTTGCGCCGGAACCAGCCTGACCCCCGGGGAGCGCGCGCTGTTCCGGGAGGCTGATCCGCTGGGCTTCATCCTGTTCCGCCGGAACGTGGACAGCCCCGACCAGGTCCGGCGGCTGGTGGCGGAGATGCGCGACAGCGTCGGCCGCGACGCGCCCGTGCTGATCGACCAGGAAGGCGGCCGGGTGGCCCGCCTGCGCCCGCCGCACTGGCCCGCCCTGCCGGCGGCGCGCGCCTGCGGGGTGGTGGCGGAACGGGACCCGATACGGGGGACGCGTGCGTCGTGGCTGCATGGCCGGCTGCTGGCCCACATGCTGGCGGACCTGGGCATCGACGTGGACTGCGCCCCCGTGGCTGACGTGCCGGTGCCCGGCGCCCATGACGTGATCGGCGACCGCGCTTTCGCGGGGGAGCCGGGGCTCGTGGCCACCCTCGCGCGGGCCCAGGCGGAGGGGCTGATGGCTGGCGGGGTGCTGCCGGTGATGAAGCACATCCCCGGCCATGGCCGCGCCCATGTGGACAGCCACAAGGAACTGCCGGTGGTCCATGCCGACCGGATCGACCTGGAGCGGCAGGACTTCGCCCCGTTCCGCGACCTGGCCGACCTGCCGCTGGGCATGGTGGCACACGTGGTCTACACGGAAGTGGACCCGCACCGGCCCGCCAGCACCTCCAATACCGTGATTTCTGAGGTGGTCCGCGGCTGGATCGGCTTCCGGGGGCTGCTGTTCAGCGACGACATCGGCATGCAGGCCTTGAGCGGCACAGCCGGCCAACGGGCCGCGGCGGTGCTGGCCGGCGGCTGCGACGTGGCGCTCCATTGCGGGGGTGACTTCGCGGAGATGCAGGACGTGGCCGCCAATGGGCGGGCGCTGACCCCGGAGTCGCTGGCCCGCTGGCAGGCGGCAAAGGCGCTGGTACGGGCGCCTGAGCCGGCCGACGCACAAGAGCTTCGGGCCGAGTTGGACGCGATCCTGGCGGGTGGGGTGGCCTGAGATGGACGAGATTTCCGGCTTCATCCAGGCCCTGACCGTGGTGCTGCTCCCCGGGCTGGTCGCCATCACCTTCCATGAGGCGGCCCATGGCTATGTGGCCAAGCGCTTCGGGGACAACACGGCCTACATGCTGGGCCGGGTGACCTTCAACCCGCTGAAGCACATCGACCCGTTCGGCACCATCATCCTGCCCCTGATCATGTTCTTCACCACAGGGTTCCTGTTCGGCTGGGCCAAGCCCGTGCCGGTGGATTTCCGGAACCTGCGTGACCCGAAGCGGGACATGATCTGGGTGGCCCTGGCCGGGCCCGGTGTGAACATCTTCCTGGCCTTGATGTCCGCCTTCCTGCTGCACACCGTGCCGCTGATGCCGGAGGCCGCGCAGGAGTGGTTCCACCAGAACCTGCTGTTCTCCGTCCAGATCAACGTGTTGCTGGCCGTCTTCAACATGCTGCCGCTGCCGCCGCTGGATGGCGGGCGGGTGGTGACGGGGATCCTGCCCGGCCGGCTGTCCTACCAGTTCGCCAGCATCGAGCGCTATGGCATGCTGATCCTGCTGGCGGCCGTGTTCCTGGTGCCCTTCACTGCCCAGCAGCTCGGGTACAGCTTCAACCCGCTGTTCTATGTGCTGCTGCCGCCCATGGACTTCATCACGGACCTGATCGTCCGCGTGGCCGGGCTGACCTGACCTCCCATGGCGGACCCGTTGAGCCCAGACCCGTTCGACCAGCCCGTGCGCGACGGGACGCCGGAGGTGGTGGCCGACGCGCCGCTGCTGCTGGCCATCGACGGTTACGAAGGTCCCATCGACCTGCTGCTGACCCTGGCGCGCGACCAGAAGGTGGACCTGACCCGGGTCAGCATCCTGCAACTGGCCGACCAGTACCTGTCCTTCGTGGAGACGGCCAAGCGCCTGCGCCTGGAGTTGGCGGCGGACTATCTCGTGATGGCGGCCTGGCTGGCTTACCTGAAGTCCCGCCTGCTGCTACCCGAGCCGGAGACGGAGGAGCCCAGCGGCGAGGAGCTGGCCGCCGCCCTGGCTTTCCAGCTCCAGCGGCTGGAGGCCATGCAGGGCGTGGCCGCCCGACTTCTGGCCCGGCCCCGGCTGGGCCGCGACGTCTTCGCCCGCGGCGCGCCGGAGGACATGCCGGTGCTGGAGAAGCGCATCCATGAGGTGTCGCTCTACGACCTGCTGAAGGCCTATGGCGAGCACAAGCAGCGCCAGATGAAGCAGGGCCCCCTGACCATCGCCGCCACCGAGCTGTATTCCATTGAGGACGCGGTGGCCCGGGTGGAGGCCATGCTGGGCAAGCTGCCGAGCTGGACCAAGCTCAGCAGCTTCCTGCCCGCTGGCTGGCGCAGCGGCGGGGTGAAGACCCGCTCCGCCCTGGCCAGCACCTTCGTCGCCACGTTGGAGCTGGCCAAGGCCGGCCGGCTGGAGATTCGCCAGGAGGGGGCGTTCGGCCCCATCTTCCTGCGCACCCCGCAATCCCAGGAAGGGGGCACCTGACCCATGCCCATCCCCGACGACCGCAACCAGCAGCTCCGCCTCGTGGAGGCCATCCTCTTCGCCAGCGCCGACCCGGTGCCGGAAGAGGCGCTCCAGGCCCGTTTCGGGGAGGGGGTACAGGTGCGGGAGCTGCTGCTGGACCTGCAGGCGCTGTATGAGCACCGTGGCGTGAACCTGTCCGCCATGGGCGGCCGCTGGGCCTTCCGCACCGCCCCCGACCTGGGCGAGCACTTGCGCAGTGAGACGGAAGTGACGGCCAAGCTGTCCCGCGCCGCCATCGAGACCCTGGCCATCATCGCCTACCACCAGCCGGTGACCCGGGCGGAGATCGAGAGCATCCGCGGCGTGGCCACCAGCAAGGGCACCCTGGACATCCTGATGGAGGCGGGCTGGATCAAGCCGGGCCGCCGGCGGGAAACGCCGGGCCGGCCGGTCACCTGGGTGTCCACGCCCCATTTCCTGGACCATTTCGGCCTGGAGTCCCTGCGCGACCTGCCGGGGGTGGAGGATCTGCGCGCCGCCGGCCTGCTGGACAGCCGTTCCGGCATGGGTCCGCTGGCGCCGGTCGCCCTACCGGCGGAGGCCGAGCCGGAACCCGCCGAGGGCTGAGGGCGGGGGCCGGCGCAACAGGCCCATTGTCGCACGCGACTGATAATGGTTTGCATTCTGCGCTGGGCGTGACTTAATGGGCGGATATGGCCCCGCTCCCCGGGGCGCGATGTGGGTTCGTCGGCCATCATGGATGCGACGTTTCTGTCTCCCCCCGTTCCCGTTCTCCCCTCTGGCGCAGCCTGTCCGCGAGGGTGGAGGCTGCTGCCCCGGCCAAGGTCCCGGCTCGGGAACGTGGCAGCCCGGTGGACGCCCTGGGCCCCCGGCAGGCGCCGGCCGCGGCGGAGCTGCGGCCTGCCCTGGCTTTGGAGCGGGTAAGCCACCGCTACAAGGCCAAGGTAGCGGTGGACGATGTCAGCCTGCACATCGCCTCGGGGGAGATCGTCTGCCTGGTCGGCCCGTCGGGCTGTGGCAAGTCCACGCTGCTTCGCCTCGCGGCGGGGCTGGAGCGGCTGCAGCAGGGTACCGTCGCCATCGCCGGGAAGACCATTGCCGATCCGTCCGCGAGCCTGCCGCCGGAGCGGCGGGGAATCGGCCTGGTGTTCCAGGACTTCGCCCTGTTCCCGCACCTGACCGTGCTGGACAATGTCCGCTTCGGCCTCAACAAGCTGCCGCCCGCCACCCAGAAGGAGCGGGCGCTGGCCGCCCTGAAACAGGTGGGCATGGAGGCCTATGCCGCCGCCTACCCGGACGCCCTGTCCGGCGGGCAGCAGCAGCGGGTGGCTCTGGCCCGCGCCATGGCGCCCCAGCCGGCGGTGCTGCTGCTGGATGAGCCCTTCTCCGGCCTGGACACCCGCCTGCGTGAGACGATCCGGGACGAGACGCTGCATGTGCTGAAGCAGAGCGGGGCCGCCACACTGGTCGTCACCCACGACCCGGAGGAGGCCATGTTCCTGGCCGACCGCATCGCCCTGATGCGCGACGGCCGCATGGTCCAGGTGGGCAAACCGGTGGATCTCTACACCAAGCCTGTCTGCATCTTCGCCGCCAGCTTCTTCGGGGAGGTGAACCGCCTGCGCGGCACCGTCCGCCAGGGCCGGGTGGAGACGCCGGTGGGCAGCGTTCCGGCGGCCCGGCACGCGGACGGCACGGCCGTGGACGTGCTGATCCGGCCGGAGGGCCTGCGCCTGTCCGCCGACCCGGCCGCCGGCCCGGATGGGCGGCTGCCGTACCTGGCCCGGGTGGAGGCGGCCCGGCTGTTGGGGCGCACCAGCCTGGTGCATCTGCGGGTTTCGGACGGGCAGGGGGGCATCCACCTGCATTCCCGCATGCCCGGCCAGTTCCTCCCCGAGGAGGACAGCCATGTCTCGGTCACGCTCGACCCGCAACAGGCCTTCGTCTTTTCCGCAAGCGACCCCATGTAACGGGTGGCGTTGAGGTGTGGGGGGCGGCGTTGCGGCCCCCGACCCTTTCTGCCATTATCCCGCGCCAGCGTCCGGGGCGCCCCCGAACTGCGGAGAAAGCATAATGTCCATCGGTATTTGGCAGCTCGTCCTCGTGCTCGTTATCGTGCTCCTGCTCTTCGGGGCGGGGAAGCTGCCGCGGGTCATGGGTGACCTCGCCAAGGGCATGAAGAACTTCAAGCAGAACCTGAAGGAAGGCGAGGAGACGGAAGCGGTGGACGCCGGCCGGGCCATCCGGTCCGACACCGCCGTGCCGCCCGCGTCCACCCAGGGCACCGCCTCCAAGGAAGAGGCCAAGGGTTGAGGCCGGCCCCGTCACCTCTAGGACGCTGCCGCCATGCTTGACATCGGTTGGTCGGAGATCGCCGTCATCGCCGTGGTGGCCCTGCTGGTCATCGGGCCGAAGGACCTGCCGCGGGCCCTGGCGACCGTGGGCAAGTGGGTGCGCAAGGCACGCATGCTGGCCCGGGAGTTCCAGTCAAACGTGGATGAGATGGTCCGGCAAGCGGAACTGGAAGACCTGCGCAAGCAGGTGGACGAGGCCCGCAGCTTCAACCTGGCCACCCAGTTCGAGAAGACTGTGGACCCGGACGGCGGCCTGCGGAACGCGCTGAAGGTCGACGACACACCACGCCCCACCGCGGTGGATGCGGGCCGGGAGGCTGACAAGGCCCCGGCACCGGCGGCGCTTCCCCCGGCCCAGCCGGTGCCGACCCTGGAGGCCGACCCGGTGCCGGTCGCGGCCCCCGTCGCCCCGGCGGCCCCCGCCGAGGCCGCCCCGCTGCCCAAGGCGGCAGGCGACACTGCGGCGCGAGGCTGACCCCATGGCGATGCACAACATGCCCGCCGGCGAGGAAGAGGTCGATGCCAGCAAGATGCCGCTGCTCGACCACCTGATCGAGCTGCGCAACCGGCTGGTCTACAGCCTTGCAGCCCTGTTCATCGCTTTCCTTCTCTGCTTCTACTTCGCGGAAGCGATCTACAAGCTGCTGATGTACCCGCTGGTGCTGGCCTATGGCCCGGACGCGCAGAACCGGCGGATGATCTACACGGCGCCGCAGGAGGCGTTCCTGACCTATGTGAAGGTGGCGTTCTGGGGCGGGGCGCTGATCTCCTTCCCCATCATCGCCAACCAGGTCTGGAAATTCGTCGCCCCCGGCCTCTACAAGCACGAGAAGAAGGCGTTCCTGCCGTTCCTGGTGGCAACGCCGGTCCTGTTCAGCATCGGCGGGCTGCTGGTCTATTTCTTCATCATGCCCATGGCCCTGCGCTTCTTCATCGGCTTCGAGTCCGCCGGCGGTGAAGGAAGCCTCGCCATCGTGGCTGAGACGCGGGTGGCCGAGTACCTGTCGCTGGTGATGACGCTGATCTTCGCCTTCGGCATCGCGTTCCAGCTGCCCGTGTTGCTGACCCTGCTGGCCCGGGTGGGGCTGGTGACGGCGGACGGGCTGGCGTCCAAGCGGCGCTACGCCGTCGTCATCATCTTCGTCGCCGCGGCCATCCTCACCCCACCGGACGTGATCAGCCAGGTGGGCTTGGCCATCCCGCTGATCCTGCTCTACGAGGTCTCGGTCTTCATGGCCCGCCGGATCGAGAAGCAGCGCGCGGCGGCCGAGGAAGCCGAGGACGAGGCGGTCTGA

Protein sequences of DBSCAN-SWA_1

>NZ_CP051775|1394238:1400426|1399625_1400426_+|WP_075769199.1|DBSCAN-SWA
MPAGEEEVDASKMPLLDHLIELRNRLVYSLAALFIAFLLCFYFAEAIYKLLMYPLVLAYGPDAQNRRMIYTAPQEAFLTYVKVAFWGGALISFPIIANQVWKFVAPGLYKHEKKAFLPFLVATPVLFSIGGLLVYFFIMPMALRFFIGFESAGGEGSLAIVAETRVAEYLSLVMTLIFAFGIAFQLPVLLTLLARVGLVTADGLASKRRYAVVIIFVAAAILTPPDVISQVGLAIPLILLYEVSVFMARRIEKQRAAAEEAEDEAV
>NZ_CP051775|1394238:1400426|1396777_1397383_+|WP_075769110.1|DBSCAN-SWA
MPIPDDRNQQLRLVEAILFASADPVPEEALQARFGEGVQVRELLLDLQALYEHRGVNLSAMGGRWAFRTAPDLGEHLRSETEVTAKLSRAAIETLAIIAYHQPVTRAEIESIRGVATSKGTLDILMEAGWIKPGRRRETPGRPVTWVSTPHFLDHFGLESLRDLPGVEDLRAAGLLDSRSGMGPLAPVALPAEAEPEPAEG
>NZ_CP051775|1394238:1400426|1398850_1399090_+|WP_075769109.1|DBSCAN-SWA
MSIGIWQLVLVLVIVLLLFGAGKLPRVMGDLAKGMKNFKQNLKEGEETEAVDAGRAIRSDTAVPPASTQGTASKEEAKG
>NZ_CP051775|1394238:1400426|1399123_1399606_+|WP_075769108.1|DBSCAN-SWA
MLDIGWSEIAVIAVVALLVIGPKDLPRALATVGKWVRKARMLAREFQSNVDEMVRQAELEDLRKQVDEARSFNLATQFEKTVDPDGGLRNALKVDDTPRPTAVDAGREADKAPAPAALPPAQPVPTLEADPVPVAAPVAPAAPAEAAPLPKAAGDTAARG
>NZ_CP051775|1394238:1400426|1394238_1395264_+|WP_075769113.1|DBSCAN-SWA
MSGKAPLAIAFGCAGTSLTPGERALFREADPLGFILFRRNVDSPDQVRRLVAEMRDSVGRDAPVLIDQEGGRVARLRPPHWPALPAARACGVVAERDPIRGTRASWLHGRLLAHMLADLGIDVDCAPVADVPVPGAHDVIGDRAFAGEPGLVATLARAQAEGLMAGGVLPVMKHIPGHGRAHVDSHKELPVVHADRIDLERQDFAPFRDLADLPLGMVAHVVYTEVDPHRPASTSNTVISEVVRGWIGFRGLLFSDDIGMQALSGTAGQRAAAVLAGGCDVALHCGGDFAEMQDVAANGRALTPESLARWQAAKALVRAPEPADAQELRAELDAILAGGVA
>NZ_CP051775|1394238:1400426|1395265_1395952_+|WP_075769112.1|protease|DBSCAN-SWA
MDEISGFIQALTVVLLPGLVAITFHEAAHGYVAKRFGDNTAYMLGRVTFNPLKHIDPFGTIILPLIMFFTTGFLFGWAKPVPVDFRNLRDPKRDMIWVALAGPGVNIFLALMSAFLLHTVPLMPEAAQEWFHQNLLFSVQINVLLAVFNMLPLPPLDGGRVVTGILPGRLSYQFASIERYGMLILLAAVFLVPFTAQQLGYSFNPLFYVLLPPMDFITDLIVRVAGLT
>NZ_CP051775|1394238:1400426|1397469_1398747_+|WP_169654902.1|DBSCAN-SWA
MAPLPGARCGFVGHHGCDVSVSPRSRSPLWRSLSARVEAAAPAKVPARERGSPVDALGPRQAPAAAELRPALALERVSHRYKAKVAVDDVSLHIASGEIVCLVGPSGCGKSTLLRLAAGLERLQQGTVAIAGKTIADPSASLPPERRGIGLVFQDFALFPHLTVLDNVRFGLNKLPPATQKERALAALKQVGMEAYAAAYPDALSGGQQQRVALARAMAPQPAVLLLDEPFSGLDTRLRETIRDETLHVLKQSGAATLVVTHDPEEAMFLADRIALMRDGRMVQVGKPVDLYTKPVCIFAASFFGEVNRLRGTVRQGRVETPVGSVPAARHADGTAVDVLIRPEGLRLSADPAAGPDGRLPYLARVEAARLLGRTSLVHLRVSDGQGGIHLHSRMPGQFLPEEDSHVSVTLDPQQAFVFSASDPM
>NZ_CP051775|1394238:1400426|1395958_1396774_+|WP_075769111.1|DBSCAN-SWA
MADPLSPDPFDQPVRDGTPEVVADAPLLLAIDGYEGPIDLLLTLARDQKVDLTRVSILQLADQYLSFVETAKRLRLELAADYLVMAAWLAYLKSRLLLPEPETEEPSGEELAAALAFQLQRLEAMQGVAARLLARPRLGRDVFARGAPEDMPVLEKRIHEVSLYDLLKAYGEHKQRQMKQGPLTIAATELYSIEDAVARVEAMLGKLPSWTKLSSFLPAGWRSGGVKTRSALASTFVATLELAKAGRLEIRQEGAFGPIFLRTPQSQEGGT

Homologous phage analysis in the prophage region

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_075769113.1|1394238_1395264_+	beta-N-acetylhexosaminidase	A0A1B1IVS3	uncultured_Mediterranean_phage	3.8e-21	41.3
WP_075769112.1|1395265_1395952_+|protease	site-2 protease family protein	NA	NA	NA	NA
WP_075769111.1|1395958_1396774_+	segregation/condensation protein A	A0A1B1IVW1	uncultured_Mediterranean_phage	3.2e-39	37.6
WP_075769110.1|1396777_1397383_+	SMC-Scp complex subunit ScpB	A0A1B1IVT7	uncultured_Mediterranean_phage	1.5e-41	44.4
WP_169654902.1|1397469_1398747_+	ABC transporter ATP-binding protein	G3M9Y6	Bacillus_virus	6.6e-31	36.4
WP_075769109.1|1398850_1399090_+	twin-arginine translocase TatA/TatE family subunit	A0A1B1IVR9	uncultured_Mediterranean_phage	4.0e-06	54.5
WP_075769108.1|1399123_1399606_+	twin-arginine translocase subunit TatB	NA	NA	NA	NA
WP_075769199.1|1399625_1400426_+	twin-arginine translocase subunit TatC	A0A1B1IVR7	uncultured_Mediterranean_phage	5.5e-60	52.3