CRISPRimmunity

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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_CP009448	Achromobacter xylosoxidans C54, complete genome	3 crisprs	cas3,DinG,DEDDh,csa3,WYL,PD-DExK	0	0	4	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP009448_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP009448_1

1513890-1513998

Orphan

Consensus_repeat	Method
GCCGCCGCCAAGAGCCTCGCCGAAAAGGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP009448_1

>merge|NZ_CP009448|1|1513890-1513998|CRISPRCasFinder
GCCGCCGCCAAGAGCCTCGCCGAAAAGGGCTGCCCCGGCCGCTCCCGCCTCCACCGCCGCCGCCGGCGTGGCTTCGCCCGCCGCCGCCAAGATCCTCGCCGAAAAGGGC

>NZ_CP009448|1|1|1513890-1513998|CRISPRCasFinder
GCCGCCGCCAAGAGCCTCGCCGAAAAGGGC	TGCCCCGGCCGCTCCCGCCTCCACCGCCGCCGCCGGCGTGGCTTCGCCC
GCCGCCGCCAAGATCCTCGCCGAAAAGGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009448.1\|WP_006389377.1\|1507492_1508437_-\|allantoinase-PuuE	unknown	unknown	gnl\|CDD\|211797
NZ_CP009448.1\|WP_006389376.1\|1505786_1507481_-\|peptidase-M20	unknown	unknown	gnl\|CDD\|184168
NZ_CP009448.1\|WP_006389388.1\|1520762_1521395_+\|DUF4198-domain-containing-protein	unknown	unknown	gnl\|CDD\|378467
NZ_CP009448.1\|WP_006389375.1\|1504550_1505783_-\|peptidase-M20	unknown	unknown	gnl\|CDD\|349869
NZ_CP009448.1\|WP_006389383.1\|1514961_1516389_+\|dihydrolipoyl-dehydrogenase	unknown	unknown	gnl\|CDD\|235779
NZ_CP009448.1\|WP_006389391.1\|1523881_1525234_+\|tryptophan--tRNA-ligase	unknown	unknown	gnl\|CDD\|237036
NZ_CP009448.1\|WP_020924626.1\|1523415_1523739_+\|DUF3325-domain-containing-protein	unknown	unknown	gnl\|CDD\|371735
NZ_CP009448.1\|WP_038503075.1\|1521696_1523409_+\|PepSY-domain-containing-protein	unknown	unknown	gnl\|CDD\|377164
NZ_CP009448.1\|WP_038503071.1\|1499449_1502137_-\|alpha-ketoglutarate-dehydrogenase	unknown	unknown	gnl\|CDD\|237267
NZ_CP009448.1\|WP_006389392.1\|1525306_1525810_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP009448.1\|WP_006389378.1\|1508663_1509680_-\|1-aminocyclopropane-1-carboxylate-deaminase	unknown	unknown	gnl\|CDD\|183494
NZ_CP009448.1\|WP_006389369.1\|1496304_1496757_-\|DUF2214-domain-containing-protein	unknown	unknown	gnl\|CDD\|378336
NZ_CP009448.1\|WP_006389380.1\|1510672_1513540_+\|2-oxoglutarate-dehydrogenase-E1-component	unknown	unknown	gnl\|CDD\|236499
NZ_CP009448.1\|WP_006389393.1\|1526123_1528499_-\|RNA-binding-transcriptional-accessory-protein	unknown	unknown	gnl\|CDD\|225094
NZ_CP009448.1\|WP_006389379.1\|1509872_1510343_+\|AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|183009
NZ_CP009448.1\|WP_006389370.1\|1496908_1499206_-\|NADP-dependent-malic-enzyme	unknown	unknown	gnl\|CDD\|235976
NZ_CP009448.1\|WP_024068143.1\|1502433_1504491_+\|oligopeptide-transporter,-OPT-family	unknown	unknown	gnl\|CDD\|224216
NZ_CP009448.1\|WP_006389384.1\|1516465_1517557_+\|cell-division-protein-ZapE	unknown	unknown	gnl\|CDD\|224402
NZ_CP009448.1\|WP_006389385.1\|1517677_1518211_+\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|171561
NZ_CP009448.1\|WP_006389389.1\|1521418_1521700_+\|DUF3649-domain-containing-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP009448.1\|WP_006389377.1\|1507492_1508437_-\|allantoinase-PuuE	gnl\|CDD\|211797	TIGR03212, uraD_N-term-dom, putative urate catabolism protein. This model represents a protein that is predominantly found just upstream of the UraD protein (OHCU decarboxylase) and in a number of instances as a N-terminal fusion with it. UraD itself catalyzes the last step in the catabolism of urate to allantoate. The function of this protein is presently unknown. It shows homology with the pfam01522 polysaccharide deacetylase domain family.	0
NZ_CP009448.1\|WP_006389376.1\|1505786_1507481_-\|peptidase-M20	gnl\|CDD\|184168	PRK13590, PRK13590, putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional.	0
NZ_CP009448.1\|WP_006389388.1\|1520762_1521395_+\|DUF4198-domain-containing-protein	gnl\|CDD\|378467	pfam10670, DUF4198, Domain of unknown function (DUF4198). This family was previously missannotated in Pfam as NikM.	6.31409e-10
NZ_CP009448.1\|WP_006389375.1\|1504550_1505783_-\|peptidase-M20	gnl\|CDD\|349869	cd02697, M20_like, M20 Zn-peptidases include exopeptidases. Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.	0
NZ_CP009448.1\|WP_006389383.1\|1514961_1516389_+\|dihydrolipoyl-dehydrogenase	gnl\|CDD\|235779	PRK06327, PRK06327, dihydrolipoamide dehydrogenase; Validated.	0
NZ_CP009448.1\|WP_006389391.1\|1523881_1525234_+\|tryptophan--tRNA-ligase	gnl\|CDD\|237036	PRK12284, PRK12284, tryptophanyl-tRNA synthetase; Reviewed.	0
NZ_CP009448.1\|WP_020924626.1\|1523415_1523739_+\|DUF3325-domain-containing-protein	gnl\|CDD\|371735	pfam11804, DUF3325, Protein of unknown function (DUF3325). This family of short proteins are functionally uncharacterized. This family is restricted to Alpha-, Beta- and Gamma-proteobacteria.	3.16823e-22
NZ_CP009448.1\|WP_038503075.1\|1521696_1523409_+\|PepSY-domain-containing-protein	gnl\|CDD\|377164	pfam03929, PepSY_TM, PepSY-associated TM region. The PepSY_TM family is so named because it is an alignment of up to five transmembranes helices found in bacterial species some of which carry a nested PepSY domain, pfam03413.	7.6218e-68
NZ_CP009448.1\|WP_038503071.1\|1499449_1502137_-\|alpha-ketoglutarate-dehydrogenase	gnl\|CDD\|237267	PRK13012, PRK13012, 2-oxoacid dehydrogenase subunit E1; Provisional.	0
NZ_CP009448.1\|WP_006389378.1\|1508663_1509680_-\|1-aminocyclopropane-1-carboxylate-deaminase	gnl\|CDD\|183494	PRK12390, PRK12390, 1-aminocyclopropane-1-carboxylate deaminase; Provisional.	0
NZ_CP009448.1\|WP_006389369.1\|1496304_1496757_-\|DUF2214-domain-containing-protein	gnl\|CDD\|378336	pfam09980, DUF2214, Predicted membrane protein (DUF2214). This domain, found in various hypothetical bacterial proteins, has no known function.	3.49506e-56
NZ_CP009448.1\|WP_006389380.1\|1510672_1513540_+\|2-oxoglutarate-dehydrogenase-E1-component	gnl\|CDD\|236499	PRK09404, sucA, 2-oxoglutarate dehydrogenase E1 component; Reviewed.	0
NZ_CP009448.1\|WP_006389393.1\|1526123_1528499_-\|RNA-binding-transcriptional-accessory-protein	gnl\|CDD\|225094	COG2183, Tex, Transcriptional accessory protein [Transcription].	0
NZ_CP009448.1\|WP_006389379.1\|1509872_1510343_+\|AsnC-family-transcriptional-regulator	gnl\|CDD\|183009	PRK11169, PRK11169, leucine-responsive transcriptional regulator Lrp.	4.90767e-43
NZ_CP009448.1\|WP_006389370.1\|1496908_1499206_-\|NADP-dependent-malic-enzyme	gnl\|CDD\|235976	PRK07232, PRK07232, bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed.	0
NZ_CP009448.1\|WP_024068143.1\|1502433_1504491_+\|oligopeptide-transporter,-OPT-family	gnl\|CDD\|224216	COG1297, COG1297, Predicted membrane protein [Function unknown].	0
NZ_CP009448.1\|WP_006389384.1\|1516465_1517557_+\|cell-division-protein-ZapE	gnl\|CDD\|224402	COG1485, COG1485, Predicted ATPase [General function prediction only].	1.11009e-171
NZ_CP009448.1\|WP_006389385.1\|1517677_1518211_+\|RNA-polymerase-sigma-factor	gnl\|CDD\|171561	PRK12528, PRK12528, RNA polymerase sigma factor; Provisional.	1.83606e-59

>NZ_CP009448.1|WP_006389380.1|1510672_1513540_+|2-oxoglutarate-dehydrogenase-E1-component
MSSEIESLSTSYLFGGNAPYVEELYEAYLDNPGSVPDNWREYFDQLQHAPATDGQESTRDQAHAPIVESFAQRAKANAFVQRAAEPDLSVASKQVSVQSLIAAYRSLGSRWADLDPLKRQERPPIPELDPAFYGLTEADLDQTYSATNTYFTTASTMTLRDILKALRDTYCRSIGAEFTHISDPAAKRWIQERLETTLGAPSYTAEEKRHILQQLTESEGLERFLHTKYVGQKRFSLEGGESFIASMDEVVNHAGENGVQEIVVGMAHRGRLNLLVNIMGKMPGDLFAEFEGKHAEGLTDGDVKYHNGFSSDLSTRGGPVHLSLAFNPSHLEIVNPVVEGSARARQERRGDAEGKQVLPVLVHGDAAFAGQGVVMETLNLAQTRGYGTGGTMHIVINNQIGFTTSDPRDSRSTLYCTDVAKMIEAPVFHVNGDDPEAVVFVTKLALDYRLQFRHDVVVDIVCFRKLGHNEQDTPSLTQPLMYKRIGHHPGTRKLYADKLTTQGVLAEGEADQLVKDYRQLMEDGQRTIEPVLTDYKSKYAIDWSPFLGAKWTDQADTAVPLAELKRIGERITTVPEGFTVHPLVAKLLNDRRTMAKGEMNLDWGMGEHLAFATLVSSGYAIRITGQDSGRGTFTHRHAVLHDQNRERWNDGTYIPLQNVSEGQAPFTVIDSVLSEEAVLGFEYGYSSAEPNTLTIWEGQFGDFVNGAQVVIDQFISSGEAKWGRQSGLTLMLPHGYEGQGPEHSSGRIERFLQLCADNNMQVIQPTSASQIFHVLRRQMIRPFRKPLVLFTPKSLLRNKDAGSPLTELAGGSFRPVIGEVDEAIDAAKVKRVLACSGKVYYDLVNARRERGADNVAIIRVEQLYPFAHKSFEAELRKYPKATEVIWVQDEPQNQGPWFYVQHHVYENMVEGQKLGYAGRAASASPAVGYLAKHQEQQKALIEAAFAPKFKAMLTK
>NZ_CP009448.1|WP_006389379.1|1509872_1510343_+|AsnC-family-transcriptional-regulator
MAAIAGLDRIDRQILRLLQQDAQITNLDLSARVHLSPAACLRRVEKLRAEGVIRKTVALLEPAEVEMATLVIVGVVLDRSTPESFTDFEAAARGISGCLECHLVAGEFDYFLMLRIRDLERFNKLHAGEIIKLPGVRQIRTFFVLKEILSTTELPL
>NZ_CP009448.1|WP_006389378.1|1508663_1509680_-|1-aminocyclopropane-1-carboxylate-deaminase
MDLQRFPRHRLTFGDTPIEKLERLSAHLGGKVEIYAKREDCNSGLAFGGNKLRKLEYLIPQALEQGCDTLVTIGGIQSNHTRMVAAVAAKLGLACVLVQENWVDYSDAVYDRVGNIMMSRLMGADVRLVDQGFDIGFRRSWEEALEDVRKRGGKPYAIPAGASDHELGGLGYVGFAEEVRRQEAELGFKFDYIVVCAVTGSTQAGMVVGFAADGRANRVIGIDASATPDQTRAQILRIARRTADLVGLQRPITDSDVVLDTRYAYPAYGLPSAETNEAIRLCARLEGMMTDPVYEGKSMQGMMDIVRRGEIPAGSRVLYAHLGGVPAINAYSFLYRNG
>NZ_CP009448.1|WP_006389377.1|1507492_1508437_-|allantoinase-PuuE
MSTYDATDSYPRDLIGYGRNPPHAQWPGNARIAVQFVLNYEEGGENCVLHGDAGSEQFLSEMFNPASYPERHLSMEGIYEYGSRVGVWRILREFEKRGLPLTVFAVGMALQRHPELAAALVELDHEIACHGWRWVHYQNVDEATEREHMRLGMDAIAQLTGARPLGWYTGRDSPRTRRLVADYGGFEYDSDYYGDDLPFWMRVQKSDGSVAPQLIVPYTLDCNDMRFALPQGYSHADPFFQYLKDSFDALYAEGDEAPKMLSIGMHCRLLGRPGRIVALQRFLDHIARHDRVWVCRRLDIARHWQARHPYQPAP
>NZ_CP009448.1|WP_006389376.1|1505786_1507481_-|peptidase-M20
MAHTLAQFNDATPQAAAAMLADLYPHAPWAAEQAVRARPMHSVAQLQLALQRAVDDADAATQLALLRAQPAPDAGTDAAALIADHAARFGFPFVLSRYSPRGASLQGTQLVQALERRRHNAPDDERREALRQLHRDAEVRLYERFGVEPELGNDIWDWQEKLSAHSDPGYAENGQLTVTYLTDAHRACAQRISHWMRDCGFDEVGIDAVGNVVGRYHAARADAPILMSGSHYDTVRNAGKYDGRLGIFVPMACVRALQRQGRRLPYAIEVIAFSEEEGQRYPATFLGSGALIGDFQPRWLEQRDADGISMREAMARAGLCVDDIPKLKRDPARYLGFVEVHIEQGPVLNEMGLPLGVVTSINGCVRYRVRIHGTACHAGTTPMDRRRDAAVAAAELIVFVEGRAARDGDSVGTVGMLEVPNGSINVVPGECRFSLDLRAPSDPQRDALASDVLAELEAICLRRGLRYTLEETMRAAAAPSAPAWQQRWERAVQALGVPVHCMPSGAGHDAMKLHEIMPQAMLFVRGQNAGISHNPLESTTNHDMQLAAQAMQRLLDDLANDATS
>NZ_CP009448.1|WP_006389375.1|1504550_1505783_-|peptidase-M20
MTDYARLDAWVDAHFDEEVRFLQELVRVPTDTPPGNNAPHAVRTAELLQGFGLAAESHPVPADEVRAYGMESITNLIVRREYGAGGRRVALNAHGDVVPPGDGWEHDPYGAQIEDGCLYGRAAAVSKSDFASFTFALRALEAVARPSQGAVELHFTYDEEFGGLLGPGWLLRQGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKMAHAAIPATGVDALQGAVAIMNALYAQNARYREITSRVEGISHPYLNIGRIEGGTNTNVVPGKVVFKLDRRMIPEENAAEVEADIRRIIEEAAAATPGIRVEIKRLLLANAMRPLPGNQPLVDAIRRHGQELFGESIPAMGTPLYTDVRLYAEAGIPGVIYGAGPRTVLESHAKRNDERVVLEDLRRATKVIARTLADLLQPA
>NZ_CP009448.1|WP_024068143.1|1502433_1504491_+|oligopeptide-transporter,-OPT-family
MTQPTSVPAEVTLPELTFRGVLLGAVITIIFTASNVFLGLKVGLTFSSAIPAAVISMSVLRLFKDANILENNMVQTQASAAGTLSAIIFILPALVMMGHWQGFPFWQTLGICAAGGMLGVMFTIPLRHVMVVQSDLPYPEGVAAAEILRVGSAERAQDVAADAGRAPAGPAATGMGDIVSGGVVAAAVSFAASGLRVLGDGVSGWFALGGAVFRLPMGFSLALLGAGYLIGIVAGLAMLTGLVISWGIAVPILTSMAEIPADMSLAKFATGLWSSQVRFIGAGVIGVGAIWTLATLFMPMARGVKASFSALTRAGAARAGKAPRTERDLSAGWISVVTLVLVAVLVITFQVFLADAPLSAAAVWKLVAYAVLFAFVFGFLVAAACGYMAGLVGTSTSPISGVGIVAIVLVSLLLLVLGGELLAVQNGVQMTIALAIFSTSAVVAVASISNDNLQDLKTGWLVGATPWRQQVALLIGCVLGAAVISPVLDLLYNAYGFADAMPREGMDPSQALSAPQATLMLAIARGIFTHQLNWTMILIGMAVGVGLIVVDEILKRTCKVARIPVLAVGIGIYLPPTVAAPIVVGALLAWLLERALRRRAAAAGKDYVSFADAANRRGVLIASGLIVGESLVGVVMAAIIGASGTDAPLAIAGEEFARTASFLGLAVFALVAVLFWRRVMRLAQP
>NZ_CP009448.1|WP_038503071.1|1499449_1502137_-|alpha-ketoglutarate-dehydrogenase
MCDASHSSAGPDPRHDADPAETAEWRDGLQSLVEASGAERAGYVLDNLLGHAATLGLRANSQTRTAYLNTIPADQEPPFPGNLAVEERIARINRWNALAMVVRANQAHGELGGHIASYASAADLFEVGFNHFFRAAGADGPGDLVYMQPHSAPGVYARAYLEGFLSEDDLAHFRQEITATSRGLRGLSSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLEHRSLVPASDRKVWGIFGDGEMDEPESIAALTLAAREKLDNLVFVVNCNLQRLDGPVRGNGRIIDELETLYAGAGWNVIKLVWGSDWDALLRRDGNGALARAFANTVDGQFQTFAANDGAFNRAHFFNQNPELAALVADWTDEAIDRLHRGGHDMVKIHAAYHRAAHHRGQPTVILAQTKKGFGMGAAGQGKMTTHQQKKLDDEALLAFRDRFALPISDADCLALKFYRPAEDSAELRHLQARRAALGGHIPRRRTQAPRLSPPAVDQWARFALNADGKEMSSTMAIVRMLTALLKDPQVGPRIVPIVADEARTFGMANLFRQIGIYSAQGQLYEPEDIGSVLYYREARDGQILEEGITEAGAISSWTAAGTSYSVNGLPMLPFYIYYSMFGFQRIGDLIWAAADQRTRGFLIGATSGRTTLGGEGLQHQDGSSHIMAAAVPNCRAYDPAYAYEVAVIVEYGMRRMLDEQRDEFFYLTVTNENLAQPDLPRDGAAAEGILRGMYRLRPARQQAAVRLLGAGPMLREAEMAAERLHAEYGVDAEVWSVTSFSELARDGREAERARALGLPAAPDADWVRACLGGSDAPVVAATDYVRAVPEQIRAWVPAPYRTLGTDGFGRSDTRARLRDFFEVSADWIVLHALDSLGRQEQANALRLKLGAADRATPPWAQ
>NZ_CP009448.1|WP_006389370.1|1496908_1499206_-|NADP-dependent-malic-enzyme
MDETLTKLALDYHAYPTPGKISVTPTKPLANQDDLSLAYSPGVAAACMAIFDQGDDAASKYTSRGNLVGVITNGTAVLGLGNIGPLAAKPVMEGKGCLFKKFAGIDVFDIELAENDPDKLVDIIAALEPTLGGVNLEDIKAPECFYIEKKLRERMKIPVFHDDQHGTAIISSAAILNGLKVVGKDIGTVKLACSGAGAAAIACLDLLVHLGVKRENIYVVDSRGVIWEGRDENMEANKKRYAQKTDARTLADVVNGADVFLGCSTAGVLTADMVKTMADRPLILALANPEPEIRPEVAKAARPDCIIATGRSDYPNQVNNVLCFPFIFRGAMDAGASRITEEMKLACVKAIAELAQAEQNDEVARAYAGQELSFGPDYIIPKPFDPRLIVQIAPAVAQAAADSGVAARPIEDIEAYRQKLMGFVYHSGQLMRPLFAQAKKAPKRVIYADGEDERVLRAVQTVADEKLAFPILIGRPSVIEMRIKKFGLRLIAGQHFEIVDPEDDSRFNETWSAYYQLKGREGVTPAIAKAMIRKHNTLIGAMLLRRGDADALLCGVASKYDNQLKYIDEIIGKKEGQTYAALNVLMLPDQTLFVTDTHVNENPSAEEVANITIQAADEMLRFGVVPKIALLSHSNFGSRVTESSRKMAAARQLVQDRAPDLEVDGEMHADAALSEKIRVLAYPDSTLKGRANLLVMPTLDTGNITYNMLKMTGSNGVAMGPILLGAARPVHILTTSATVRRIVNMTALAVVDAQQEAAEAAKKRR
>NZ_CP009448.1|WP_006389369.1|1496304_1496757_-|DUF2214-domain-containing-protein
MLLDAFLAWFHFLAIFVLVVVLTAEAVLLRPDLTPATLKRLVIYDRLYLLSAILVLATGVLRLMLGIKGAAFYMGNPWFHAKITLFVIIGLCSIPPTLAFLRWAKQARQQPAFVPDAAQIKRARRWVMIESHLFIFLPLFAVLMARGIGA
>NZ_CP009448.1|WP_006389383.1|1514961_1516389_+|dihydrolipoyl-dehydrogenase
MSKQFDVVVIGAGPGGYIAAIRAAQLGMSVACIDAWQNGQGGPAPGGTCTNVGCIPSKALLQSSEHFEQANHHFAEHGIEVKGVSLKLDTLIGRKNSVVKQNNDGILYLFKKNKVTFFHGKGAFAGQVEGGWAIKVTGTAEEDLVAKHVVVATGSSARELPGLPFDEKVVLSNDGALNIGAVPKTLGVIGAGVIGLEMGSVWRRLGAEVTILEAMPEFLAAADQQVAKEALKAFTKQGLNIQMGVKIGEIKATAKSVTVPYVDAKGAEQKLVVDKLIVSIGRVPYTGGLNADAVGLKLDERGFIAVDGDCKTNLPNVWAVGDVVRGPMLAHKAEEEGVAVAERIAGQHGHVNFDTVPWVIYTSPEIAWVGKTEQQLKAEGREYKAGSFPFLANGRARALGDTTGFAKVIADAKTDEVLGVHIVGPMASELISEAVTIMEFRGAAEDIARICHAHPTLSEAVKEAALAVDKRALNF
>NZ_CP009448.1|WP_006389384.1|1516465_1517557_+|cell-division-protein-ZapE
MNVREYYEHALAERGYKPDEAQKKAIDRLQRYYDEWVKFKAMRSNALKKLLNRPDVPRGVYLWGGVGRGKSFLMDAFYATVPVVRKTRLHFHEFMRGVHRELEEVKGMQDPLDEVAKRVAKRYRLICFDEFHVSDVADAMILHRLLFKLFEYGTSFVMTSNYEPSTLYPDGLHRDRVLPAIELIQARMDVMNVDAGVDYRRRSLEQVQCYHTPLDEHAQQALQRAFDSLADTPPQEPLLHIEHREIRALALAGSVVWFDFATLCGGPRSQNDYLELANRFHAVILSGVPRMGPRQASEARRFTWLIDVFYDHRVKLIMSAECEPEEIYTEGALANEFHRTVSRILEMQSREYLESERRLTATL
>NZ_CP009448.1|WP_006389385.1|1517677_1518211_+|RNA-polymerase-sigma-factor
MSSPILSSPASCADAPATQVDGLYRDHRPWLFGWLRRKLGCAHRAEDLAQDVFVRVIQGRKTVRAGEARALLTTIAKGLVIDHQRHAALEHAYLAYLADLPEAHAPSPETQAEQMQALMQLDRLLDSLPPKARSAFLLSQLDGLTYPEIAQRLGVSVSSVQQYMVRAMSACYAAFHD
>NZ_CP009448.1|WP_006389388.1|1520762_1521395_+|DUF4198-domain-containing-protein
MKFARTLAAVALLGSAGAAQAHFVWLERADQGPAKAYFGEWADDLREKRDGLLGKVLVAPVVTGADGKALKASAQGADFVEFAASGKGEVRLSQPIQFKDTLMQYGAKAGREDTQGKLDLELVPAAAGSNTFVLQFKGKPLAKTEVTVFGPPKWEKRLRSDENGRIEITTPWPGQYVLEAAHVEDKAGEADGKAYAKIRYVSTLTFNVTK
>NZ_CP009448.1|WP_006389389.1|1521418_1521700_+|DUF3649-domain-containing-protein
MMRYRLAVASRALAAILGGYGLASAAAACLAVWLPMQRADAVVTAQMSAFVVYTCGVIWVFATRNAWRAWAGILLPAALFGGLFLIGRMVGGA
>NZ_CP009448.1|WP_038503075.1|1521696_1523409_+|PepSY-domain-containing-protein
MKPSTGKAQGEEGLRQSMSWLHTWSGLIFGWVLFAMFLTGTLSFFRPEITRWMQPEIQAQAAPTLESVTMAQRYLTEHAPDAKRWFITPPTDREPLIQLLYQVPKPKPGERGFVRVKLDPRTGQAVQGRETRGGDFFYRFHFELETAFPWGRWLASIAGMFMLVAIISGIITHKKIFADFFTFRPKKGGQRAWMDGHNALSVLGLPFHLMITFSGLVLFATMLMPAGILAVYENPRQYSDDVFPGFKVTPPRNEPAPLVALAPLVEQVEQRWQGRVGRVTVNNPGDAGATVTLTRDAADGVSYGRLAPYARFDGVTGAFQEGQDELSPTVRTAGVIVGLHLGLFAEPLLRWFYFLVSLAGTGMVGSGLVLWIAKRRQKARPGAREAFSLRLVDGLNAGTIAGLFIAVAAFFWANRLVPADLPGRPLWEVRAFFAAWGLSLVYAFVFHKRKWVDLLSAAAASLALVPVINAVTTSRHLGVSLPTGDWVMAGFDLTCLAGALLLGWMARKAARARKAPAKAGGKAAARTAAPAQVQAQPQPDTQAQPVARPRAPVASAMAQATPSEAAYEPR
>NZ_CP009448.1|WP_020924626.1|1523415_1523739_+|DUF3325-domain-containing-protein
MTLAAFCLAYAGFSALCLGMDRHYEDLFDRALPRRHRVPLRTFGWLALALSLCASAAVWGWSYGTVEWIGILSIAGLLLIWFLTFRPRAALTAGGLCAVAAPLLAVL
>NZ_CP009448.1|WP_006389391.1|1523881_1525234_+|tryptophan--tRNA-ligase
MNTRVLTGITTSGTPHLGNYAGAIRPAVQASTQPGVDAFFFLADYHALIKCDDPARVARSRLEIAATWLAVGLDPERVTFYRQSDIPEIPELSWLLTCVTAKGLMNRAHAYKASVDQNVAKGVDPDDGVTMGLFSYPVLMAADIVMFNANKVPVGRDQIQHLEMARDIAQRFNHLYGREYFTLPEVAIEEDVATLPGLDGRKMSKSYNNTIPLFEGGAKALRASIMRIVTDSREPGEPKDAEGSHLYTIYRAFATHEQATAFRQQLEQGLGWGEAKQALYDHLENLLAPMRERYFDLMANPGRIEDVLQAGAAKARKLAVPMMRELREAVGLRNLNAQAPGKQAQAKKEKGKGARFVSFRDEDGGFRFRLLAADGEELLLSQRFADPKEAGALMRRLQSESPEALLQATADGLAAVLDGAVVAAAPAGAAGDAQAQLAKARDALLSMAQE
>NZ_CP009448.1|WP_006389392.1|1525306_1525810_-|hypothetical-protein
MRNTITLAANETATITEKEASLSGAYNEVTLGQYAHLKVDGAEVTFKHITLERLGSRIIELTNGAQLHVGALGFASMGASIIYRIGAGCVLTFDASQWDPEVVANTTFDFASQGSGTLKYFPFINPEWLDCPTVTGYSEGDMLEIAGQGNAQRFQVRDGRIVSAGAR
>NZ_CP009448.1|WP_006389393.1|1526123_1528499_-|RNA-binding-transcriptional-accessory-protein
MSETSVITNVAAGVDNARIVAQLATELGARASQIASAVELLDDGATVPFIARYRKEATGGLDDTVLRNLEVRLGYLRELEERRGAILESISQQGKLTPELQQEIATADTKQRLEDLYAPYKPKRRTRAQIAREAGLEPLADAILSDTACDPAALAAQYLNPEASINDAKAALDGARDILAERYAENADLLADMREHLWSTGYLYSKMVDGKETEGANFRDWFDFNEPLRTLPSHRILALLRGRQQGVLEIRLGLEAELEAQLPHPCVARIASFLKLGNGLFALDASPRARWLGEVCRWTWRVKLVTAFESELIGRLRETAEAEAIRVFAANLKDLLLAAPAGPKAVLGLDPGIRTGCKVAVIDRTGKVVDTTTVYPFEPRRDREGTINTLAALVARHKVDLIAIGNGTASRESEKLVGDMQERFPDLKVTRVVVSEAGASVYSASETAAQEFPDLDVTLRGAVSIARRLQDPLAELVKIDPKAIGVGQYQHDVNQRELARSLDAVVEDCVNAVGVDVNTASAALLARVSGLNSLLAKNIVAWRDENGAFPTREQLRKVPRFGDKAFEQAAGFLRIPNGDNPLDASSVHPEAYPVVERIVAKIKAEVKQIIGQRDALKGVSPSDFTDERFGLPTVRDIFAELEKPGRDPRPEFKTAQFKEGVETLNDLYPGMVLEGVVTNVANFGAFVDIGVHQDGLVHISALAEKFVKDPRDVVRVGQTVSVKVLEVDVARKRVALTMRLNDTAAPARRGADAPKGGDRPGRRPQGDNGRGNAGGAGMNSAMADAFAKLKR

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Crispr_ID: NZ_CP009448_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP009448_2

4314070-4314177

Orphan

Consensus_repeat	Method
TTTTCATCGCCGAGCCGCCTCAAGATGAAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP009448_2

>merge|NZ_CP009448|2|4314070-4314177|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGATGAAAAATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCCTTTTCATCGCCGAGCCGCCTCAAGATGAAAA

>NZ_CP009448|2|2|4314070-4314177|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGATGAAAA	ATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCC
TTTTCATCGCCGAGCCGCCTCAAGATGAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009448.1\|WP_006387144.1\|4306525_4307509_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
NZ_CP009448.1\|WP_006387145.1\|4305606_4306515_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|184959
NZ_CP009448.1\|WP_080747579.1\|4316265_4317747_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|273830
NZ_CP009448.1\|WP_006384576.1\|4321184_4322075_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP009448.1\|WP_006387133.1\|4323136_4324339_+\|DUF2863-domain-containing-protein	unknown	unknown	gnl\|CDD\|371362
NZ_CP009448.1\|WP_076468376.1\|4322118_4322892_-\|dioxygenase	unknown	unknown	gnl\|CDD\|153375
NZ_CP009448.1\|WP_080747578.1\|4307566_4309078_-\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|236215
NZ_CP009448.1\|WP_052102908.1\|4317797_4318880_+\|hemolysin-D	unknown	unknown	gnl\|CDD\|185090
NZ_CP009448.1\|WP_038504108.1\|4320444_4321149_+\|siderophore-interacting-protein	unknown	unknown	gnl\|CDD\|99790
NZ_CP009448.1\|WP_024069800.1\|4324348_4325464_+\|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP	unknown	unknown	gnl\|CDD\|378385
NZ_CP009448.1\|WP_006387139.1\|4311313_4314019_+\|aconitate-hydratase-AcnA	unknown	unknown	gnl\|CDD\|236445
NZ_CP009448.1\|WP_006220534.1\|4325670_4326231_+\|elongation-factor-P	unknown	unknown	gnl\|CDD\|234788
NZ_CP009448.1\|WP_038504106.1\|4318879_4320409_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|129794
NZ_CP009448.1\|WP_006387149.1\|4300228_4301224_+\|NAD(P)H-quinone-oxidoreductase	unknown	unknown	gnl\|CDD\|176180
NZ_CP009448.1\|WP_006387147.1\|4302049_4304251_-\|TonB-dependent-siderophore-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP009448.1\|WP_006387148.1\|4301220_4301988_+\|NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235546
NZ_CP009448.1\|WP_006387140.1\|4310079_4311009_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP009448.1\|WP_080747577.1\|4304535_4305411_-\|pirin-family-protein	unknown	unknown	gnl\|CDD\|224655
NZ_CP009448.1\|WP_006387137.1\|4315304_4316216_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176149
NZ_CP009448.1\|WP_006387141.1\|4309074_4309962_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|187627

Protein	Function_ID	Function_description	E-value
NZ_CP009448.1\|WP_006387144.1\|4306525_4307509_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	3.3317e-127
NZ_CP009448.1\|WP_006387145.1\|4305606_4306515_+\|hypothetical-protein	gnl\|CDD\|184959	PRK14997, PRK14997, LysR family transcriptional regulator; Provisional.	1.1118e-62
NZ_CP009448.1\|WP_080747579.1\|4316265_4317747_+\|hypothetical-protein	gnl\|CDD\|273830	TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins].	2.25684e-58
NZ_CP009448.1\|WP_006384576.1\|4321184_4322075_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain 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.	2.94943e-47
NZ_CP009448.1\|WP_006387133.1\|4323136_4324339_+\|DUF2863-domain-containing-protein	gnl\|CDD\|371362	pfam11062, DUF2863, Protein of unknown function (DUF2863). This bacterial family of proteins have no known function.	0
NZ_CP009448.1\|WP_076468376.1\|4322118_4322892_-\|dioxygenase	gnl\|CDD\|153375	cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.	1.3179e-120
NZ_CP009448.1\|WP_080747578.1\|4307566_4309078_-\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|236215	PRK08276, PRK08276, long-chain-fatty-acid--CoA ligase; Validated.	0
NZ_CP009448.1\|WP_052102908.1\|4317797_4318880_+\|hemolysin-D	gnl\|CDD\|185090	PRK15136, PRK15136, multidrug efflux MFS transporter periplasmic adaptor subunit EmrA.	2.28011e-99
NZ_CP009448.1\|WP_038504108.1\|4320444_4321149_+\|siderophore-interacting-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	7.38838e-39
NZ_CP009448.1\|WP_024069800.1\|4324348_4325464_+\|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP	gnl\|CDD\|378385	pfam10093, EarP, Elongation-Factor P (EF-P) rhamnosyltransferase EarP. This entry includes family members such as EarP enzymes which are essential for post-translational activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate. This was further confirmed for Pseudomonas aeruginosa, Pseudomonas putida, and Neisseria meningitidis. As for S. oneidensis and P. aeruginosa, EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis for arginine glycosylation by EarP. Mutational analysis of efp and earP genes, resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP and EF-P are essential for P. aeruginosa pathogenicity.The protein family is also annotated in the CaZy Database as GT104.	4.19896e-175
NZ_CP009448.1\|WP_006387139.1\|4311313_4314019_+\|aconitate-hydratase-AcnA	gnl\|CDD\|236445	PRK09277, PRK09277, aconitate hydratase AcnA.	0
NZ_CP009448.1\|WP_006220534.1\|4325670_4326231_+\|elongation-factor-P	gnl\|CDD\|234788	PRK00529, PRK00529, elongation factor P; Validated.	2.09721e-96
NZ_CP009448.1\|WP_038504106.1\|4318879_4320409_+\|MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	7.53946e-126
NZ_CP009448.1\|WP_006387149.1\|4300228_4301224_+\|NAD(P)H-quinone-oxidoreductase	gnl\|CDD\|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	0
NZ_CP009448.1\|WP_006387147.1\|4302049_4304251_-\|TonB-dependent-siderophore-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.	3.73232e-108
NZ_CP009448.1\|WP_006387148.1\|4301220_4301988_+\|NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	4.98682e-91
NZ_CP009448.1\|WP_006387140.1\|4310079_4311009_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain 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.	3.03799e-56
NZ_CP009448.1\|WP_080747577.1\|4304535_4305411_-\|pirin-family-protein	gnl\|CDD\|224655	COG1741, COG1741, Pirin-related protein [General function prediction only].	4.60601e-36
NZ_CP009448.1\|WP_006387137.1\|4315304_4316216_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176149	cd08460, PBP2_DntR_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to 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.	3.79418e-69
NZ_CP009448.1\|WP_006387141.1\|4309074_4309962_-\|oxidoreductase	gnl\|CDD\|187627	cd05369, TER_DECR_SDR_a, Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR. TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. 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.	2.14208e-110

>NZ_CP009448.1|WP_006387139.1|4311313_4314019_+|aconitate-hydratase-AcnA
MPHNTLDTLKNFKIGNKSCQYYSLPALGKALGIDVQRLPVSIRIVLESVLRNCDGKKVTEEHVRQLANWQANAKREDEIPFVVARVVLQDFTGVPLLADIAAMRSVADKMGKSPKSIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFKRNQERYQFMKWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVHQDKKNNVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVAERATIGNMAPEYGATMGFFPVDGRTIDYFRGTGRTEDEIAAFEAYFKAQDMFGVPAAQDISYTKLLTLDLSTVAPSLAGPKRPQDRIEIGNVKSTFIDLFSKPVAENGFNQPAEKLQQTFTTSTGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTPDLNEVITSNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYALAGTVTRDLMTEPVGRGKNGDIWLGDIWPTTEEVEALLKYALDPKAFEANYGQVKSNPGKLWENIKGVTGETYNWPDSTYIAEPPFFEGFGMTPGAMPTVKNARALGVFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKNLMIPARPDGSRFEGGETLFQPTGEQMSIYDAAMKYVAAGTPTVVFGGEEYGTGSSRDWAAKGTQLLGVKAVITRSFERIHRSNLVGMGVLPLQFKGSDSVQSLGITGEETYDISGLENGIKPMQDVTLTITRKDGSKQDVTLLLRIDTPIEVDYYQHGGILPFVLRQLLAA
>NZ_CP009448.1|WP_006387140.1|4310079_4311009_+|LysR-family-transcriptional-regulator
MTTPPVLDLNLIQLFVTIVEAGTLSEAALRQGVTRSHVSRNLQKLERAFGAQLIRRTTRRLELTHEGSVLYDHGARMAREVESARHALQKLGAEPTGHVRLSLPTGLGELDMLRPLLVRFALEHPSLSLRVLFSNRVSDLISSEIDVALRAISVPPQDYVARELGRIKWHLCAAPEYLARMGMPAHPRDLGRFDFLGPPGPRPQATLRLRGKGQPHEVKLATRLQSEYFPFLAQAAREGAGVALLPAYIVRPDLEAGRLLQVLPAYQAEGPGDKLYILTSPTPYPSSAQRALVDFLKRELEPLLRTFLA
>NZ_CP009448.1|WP_006387141.1|4309074_4309962_-|oxidoreductase
MFRADLFQGQRILITGGGTGLGYAMARQLAALGATVHLCGRRLAVLEQAAQALRGESGGQVHVHPVDIRDAGAVDAMVARIWDQHGGLDALVNNAAGNFISPTEKLSERGFNAIADTVFRGTFYMTQAVGKRWIGSGASGAVVSIVVTWVWTGSPFVVPSAMSKAGIDAMTKSLAVEWGRRGIRLNAIAPGVIPTEGASARLRPNDSGTDALVKQNPMQRLGQGQDIGELAAFLLAPGNDWINGQTIALDGGDYLANGAYFKQYFDWSDDDWAAARAAIEARTAADKAQRSAGQA
>NZ_CP009448.1|WP_080747578.1|4307566_4309078_-|long-chain-fatty-acid--CoA-ligase
MSASVTQGAGRIIAGDCQLDRAALMRRGEQVAAGLAAMGIGQGDVVAVLLRNGMPYLEIIQACKRLGCYYCPINWHYTPDEVAYLVRDSGARLLIAEEDLWQAARAALPADLPSRRVGAAAVSEDYASWREAQAPYDGPVVAPRGHMAYTSGTTGRPKGVVRAPFPLDQLAQRLAAVEAVVEQAYGLRSGCRALLPAPVYHSAPSVFAQVALRVCETLVLAPRFDPLEVLRLIERHRIDTVYLVPIMYVRLLKLDPAQRAAFDLSSLRFVASTGAPCAPALKRAMIDWLGPVIHETYASSEAGMVTVIDSHEALARPGSAGRPIGGAQIRIYGDDGALCAPGQIGRIHVRQPAYADFTYRNNPEARSRIERDGLIGLGDLGYLDDDGYLFVCDRESDMVISGGVNIYPAEIEHHLTQYPGVADCAVFGVPDDEFGERLLALVQPAADTALAPEEVLRWLSTRVARYKVPRELRLRQTLPRDDNGKIAKRRLRDAFWAERDRKV
>NZ_CP009448.1|WP_006387144.1|4306525_4307509_-|tripartite-tricarboxylate-transporter-substrate-binding-protein
MFMKNSGIGRAAAALLLCMAAASPALAAFPERPVKLVVPYTPGGAADLLSRVLAERLSQELAQPVVVENKPGANTMIAATQVARAQPDGYTLFLASNASMVLNPMLYRKISYDAQRDFRVLSVVAELPLVVVANNSVPASTLAQFVDYARARPGKLNYASVGIGNPLQLATELLKSRTGIDVAHVPYNGSAPALSSLMANDTQLMVDVISTSLPLVRENKIKALAVTGAQRLPVLPDVPTVAESGFAGFRAATWFGVAVPRGTPPAEADRLREAVAAVMRQADFRDRFQAQGLVIQAPRGQAEVDAYLAEDRERWNGVIQANHIRLD
>NZ_CP009448.1|WP_006387145.1|4305606_4306515_+|hypothetical-protein
MHSYIHHLDDLLLFTEVVEKGGFSAAARVLNMQRSKLSRRVAELEARLGLRLLQRNTRRVSLTPMGEQIYVHALAMAREARSAFDLAAAMGDTPSGLLRMTAPSALAVTLLGELVARFCLQHPGVRVLLDTRDQVIDLVGEGYDLAFRAQGASLTDSRLVARELAPVPLILVAAPAMARAAPRHPRDLNALPLLAHATQDSPQSWHFVGPAGEAESIEFRPRCLSSNLAALREMARAGLGVALLPHYLCAGSLAKGDLAQLLPAWRAAPARIYAVMPARRGAPLALRRFLDFAAAEMPALLA
>NZ_CP009448.1|WP_080747577.1|4304535_4305411_-|pirin-family-protein
MSPLVLVDHFIMTGPAVAPHPHAGISTVTLLLEDTQGGLRIRDSLDNEHEARAGDLHWTVAGRGIVHGHELVGAARLNGLRLYVNLPARLKSMPPSATLVRGWEMPVLQSDAGRVRVVSGRYDGWDAPLATPEPLLILDGWLRPGASRLVPLPAGWNAWLYAAQGELGVRARHETTPPPRPPVEAAPVIPAARFRPAGRAATTGRRAADPDFAVLPPGAALTATADRDGFLQLLAAGAPAHFILVAGAAIDEPVIQRGPFVMTDARALAQAVAAYEAGDFGQLRQESGVPG
>NZ_CP009448.1|WP_006387147.1|4302049_4304251_-|TonB-dependent-siderophore-receptor
MKIRTLACVVAALPYTAIVHAQSAAPAADGSVVSMEAIKVEASADASAGGLAQPYAGGQVARGGRVGVLGTQDIMSTPFSVTSYTNELIQDKQARSVGDVLQNDAGVRVARGFGNFQESYFIRGFILSSDDVAYNGLYSLLPRQYIATELFERVEVLRGASAFLTGAAPSGGGIGGVINLVPKRAPNEPLTRFTTGVSSGGQFSVSTDIARRFGPDDSTGIRLNVANRSGDTGIDDEHSRTSLVSLGLDWRSADTRLSADIGWQENKLKRARPNVTLRGVTSVPDAPDASSNYAQPWSYSNERDVFGTVRAEHDFSDKLTGWAAFGMRRSDEANSLGNVTVTNGSTGDGNFYRFDNTREDSVNTGELGLRAKVRTGPVGHEFVASASFFDLKKKNAYVMDYLNTFPTNIYDPVSYDRPAYGSKALFGNDLDDPALQGRTRLSSYAFGDTMSFLDDKVLLTLGIRHQRLSQRDYAYNTGKEQSAYDASRNSPAAGIVFKVAPSVSLYANYIEALVAGDTAPQTANGKPVPNAGQSLQPYVSKQKEIGVKYDGGGLGAGLALFSTDKPRAAYNASNAFTASGKDRHQGIELTVFGEPVNRVRVLGGMTFLDAKQRSTGNSAIDGNRVIGVPRFQANLGAEWDIPGVQGLTVDGRVVYTGASYADDANTLKVPGWTRFDAGLRYMMDVDGHVVTLRARVENIANRNYWSSVGGYPGNGYLVLGGPRTFSLSASMDF
>NZ_CP009448.1|WP_006387148.1|4301220_4301988_+|NAD(P)-dependent-oxidoreductase
MSARFQDQVIIVTGAVGGIGSAIVEGFLAEGGKVGLIDFNSQGGQAYEKELKKRGHAVSFVHADVSHFDQCQAAYERITRDLGPATILVNNVGISPKTDGRALKVWEMTPGEWDKVVAVNLNSVFYMTHLATPHMVRQRQGRVINMSSVAGKAYCDIVAAHYAATKAALLGLTRHWAAELGEHDVTVNGLAPGRISTPLLKSVPKEINDAVAEVTALRRLGTPEEVADACLFFASDQARFVTGQVLDVAGGWLMT
>NZ_CP009448.1|WP_006387149.1|4300228_4301224_+|NAD(P)H-quinone-oxidoreductase
MSLRCTFIDHGTGGAPDCLRLAEREMAAPAGRQVLIEVVYAGVNRPDVLQRSGSYPPPPGASPYLGLEVAGTIVAVGPDATRWQVGDRVCALTPGGGYAQYCLADERHCLPVPRGLDLLSAAAIPENYFTVWTNVFERARLAAGEKFLVHGGSSGIGLTAIQLARAFGAEVWTTVGNQEKAEACLKAGAHHAVLYRDTDFEADIRQATGGQGVDVILDMVGGAYINKNIRLLAVNGRLVQIAFLEGSKAEIDALPIMTKRLSFTGSTLRPRSDEDKGAIAQALADKVLPLMEQGRCLPLIHQVFPLEQAAQAHALMESSKHIGKIMLKVRA
>NZ_CP009448.1|WP_006387137.1|4315304_4316216_-|LysR-family-transcriptional-regulator
MRLVQLMDLNLLVALDALLAEGSVTGAAERLQLSVPAMSRTLERIRRMMGDPLFVRAGRGLVPTPRAEALREPVRALVAQARELLAQDAAFDLKTLRRVFTIRADDGAVSTLGPALLDTLAKEAPRVTVRFISQGKQDVLSLREGAIDLDIGVIEDMGPEIVRQRLFPDRFVAVFRPANPLARHRKLTPERFARARHATVSRRGVLSGPVDIELGKVGLARHISAVTHSFAEALAITRKSDLVATVPDLLTLHLRDDLQMRALPFDTPAVTISQAWHPRFNEDPAHRAIRQMVHRISLAISGR
>NZ_CP009448.1|WP_080747579.1|4316265_4317747_+|hypothetical-protein
MAASSTRKHAMIHSTRYRPDARPARRMRLRHAPLAAALAALVAVAGCASHDGLRPAGKPLDLAALDAGQDIAAAVRDTADDAAPWWRAWGDDQLDRLMADALRQAPGVRAAQARLGQAEAVFGSVAAKRQPTLDGSATITADRYPGHYTYGAPYADNTGGSGSLLASLRLRLDIWGKWRALADAARLDAEGAALAHADAQLALQQGIAAAYLRLDAAFRLHELARQQRERQRQALELHQTRRQAGLGSDAPVADARGRLARMDAEVERLDREIARQRHALAALAGQAPGYGDALRRPRLARLRPDVLAQRKRLDAADRRIEAAKAEFYPDIDLKAFAGLQSLGLSHLLQGNSLAAGIGPALTLPIFDGGRLRAGLRDRIAGYDLAVADYDAAVVRALQEVADGLAGMAQARARRDAARVSLREAGTLARLQAVRASRGLSARQDEIDTDLERLRADSELAAADLDLGLARTALAGALGGRWSPSQSSDNEALK
>NZ_CP009448.1|WP_052102908.1|4317797_4318880_+|hemolysin-D
MLAGGATLLAGAGWAAWTFLAGAATQTTDNAYVNGHVVAITPQVGGAVSAIWADNAARISAAQTRVEVDPADTQIALAGARADLARARRRVQALFASRDQAGAEVARRQAELDRAQADVSARRGIAAQGAITSEEARHAADALNAARAALAVAQAAERAAQAQVDGVTPDTHPDVTLAQARLRAAALDAQRTTIRAPVGGMVAQRSVQLGKHVAIGDKLMAVVPLDQMWIDANFKEIQLAGICPGQPAVVTVDAHGAKVRYRGRVGDVMAGSGSAFALLPSQNATGNWIKVVQRVPVRINLDPKELADHPLRIGLSAEVTVDTARCDPAQAGAARGETTDIYRQQRQAADTLAQAGQGLQ
>NZ_CP009448.1|WP_038504106.1|4318879_4320409_+|MFS-transporter
MSAAPRPIEPMTGLPRVVAAVAISLASFMAVVDITIANVSVPTISGNLGVSPEIGEWAITFFAIANSICIPLTGWLSRRLGQVRLFVLSVAAFTLASVLCGVAQNFESLLAFRVLQGMVSGPIVPLSQALLVAIFPPDKRTLALSMWAMTNMAGPVAGPVLGGWLTDDFSWPWIFLVNAPVGIAVVAVTATMFRGRDTPSTRLPVDLRGLILLAVAIGCLQLTLDRGRTLDWFASPFIVTTALLSALGFVFLVIWELGEAHPIVDLSLFRHRNFAMGTLAVAVGFGLYFAALVLIPLWLQTDMRYTATWAGLATAPMGVFGILLAPLLGRWVQRGDARVFASLAFVAWSLVGWWRASMTTDVGVGLISLACLLQGIGIGLFLTPLVSLSLAGLPPERIAAASGLQTAIRMMAGSLVASLASTYWDERSRYYQNVLVDSATPARPAVQDTLNARAGAGLDEPQSWGVIWNGLKTQADMLALNDFFLWSSLAFALSIALVWLARHPRAAKA
>NZ_CP009448.1|WP_038504108.1|4320444_4321149_+|siderophore-interacting-protein
MQPFSLPRRDVPCIVLRARDVARDMRRLTLGGPELSAWLARPGVDQPGAWVKVFPPGVPGRAYTLRGIDFEASSVEIDFVVHGDAPGTVSEWARRARPGDAVSIAGPRDGGFSLLADTRWVWLGADASAWPAASRIIESLPGGIQVLGVRHPAGDDDWPAIARARAPQWAARSLPPGGDEPSAPAPDGPGQVWLAGQAAWVKAWRAHWLQRLRFDPARLSAKGYWKAGEQDYKE
>NZ_CP009448.1|WP_006384576.1|4321184_4322075_+|LysR-family-transcriptional-regulator
MKKELDRMRDMALFVQVAALGSLTRAAESTGVPASTLSRRISEFESQIGVKLLHRSTRRLALTDIGQRYLERITDVVDRARAISGELEEEMGRPTGHLRVCAPVDFNAYFPEAALADYCASHPGVRFELHCSAQLPDLATEPYDICIATTEPPQASRMVRRRIGMAEYQLYAAPAYLRAYGVPAHPAELARHRCVVMPDSESGLALTDGNASAQVALAPLLVLNNQLAVENLLRDGLGIGPLTRGRADALVREGALAPVLPGWTLPPRPILALTASRALPARVRGFIDLLVARVVT
>NZ_CP009448.1|WP_076468376.1|4322118_4322892_-|dioxygenase
MRWPTLFVSHGSPMLAVEPGATGPALAAWSRSLGRKPGAILVVSPHWMGHGLALSTRDRQVAWHDFGGFPPELYTLQYAAPGSPELAARVQALLAEGGIAADRDPRRPLDHGAWVPLRYLYPEVDVPVVQLSLDMGRDAAGQLELGRALAPLRDEDVLIIGSGSLTHNLRDVRMPQDAQPAPYVPAFQAWYVDRLAAHDVPALLDWQARAPGAAQAHPHDDHLMPLYVALGAGGARATRLTDEISYGALAMDAYAFD
>NZ_CP009448.1|WP_006387133.1|4323136_4324339_+|DUF2863-domain-containing-protein
MARSRSQSAPRLTRDATRLITLAQSLNRSGSRVEDVYWENQLGEAIPKLLKAGQDAPLEAALDHLAQGDVGAYEVLIEQAETLSESMKIDKNGVRYDILLIVAPVVAWTRYAIPTGPVPASAQQALLAQLHGHVLSSQARSALMPHLVSVDQMPRTFSETWQWLQRLGSQALGAETTKPALNTEVETANMLADTRYIVAAVAVPEFAPVFRWQEQIGEADASRDACLAQWAAQAQPTLAGLLPGCGFEALLPDAYYVSNREADRRVRPLSLRAAISWLEGAVSLDASQLRAVIAGCGESRVDEYRVSFTARNSNDVYYGCVWPLYGREEDLPADEGQPDVVDEIAALLKEYGVSDVRRIPGVLPPEYCEDCGAPYFPNPLGELVHAELPEDAEAAPAKFH
>NZ_CP009448.1|WP_024069800.1|4324348_4325464_+|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP
MQADIFCRVVDNYGDIGVCWRLARRLAHGHGWEVRLWVDDLASFARIQPGIDAGLARQAFNGVDIVRWSDAPDPALGARDVVIEAFACDPPEPFLDSMRQRHPAWINLEYLSAEAWVESCHGLPSQRPDGLVKHFYFPGFTPATGGLLREPGLSAERDAFQADTAAQDTFLRGLGVAEAHLSLRHNGARTMSLFCYPDAPVDGLARALAADPRPALLLAPEGVAPGLEAACAMPGGPAVARLPFVAQPDFDRVLWCADLNFVRGEDSFVRAAWAARPLVWQIYPQDENIHLEKLDAWLARYPAPETATALMRAWNQPGAGAATAAALAAALAPPAWQAWARAARDWDAAQAARPDLAENLAGFCAELAKKR
>NZ_CP009448.1|WP_006220534.1|4325670_4326231_+|elongation-factor-P
MKTAQELRVGNVVMVGKDPLVVQKAEYNKSGRNAAVVKLKFKNLLTASASESVYKADEKFEVVQLDRKECTYSYFGDPMYVFMDEEYNQYEIEAESMGDALNYLEEAMPVEVVFYDGRAISVELPTTIVREITYTEPAVRGDTSGKVTKPAKINTGYELNVPLFCAIGDKIEIDTRTNEYRSRVNN

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Crispr_ID: NZ_CP009448_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP009448_3

5870980-5871087

Orphan

Consensus_repeat	Method
GAAGGCGGCTTCCGTGGCGGCGACCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP009448_3

>merge|NZ_CP009448|3|5870980-5871087|CRISPRCasFinder
GAAGGCGGCTTCCGTGGCGGCGACCGCGATTCGCGTCCGAGCTTCAGCGATCGCCCCAGCTTTGGCGACCGTCCGCAGCGCGAAGGCGGCTTCCGCGGCGGCGACCGC

>NZ_CP009448|3|3|5870980-5871087|CRISPRCasFinder
GAAGGCGGCTTCCGTGGCGGCGACCGC	GATTCGCGTCCGAGCTTCAGCGATCGCCCCAGCTTTGGCGACCGTCCGCAGCGC
GAAGGCGGCTTCCGCGGCGGCGACCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009448.1\|WP_006389812.1\|5856348_5857011_+\|thiaminase-II	unknown	unknown	gnl\|CDD\|381700
NZ_CP009448.1\|WP_038504578.1\|5854402_5855101_-\|cell-wall-hydrolase	unknown	unknown	gnl\|CDD\|376559
NZ_CP009448.1\|WP_006389807.1\|5868367_5869129_+\|uracil-DNA-glycosylase	unknown	unknown	gnl\|CDD\|235376
NZ_CP009448.1\|WP_038505224.1\|5873565_5875692_-\|lytic-transglycosylase	unknown	unknown	gnl\|CDD\|381604
NZ_CP009448.1\|WP_006389808.1\|5866356_5868093_-\|ShlB/FhaC/HecB-family-hemolysin-secretion/activation-protein	unknown	unknown	gnl\|CDD\|225387
NZ_CP009448.1\|WP_006389786.1\|5881197_5882196_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|270294
NZ_CP009448.1\|WP_006389818.1\|5852145_5852994_-\|DUF1311-domain-containing-protein	unknown	unknown	gnl\|CDD\|226278
NZ_CP009448.1\|WP_006389819.1\|5851677_5852079_+\|DUF488-domain-containing-protein	unknown	unknown	gnl\|CDD\|225730
NZ_CP009448.1\|WP_006389784.1\|5883340_5883676_-\|phage-holin-family-protein	unknown	unknown	gnl\|CDD\|377198
NZ_CP009448.1\|WP_080564321.1\|5858105_5858309_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP009448.1\|WP_035184374.1\|5875911_5876586_+\|5-formyltetrahydrofolate-cyclo-ligase	unknown	unknown	gnl\|CDD\|274270
NZ_CP009448.1\|WP_006389790.1\|5876888_5878319_+\|circularly-permuted-type-2-ATP-grasp-protein	unknown	unknown	gnl\|CDD\|225190
NZ_CP009448.1\|WP_038504588.1\|5871271_5872453_+\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|224481
NZ_CP009448.1\|WP_006389787.1\|5880180_5881044_+\|proteasome-type-protease	unknown	unknown	gnl\|CDD\|239734
NZ_CP009448.1\|WP_038505221.1\|5853024_5854200_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226419
NZ_CP009448.1\|WP_006389813.1\|5855472_5856258_+\|3-hydroxybutyrate-dehydrogenase	unknown	unknown	gnl\|CDD\|184025
NZ_CP009448.1\|WP_006389788.1\|5879321_5880125_+\|transglutaminase-family-protein	unknown	unknown	gnl\|CDD\|224224
NZ_CP009448.1\|WP_006389811.1\|5857050_5857398_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379331
NZ_CP009448.1\|WP_006389789.1\|5878321_5879308_+\|alpha-E-domain-containing-protein	unknown	unknown	gnl\|CDD\|377234
NZ_CP009448.1\|WP_006389803.1\|5872465_5873569_-\|tRNA-CCA-pyrophosphorylase	unknown	unknown	gnl\|CDD\|139469

Protein	Function_ID	Function_description	E-value
NZ_CP009448.1\|WP_006389812.1\|5856348_5857011_+\|thiaminase-II	gnl\|CDD\|381700	cd19365, TenA_C-like, uncharacterized TenA_C proteins. This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins.	4.99437e-95
NZ_CP009448.1\|WP_038504578.1\|5854402_5855101_-\|cell-wall-hydrolase	gnl\|CDD\|376559	pfam01520, Amidase_3, N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.	2.87474e-40
NZ_CP009448.1\|WP_006389807.1\|5868367_5869129_+\|uracil-DNA-glycosylase	gnl\|CDD\|235376	PRK05254, PRK05254, uracil-DNA glycosylase; Provisional.	1.7219e-112
NZ_CP009448.1\|WP_038505224.1\|5873565_5875692_-\|lytic-transglycosylase	gnl\|CDD\|381604	cd13401, Slt70-like, 70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.	1.96397e-60
NZ_CP009448.1\|WP_006389808.1\|5866356_5868093_-\|ShlB/FhaC/HecB-family-hemolysin-secretion/activation-protein	gnl\|CDD\|225387	COG2831, FhaC, Hemolysin activation/secretion protein [Intracellular trafficking and secretion].	4.01038e-129
NZ_CP009448.1\|WP_006389786.1\|5881197_5882196_+\|hypothetical-protein	gnl\|CDD\|270294	cd13576, PBP2_BugD_Asp, Aspartic acid transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.	1.6032e-132
NZ_CP009448.1\|WP_006389818.1\|5852145_5852994_-\|DUF1311-domain-containing-protein	gnl\|CDD\|226278	COG3755, COG3755, Uncharacterized protein conserved in bacteria [Function unknown].	1.75398e-08
NZ_CP009448.1\|WP_006389819.1\|5851677_5852079_+\|DUF488-domain-containing-protein	gnl\|CDD\|225730	COG3189, COG3189, Uncharacterized conserved protein [Function unknown].	4.14397e-43
NZ_CP009448.1\|WP_006389784.1\|5883340_5883676_-\|phage-holin-family-protein	gnl\|CDD\|377198	pfam04020, Phage_holin_4_2, Mycobacterial 4 TMS phage holin, superfamily IV. These proteins are predicted transmembrane proteins with probably four transmembrane spans. The 1.E.40 is represented by the mycobacterial 4 phage holin, but it also contains many cyanobacterial. proteobacterial and firmicute proteins. Holins are encoded within the genomes of Gram-positive and Gram-negative bacteria as well as in those of the bacteriophage of these organisms. The primary function of holins appears to be transport of murein hydrolases across the cytoplasmic membrane to the cell wall where these enzymes hydrolyze the cell wall polymer as a prelude to cell lysis. When chromosomally encoded the enzymes are therefore autolysins. Holins may also facilitate leakage of electrolytes and nutrients from the cell cytoplasm, thereby promoting cell death. Some may catalyze export of nucleases.	2.02938e-20
NZ_CP009448.1\|WP_035184374.1\|5875911_5876586_+\|5-formyltetrahydrofolate-cyclo-ligase	gnl\|CDD\|274270	TIGR02727, Uncharacterized_protein_YqgN, 5,10-methenyltetrahydrofolate synthetase. This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism].	4.00284e-42
NZ_CP009448.1\|WP_006389790.1\|5876888_5878319_+\|circularly-permuted-type-2-ATP-grasp-protein	gnl\|CDD\|225190	COG2308, COG2308, Uncharacterized conserved protein [Function unknown].	0
NZ_CP009448.1\|WP_038504588.1\|5871271_5872453_+\|SAM-dependent-methyltransferase	gnl\|CDD\|224481	COG1565, COG1565, Uncharacterized conserved protein [Function unknown].	1.68132e-105
NZ_CP009448.1\|WP_006389787.1\|5880180_5881044_+\|proteasome-type-protease	gnl\|CDD\|239734	cd03765, proteasome_beta_bacterial, Bacterial proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.	7.6888e-137
NZ_CP009448.1\|WP_038505221.1\|5853024_5854200_-\|hypothetical-protein	gnl\|CDD\|226419	COG3904, COG3904, Predicted periplasmic protein [Function unknown].	1.28926e-12
NZ_CP009448.1\|WP_006389813.1\|5855472_5856258_+\|3-hydroxybutyrate-dehydrogenase	gnl\|CDD\|184025	PRK13394, PRK13394, 3-hydroxybutyrate dehydrogenase; Provisional.	7.48374e-158
NZ_CP009448.1\|WP_006389788.1\|5879321_5880125_+\|transglutaminase-family-protein	gnl\|CDD\|224224	COG1305, COG1305, Transglutaminase-like enzymes, putative cysteine proteases [Amino acid transport and metabolism].	8.19385e-43
NZ_CP009448.1\|WP_006389811.1\|5857050_5857398_-\|hypothetical-protein	gnl\|CDD\|379331	pfam13682, CZB, Chemoreceptor zinc-binding domain. The chemoreceptor zinc-binding domain (CZB) is found in bacterial signal transduction proteins - most frequently receptors involved in chemotaxis and motility, but also in c-di-GMP signalling and nitrate/nitrite-sensing. Originally discovered in the cytoplasmic chemoreceptor TlpD from Helicobacter pylori, it is often found C-terminal to the MCPsignal domain in cytoplasmic chemoreceptor proteins. The CZB domain contains a core sequence motif, Hxx[WFYL]x21-28Cx[LFMVI]Gx[WFLVI]x18-27HxxxH. The highly-conserved H-C-H-H residues of this motif are believed to coordinate zinc; mutating the latter two histidines of the motif to alanines abolishes Zn binding. This domain binds zinc with high affinity, with a Kd in the femtomolar range. This domain has been shown in E. coli to be a zinc sensor that regulates the catalytic activity of pfam00990.	3.50112e-10
NZ_CP009448.1\|WP_006389789.1\|5878321_5879308_+\|alpha-E-domain-containing-protein	gnl\|CDD\|377234	pfam04168, Alpha-E, A predicted alpha-helical domain with a conserved ER motif. An uncharacterized alpha helical domain containing a highly conserved ER motif and typically found as a tandem duplication. Contextual analysis suggests that it functions in a distinct peptide synthesis/modification system comprising of a transglutaminase, a peptidase of the NTN-hydrolase superfamily, an active and inactive circularly permuted ATP-grasp domains and a transglutaminase fused N-terminal to a circularly permuted COOH-NH2 ligase domain.	3.75373e-115
NZ_CP009448.1\|WP_006389803.1\|5872465_5873569_-\|tRNA-CCA-pyrophosphorylase	gnl\|CDD\|139469	PRK13297, PRK13297, tRNA CCA-pyrophosphorylase; Provisional.	0

>NZ_CP009448.1|WP_006389807.1|5868367_5869129_+|uracil-DNA-glycosylase
MPIDNRLIPSALATQTAQLPAAWQAALQAPRVATALQAVTAHVEKRLAEGAVIYPATPFRALHGLAPSDVRVVILGQDPYHGPGQAQGLAFSVPDDCKRPPSLRNIFNEIAQEYPGTPLPAGNDLTPWAAQGVLLLNTALTVEDGQPASHAKRGWETVTDALIALVAQDPSPKVFMLWGAHAQAKQALLPHDSGHLVLMANHPSPLSARRPPVPFLGCGHFLATNRWLSDQGKNPIDWKLDKKIIPAQGEFGL
>NZ_CP009448.1|WP_006389808.1|5866356_5868093_-|ShlB/FhaC/HecB-family-hemolysin-secretion/activation-protein
MHTIVPRSRLRQRLLPCLALCVSSIASLTIPPGLAAQSLPAEAATRASDIQRRQEQELDAQRARAAERPDVLSAPSTGAGEGPLVFPVESPCFTLDKVVWDGSPPPAALRRDSEAALGRCVGGRGLQALQAHLMARLIDRGLITARVLVPEQSLASGTLTLRYVPGRIAGVKSDGAPGWWRTALPTWPGGEVNQRDLDQALENIRRLAGQADASIDVAPGPELGDSDIIIKPGTGKRWHAYVGGDNAGMESTGKNQVNAGLTLDSPLFLYDQLSVSWNSNADLRNNDAGSRAASVNYSIPFGYWTLFAGASKSRYRQTVAGFEEPIVYGGTSKQIEAGVSVVPYRGASYKGTAMLKFLRKRANSTLNDIDIEVQRRDVVGYEFSYGHRQYIDQMVLDLGGGVRGTLPQFSDQPGYVYGDPDWNGRSTILTANAGLYLPFKVAGQQLAYQANWQIQHAKTPIVPADYFTIGNRYAVRGFDGQMTLAAEDGWTLRNDLSLNLGNLGQQLYTGLDAGRVGGPSAEYLASRTLVGAVAGLRGRIAMPYVNASYDLSAGWPLKKPDNLKTQSTVFAATLMFEF
>NZ_CP009448.1|WP_080564321.1|5858105_5858309_-|hypothetical-protein
MSIVRRGVVVSGEYSGWKILVADDRDGDTGGYYLYLKRSDTEGFDCWFEREAELQTQLADFEVKWIG
>NZ_CP009448.1|WP_006389811.1|5857050_5857398_-|hypothetical-protein
MNLDESIQKHAEWKLKFRSAISRKEQMDAETIGKDNCCQLGVWLYGEGKLKYSAKPEFGAIVQKHKAFHAEAGKIARLINSNQYEQAEKEMGTGTPYSQASSAVGAAIIAFKRHL
>NZ_CP009448.1|WP_006389812.1|5856348_5857011_+|thiaminase-II
MSFSTDAWARNAALYEKTRTMPFNQELASGQLSEQAFRHYMIQDAHYLLAFGRALAVAAAKADHADGVVQFADAAKNAVVVERSLHEGFMKQFGIDAETFASTPLSPASHHYTSFLIATAWSAPYPVALAALLPCFWIYAEIGRDIHSRATRPNPYGAWIDTYAGEEFHALVREVIASVDQAAEKASPQTRNEMHRAYTHAAQLEWMFWDSAYRLGEWAV
>NZ_CP009448.1|WP_006389813.1|5855472_5856258_+|3-hydroxybutyrate-dehydrogenase
MSNLNGKVAVVTGAASGIGKEIALTLSRAGAAVAIADLNQAGADAVAREIEQAGGKAMGVAMDVTNEDAVNQGIDRVAAAYGSIDILISNAGIQIVNPIENFAFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVAAKHALLGLARVLAKEGAKHNVRSHVICPGFVRTPLVEKQIPEQAKELGISEEDVVKKVMLGDTVDGVFTTVEDVAQTALFLSAFPSAAFTGQSFVVSHGWYMQ
>NZ_CP009448.1|WP_038504578.1|5854402_5855101_-|cell-wall-hydrolase
MGGKMAGRWARRIAASVLGLAAGLAQAAHVVVDTGHTPRQPGATGASGRVEYLYNLDLSGAVAADLQASGDRVTRVSADGAEVPLGRRTRIAPGADFFLSIHHDSMQQHYIDAGRQREFAGFSIFVSQLNPRYEDSLRCAKAIGEALLAAGEKPSLYHAEPIAGENRPLLDPRLGVHRYDGLAVLKTATMPAVLVGAGGIVNPDEEARLAKPETIQRLARAIADGVQACQAR
>NZ_CP009448.1|WP_038505221.1|5853024_5854200_-|hypothetical-protein
MSLALTLMGVSMSPAQAQAPAQQKEEPERYGPFFYLPSEPNLLIYVGAVSANDLLHMKKALREHPTISTLILQNNGGGLVHIGLVVAEEVYERGLNTYIPKDSYCASACAFVFFAGRQRLAEGRLGVHQITAPEMTGEQAQFGVSDIVTTLPKYGVSADVLGIMFSTPSKDMYFFSPQEIAKYGINRTGNVKTASSEPQQGGAPRTVPAAGPATATAPQAQAPDDDTRLPPRKPAAPNAAPAPSGPPPVTNPYMTKNPPAPAPLSDEQRAINAATLMIQAGSGTNEEAMNFTREFYADTVDYFKKSRPKSEILADKTAYFARWPVRRFVVDQNSLKAKCQDQMCMVKGLYDFKVSSPERGKTATGTSNFTYVLDLRNRYRIVMEDSEVVSR
>NZ_CP009448.1|WP_006389818.1|5852145_5852994_-|DUF1311-domain-containing-protein
MGFTNRAARLLCLAGLGALSAPAWAIDCHKAGTPAEKLICSDRGAVAADAELNRAYAALLKQAPDAQIRAMLVDSQRRWVEARNMRLEGLVSDPESLPDEKTPGAVAADLIRSRASEFKERGKGDSLPRLIRVALSQREFRKQFTGGPYSGYETSCDVLPPDYKYYACFSTRHYQNDDRVCSTEEYWATGSVYVQRYVAKVVDNKPVPVASCSYNGNDASCPGSIDDDARWNTGPKVKAPTYSSKPLPQLDGEVDDSDDHAWIKACLTDSGFPLSNPTKAGG
>NZ_CP009448.1|WP_006389819.1|5851677_5852079_+|DUF488-domain-containing-protein
MKPSAISVQRVYEGIGPDGHYRALVDRMWPRGLRRADLALDEWAKDLAPSSELRKWFCHVDERWDTFREKYLAELAEPEQQARMDALLQAAGARPVTLLYGARDTEHNQAVVLRDALQEYARHHRKRLARAPG
>NZ_CP009448.1|WP_038504588.1|5871271_5872453_+|SAM-dependent-methyltransferase
MQRPAPANLPPLSPAAQAQSAAAAAHLRAAIAAASGWLPFDHWMAEALYAPGLGYYAAGNVKLAEADARAPAGDFVTAPQLTPLFARTLARQVAQVLRQTDTQTVLEFGAGTGALAEGVLRELDAQGLQETQYLILEISADLRARQAERLAPFGERVRWLDALPERFRGCVLANEVLDAMPVSLFRWSDDGVVLERGVTLDPAQGFVWEDRPAPRRLAEAVAARMPALPGYVSEINLQAEAWIDGMSGWLEQGAALLVDYGFPQGEYYHPQRAGGTLMCHLRHHAHGDPFTAPGLQDITAHVDFTAMADAAQAAGLQVLGYTSQARFLMNAGLMELLAQLDPTDARTYAQAVAPVQKLLSEAEMGELFKVLAVGRGITQPLIGFARGDRLGKL
>NZ_CP009448.1|WP_006389803.1|5872465_5873569_-|tRNA-CCA-pyrophosphorylase
MTADVATQGLQAYIVGGAVRDALLGLTPGDHDWVVVGATPEDMARRGFIPVGGDFPVFLHPVTKEEYALARTERKSGRGYKGFTFYTGTDVTLEEDLRRRDLTVNAIAQKQDGELVDPLGGAADVRARVFRHVGEAFQEDPVRILRLARFAARFADFSVAPETMALCRQMVEAGEADALVPERVWKEVSRGLMAAAPSRMLDVLRQSGALERVMPELTGSEETGGDVDRAAARKLSLPGRYALLCRLSPGREALGRRLRVPTECNDYARLLPDMLTGLDAAQAAGADPADAQLALMERVDALRKPERFLDLLAAAAVLRPVDGNAWRDRAEAVRGVDAGAIARSCAGDPARIKQSLREARLQRLRAA
>NZ_CP009448.1|WP_038505224.1|5873565_5875692_-|lytic-transglycosylase
MAAVHGPQSGRYQKTAMKSPRTADARAGLRRWLPLLALFTAACAPVDAQQRTASVNTQPQPAAQAPQPAIAVPPAVLAGLPPTAETPALAAVVAAREAMNRKQWSILGALVPQAKSDPLGMYPEYWLLRYQLWSPPAGGRPNAELQKFINSNGDAYLADRLRADWLLAAARSGDFETVRKLAPVKNSNAQVECAILNAKHMTGQRATAAQAMAVFAPGSACWTLYDQLVADNVLGWDQLEPQLRDAIEANKTTDARKFVQYMFEPRDQKTYDVLIKDPMRWLTRQDRLPVGRNEKELVTIALARLARSDINVADSYLRREWAKSMAKSNLAWIRGQYALVAALNLDSRADDWYHEAGHIRMTEYNAGWKVRAALRQPKIDWKWVIESIDQMPAAQQQDPSWIYWKARGMAATGRREQANAAYASIADRFDFYGQLAAEELGRRITVPPRPAPISDSEIAEARANPGLRRAVQLFRLGWRQEAVPEWNFALRGMSDRQLLAAAELARAENIYDRVVNTSDRTEKEFDFSQRFIAPFEGRVTAKANAIALDPAWVYGLIRQESRFIMDARSHVGASGLMQLMPATAKWVAGKIGMSNFTPDSVNDFDTNTELGTNYLNMVLRDLNGSQMLASAGYNAGPRRPHNWRSTFNHPVEGAIFAETIPFNETRTYVKNVMSNSVYYAAMFSGQPQSLKERLGNVVPLGAESTTLP
>NZ_CP009448.1|WP_035184374.1|5875911_5876586_+|5-formyltetrahydrofolate-cyclo-ligase
MTTQNTPEDTASQLRTRLRKLRAELPEDQRSRGGLLMRARLFTWLNVARDEAVRAGRRAPAVVAAFWPMEDEPDLRPLLEQWTENGVTVALPVVRERNAPLAFLPWTPDAELRAGPYGIQEPARGAEVLPDVLLVPTLGYTESADRLGYGGGYYDRTLAALRERGHAFTTIGVAWSCGELDPGYEPAAHDFRLDAVITPDGWVPHAPQEQPGQGGTTVQRYTLR
>NZ_CP009448.1|WP_006389790.1|5876888_5878319_+|circularly-permuted-type-2-ATP-grasp-protein
MKDRSSRPAAYDEMRDSAGGIRSHYQAFERWHQEQSAEAMAARRLEADLSFRRVGITFSVAGDAAGTERLIPFDMIPRIIPADEWRRLEAGLKQRVRALNMFIHDIYHGHEIVRAGVVPAGQVFLNAQYRPEMQDVDVAEDIYCHIAGVDIVRAGAGEFYVLEDNLRVPSGVSYMLENRKMSMRLMPDAFSRIKVEPVAHYPDLLLDNLREVAPHGGDDPTVVVLTPGMYNSAYFEHAFLAQQMGVELVEGQDLFVEQNTVYMRTTQGPRKVDVIYRRLDDDFLDPLSFRADSALGVPGLLSVYRAGRVTLANAIGTGIADDKSTYLYVPDMIRFYLSEEPILSNVPTWRCGRPEELSHVLANMHDLVVKEVHGAGGYGMLVGPSASRAEVESFKERVRANPANYIAQPTLALSTVPTYVESGVAPRHVDLRPYVLCGKDIRTVPGGLCRVALTEGSLVVNSSQGGGTKDTWVLEE
>NZ_CP009448.1|WP_006389789.1|5878321_5879308_+|alpha-E-domain-containing-protein
MLSRTADNLFWMCRYTERAENTARMLDVNLQMSLLPQDAQTREGSWNAVLRISELHRLYHAKHAAISPQDVLQYMVRDAENPSSIYSCMRAARENARAVRGSLTTEVWETYNTTWLELLKHLHTGLLERNPGEFFEWVKFRSHLARGVTIGTMLEDEALYFLRIGMHLERADNTARMLDVKFHERDGDGAQQQQQEGRGEGSPSGALQSEFYRWSALLSSVSGLEIYRKVYRDVITPDRVAELLILHPDMPRSLLAAMRAVSEDLARVSNQRSTETQRRAGMLCAELQFGRVEDILRSGLHQYLEHFLDRINDLGNRISQDFLVPLSA
>NZ_CP009448.1|WP_006389788.1|5879321_5880125_+|transglutaminase-family-protein
MKQIITHVTHYRYTAPVTYSIQTLRLTPRDDEHQRVLRWHIEAPGALEQQVDAYGNITHTLTLNRPHTEIELRVVGQVLVDPLAQGALGGEDSRLPVHAYCVQTALTQADDTILAFARAVLPDGLNTPADVLTLATAIHDRVAYEPGTTDVTTAAGQVLALGHGVCQDHAHLFLACVRGLGVPARYVSGYLYTTNEHAASHAWADVWLAGTGWTSVDVTNRQFASDCHCRLAVGRDYDSASPVRGVRTGGGEESMEVSVQVQTALQQ
>NZ_CP009448.1|WP_006389787.1|5880180_5881044_+|proteasome-type-protease
MTYCVAARLDAGLVFLSDSRTNAGVDQISVFRKMTVFERPGERMMVLMTSGNLAVSQAVLNALARQHDEGGETVWNAPDMFEATRRVGAAVRAVYHREAAALHEQGVDFNVSLIFGGQIGSERCRLFQVYSAGNFIEAGSECPYFQIGEAKYGKPILDRVLRPDTSLDEAAKCALISMDSTLRSNISVGLPLDLLVYDADALRVTHFASIDEHNEYFRMIRSTWGERLRQVFAEIPDPLWTRPEDPGSLVPASRIHQPLRAEPVDMTPPAYPTPQVLAQDPGKDQPN
>NZ_CP009448.1|WP_006389786.1|5881197_5882196_+|hypothetical-protein
MTPNFPRALRRLAVPLLALGCLAGGPAMAQSNYPNHPISLVVPFAAGGPTDVVARSLGAAMSKTLGQSIVVENRPGAGGTLAATHVARAAPDGYTFLIHHNGMATAPALYRKLPFNPLTDFAYVGQVADVPMTLLGRKDLPPGDMVEFIKYARANGNKINLANAGLGAVSQLCGMLLQEALGTQFTTIPYAGTAPALTALLGGQVDVLCDQTTQTIPHIKAQRVKLYGVTTLDRIRTLPDSPTLQESGLKGFEVKVWHGVYAPKGTPPEVVAKFNESLRAALKDPAFTQKMAELGAEIVPEAKQTPAGLQSWLQSEVDKWGPIIRKAGVYAD
>NZ_CP009448.1|WP_006389784.1|5883340_5883676_-|phage-holin-family-protein
MALILVWILNAVALLAVAYLLPGITVASFGSALIAALVLGLVNMLVKPVLVLLTLPITIVTLGLFLIVINALLFWFVGSVLKGFQVNGFWWAVGGAILYSIISGLLTKLIP

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1808760 : 1820067

Burkholderia_phage(50.0%)

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_006388471.1\|1808760_1809210_+	hypothetical protein	A0A0N7IRF3	Acinetobacter_phage	5.0e-18	37.1
WP_049072536.1\|1809206_1809395_+	hypothetical protein	NA	NA	NA	NA
WP_006388472.1\|1809387_1811055_+	hypothetical protein	NA	NA	NA	NA
WP_035183554.1\|1811047_1811647_+	hypothetical protein	NA	NA	NA	NA
WP_006388474.1\|1811656_1811956_+	hypothetical protein	NA	NA	NA	NA
WP_050807756.1\|1811975_1812986_+	hypothetical protein	A9YX04	Burkholderia_phage	1.4e-76	52.2
WP_006388476.1\|1813020_1813764_+	hypothetical protein	A9YX06	Burkholderia_phage	9.6e-83	63.1
WP_006388477.1\|1813772_1814126_+	hypothetical protein	A9YX11	Burkholderia_phage	6.1e-35	65.8
WP_006388478.1\|1814122_1815304_+	hypothetical protein	A9YX12	Burkholderia_phage	2.6e-130	62.8
WP_006388479.1\|1815305_1815971_+	DUF2612 domain-containing protein	A9YX13	Burkholderia_phage	7.3e-74	60.6
WP_080747538.1\|1815985_1816930_+	hypothetical protein	A0A0M3ULD8	Salmonella_phage	5.8e-16	54.1
WP_006388482.1\|1817524_1817875_+	hypothetical protein	NA	NA	NA	NA
WP_006388483.1\|1817877_1818900_-	DNA recombinase	A0A2H4JE37	uncultured_Caudovirales_phage	3.7e-24	32.3
WP_006388484.1\|1819085_1819547_+	hypothetical protein	A0A0U5LBV3	unidentified_phage	7.7e-14	37.2
WP_006388485.1\|1819536_1820067_+	hypothetical protein	A0A2H4JFP9	uncultured_Caudovirales_phage	4.1e-43	57.4

DBSCAN-SWA_2

2660596 : 2668531

Moraxella_phage(33.33%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_006388149.1\|2660596_2661184_+	DUF1949 domain-containing protein	A0A1X9I5T8	Streptococcus_phage	1.2e-19	36.8
WP_006388150.1\|2661217_2661592_-	thioredoxin	V9SJ74	Achromobacter_phage	1.9e-10	27.8
WP_006388151.1\|2661789_2662812_-	LLM class flavin-dependent oxidoreductase	NA	NA	NA	NA
WP_006388152.1\|2663190_2663547_+	glyoxalase/bleomycin resistance/extradiol dioxygenase family protein	NA	NA	NA	NA
WP_006388153.1\|2663631_2664924_-	NCS2 family permease	A0A0R6PHV4	Moraxella_phage	5.4e-65	36.3
WP_006388154.1\|2665032_2666064_+\|tRNA	tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD	A0A0R6PI74	Moraxella_phage	1.4e-92	51.6
WP_006388155.1\|2666133_2666775_-	glycerol-3-phosphate 1-O-acyltransferase PlsY	NA	NA	NA	NA
WP_006388156.1\|2666963_2667722_+	5'/3'-nucleotidase SurE	A0A1B1ITZ2	uncultured_Mediterranean_phage	1.5e-67	51.6
WP_050807754.1\|2667706_2668531_+	protein-L-isoaspartate(D-aspartate) O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	2.5e-31	45.2

DBSCAN-SWA_3

3767699 : 3821371

uncultured_Caudovirales_phage(19.23%)

capsid,terminase,tail,protease,head,portal

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_006386181.1\|3767699_3768998_-\|protease	ATP-dependent Clp protease ATP-binding subunit ClpX	G3M9Z9	Bacillus_virus	1.7e-130	54.1
WP_006386182.1\|3769099_3769753_-	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP	A0A223W000	Agrobacterium_phage	2.2e-54	55.7
WP_006386183.1\|3769757_3771068_-	trigger factor	NA	NA	NA	NA
WP_006386184.1\|3771236_3771992_-	peptidase	NA	NA	NA	NA
WP_006386185.1\|3772254_3772800_+	TIGR00645 family protein	K4K6D8	Caulobacter_phage	1.3e-20	32.7
WP_006225311.1\|3772900_3773107_-	cold-shock protein	A0A1W6JNX5	Morganella_phage	1.4e-15	59.7
WP_006386186.1\|3773399_3773963_-	DUF924 domain-containing protein	A0A1V0SIY0	Klosneuvirus	1.2e-16	41.2
WP_006386187.1\|3774187_3774391_-	cold-shock protein	A0A2H4N7Y6	Lake_Baikal_phage	3.1e-15	62.1
WP_006386188.1\|3774760_3775081_-	hypothetical protein	NA	NA	NA	NA
WP_038503909.1\|3775171_3775570_-	hypothetical protein	NA	NA	NA	NA
WP_006386190.1\|3775692_3775980_+	hypothetical protein	NA	NA	NA	NA
WP_006386191.1\|3776073_3776346_-	hypothetical protein	NA	NA	NA	NA
WP_006386192.1\|3776447_3776843_-	enamine deaminase RidA	NA	NA	NA	NA
WP_006386193.1\|3776869_3778018_-	alanine racemase	NA	NA	NA	NA
WP_006386194.1\|3778164_3779082_+	LysR family transcriptional regulator	NA	NA	NA	NA
WP_020928335.1\|3779264_3779663_-	RidA family protein	NA	NA	NA	NA
WP_026384511.1\|3779730_3780921_-	MFS transporter	NA	NA	NA	NA
WP_006386197.1\|3781054_3781636_+	TetR/AcrR family transcriptional regulator	NA	NA	NA	NA
WP_006386198.1\|3781759_3782287_+	hypothetical protein	NA	NA	NA	NA
WP_006386199.1\|3782357_3782663_+	hypothetical protein	NA	NA	NA	NA
WP_006386200.1\|3782686_3782995_-	hypothetical protein	NA	NA	NA	NA
WP_006386201.1\|3783061_3783919_-	3-deoxy-8-phosphooctulonate synthase	E3T537	Cafeteria_roenbergensis_virus	1.1e-50	41.7
WP_006386202.1\|3784155_3785115_+	metal-dependent phosphohydrolase	NA	NA	NA	NA
WP_006386203.1\|3785138_3786356_+	hypothetical protein	NA	NA	NA	NA
WP_006386204.1\|3786399_3787110_-	aquaporin Z	A0A1B1ISL4	uncultured_Mediterranean_phage	1.2e-05	50.0
WP_006386205.1\|3787252_3787834_-	glycerol-3-phosphate responsive antiterminator	NA	NA	NA	NA
WP_006386206.1\|3787835_3789392_-	FAD-binding oxidoreductase	NA	NA	NA	NA
WP_038503912.1\|3789388_3791068_-	glycerol-3-phosphate dehydrogenase/oxidase	NA	NA	NA	NA
WP_006386208.1\|3791064_3792603_-	glycerol kinase	NA	NA	NA	NA
WP_006386209.1\|3792617_3794075_-	MFS transporter	NA	NA	NA	NA
WP_006386210.1\|3794297_3794687_+	DUF1311 domain-containing protein	NA	NA	NA	NA
WP_006386211.1\|3794791_3795151_+	hypothetical protein	NA	NA	NA	NA
WP_006386212.1\|3795161_3795674_+	hypothetical protein	NA	NA	NA	NA
WP_035182376.1\|3795775_3796048_-	hypothetical protein	NA	NA	NA	NA
WP_006387661.1\|3796565_3797276_+	SOS response-associated peptidase	Q5QF62	Pseudomonas_virus	1.7e-36	38.7
WP_006387660.1\|3797241_3797436_-	hypothetical protein	NA	NA	NA	NA
WP_038504971.1\|3797571_3797793_+	hypothetical protein	NA	NA	NA	NA
WP_038503916.1\|3798157_3798424_-	hypothetical protein	NA	NA	NA	NA
WP_038503919.1\|3798426_3798918_-	hypothetical protein	I6NSS1	Burkholderia_phage	6.9e-45	59.9
WP_006387652.1\|3799424_3800153_-	hypothetical protein	A0A0B5A5A1	Achromobacter_phage	1.2e-64	51.5
WP_006387906.1\|3800152_3800449_-	hypothetical protein	A0A0B5A4G0	Achromobacter_phage	5.6e-18	50.0
WP_038503922.1\|3800448_3803622_-	host specificity protein J	A4JX16	Burkholderia_virus	4.5e-278	47.3
WP_038503924.1\|3803618_3804233_-\|tail	tail assembly protein	A4JX15	Burkholderia_virus	7.3e-52	57.1
WP_038503927.1\|3804236_3805010_-	hydrolase Nlp/P60	A4JX14	Burkholderia_virus	5.0e-66	50.6
WP_038503930.1\|3805011_3805740_-\|tail	phage minor tail protein L	Q6JIL5	Burkholderia_virus	6.8e-65	54.9
WP_050807749.1\|3805748_3805979_-	hypothetical protein	NA	NA	NA	NA
WP_006387644.1\|3807523_3807865_-	hypothetical protein	Q6UAW6	Klebsiella_phage	5.7e-30	54.5
WP_006387643.1\|3807861_3810837_-\|tail	phage tail tape measure protein	A0A2H4J9A1	uncultured_Caudovirales_phage	6.4e-93	32.5
WP_080564275.1\|3810870_3811287_-	hypothetical protein	NA	NA	NA	NA
WP_006387641.1\|3811247_3811667_-	hypothetical protein	NA	NA	NA	NA
WP_006387640.1\|3811742_3812678_-	hypothetical protein	G8CLB2	Synechococcus_phage	2.2e-60	40.7
WP_035183160.1\|3812710_3812905_-	hypothetical protein	NA	NA	NA	NA
WP_006387638.1\|3812940_3813363_-	hypothetical protein	NA	NA	NA	NA
WP_006387637.1\|3813359_3813662_-	hypothetical protein	NA	NA	NA	NA
WP_006387636.1\|3813667_3814672_-\|capsid	minor capsid protein E	A0A2H4J890	uncultured_Caudovirales_phage	2.0e-67	41.9
WP_006387635.1\|3814752_3815103_-\|head	head decoration protein	A0A2H4JF15	uncultured_Caudovirales_phage	1.5e-17	49.6
WP_006387634.1\|3815130_3816240_-\|protease	Clp protease ClpP	A0A2H4JDI2	uncultured_Caudovirales_phage	3.1e-45	36.1
WP_006387633.1\|3816268_3817768_-\|portal	phage portal protein	A0A2H4JFL5	uncultured_Caudovirales_phage	6.4e-126	49.8
WP_006387632.1\|3817764_3817971_-	hypothetical protein	A0A2H4EUL1	Aeromonas_phage	4.5e-06	42.6
WP_006387631.1\|3818019_3820014_-\|terminase	terminase	R9TMM4	Vibrio_phage	4.7e-116	37.4
WP_006387630.1\|3820091_3820589_-	hypothetical protein	NA	NA	NA	NA
WP_006387629.1\|3820585_3821371_-	hypothetical protein	A0A1B0Z000	Pseudomonas_phage	8.8e-34	39.7

DBSCAN-SWA_4

5563627 : 5580207

Burkholderia_virus(33.33%)

tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_006385703.1\|5563627_5564446_+	NAD(P)-dependent oxidoreductase	W8CYX9	Bacillus_phage	1.4e-10	49.3
WP_006385702.1\|5564464_5565394_-	LysR family transcriptional regulator	NA	NA	NA	NA
WP_006385701.1\|5565535_5566132_-\|tail	tail assembly protein	C7BGD3	Burkholderia_phage	1.9e-49	53.0
WP_035182020.1\|5566128_5566365_-	hypothetical protein	NA	NA	NA	NA
WP_080747611.1\|5566524_5569764_-	host specificity protein J	A4JX16	Burkholderia_virus	1.3e-261	45.3
WP_006385697.1\|5569889_5570495_-\|tail	tail assembly protein	Q6JIL3	Burkholderia_virus	1.0e-50	55.7
WP_006385696.1\|5570491_5571271_-	hydrolase Nlp/P60	Q3HQU3	Burkholderia_phage	1.5e-65	47.3
WP_006385695.1\|5571273_5572002_-\|tail	phage minor tail protein L	Q6JIL5	Burkholderia_virus	2.2e-71	58.3
WP_006385694.1\|5572004_5573966_-	hypothetical protein	A0A0K0KVF1	Prochlorococcus_phage	1.9e-13	36.2
WP_006385693.1\|5573962_5574307_-	hypothetical protein	A0A0S2SYI2	Pseudomonas_phage	1.1e-20	38.4
WP_006385692.1\|5574303_5575590_-	hypothetical protein	K7PH87	Enterobacterial_phage	3.1e-12	41.1
WP_006385691.1\|5575647_5575938_-	DUF4035 domain-containing protein	S4TND7	Salmonella_phage	9.1e-13	50.0
WP_006385690.1\|5575937_5576411_-\|tail	tail protein	A4JX08	Burkholderia_virus	1.4e-26	44.4
WP_006385689.1\|5576416_5576884_-	hypothetical protein	NA	NA	NA	NA
WP_006385688.1\|5577135_5577777_-	hypothetical protein	NA	NA	NA	NA
WP_006385687.1\|5578001_5578697_+	LexA family transcriptional repressor	NA	NA	NA	NA
WP_006385686.1\|5578749_5580207_-	DUF1254 domain-containing protein	M1IA53	Paramecium_bursaria_Chlorella_virus	3.6e-65	35.8

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP009448

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection