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_CP032471	Helicobacter pylori strain 479-C2-EK2 chromosome, complete genome	5 crisprs	cas4,cas3,DEDDh	2	2	0	0

1. NZ_CP032471

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP032471_1

• CRISPR_ID: NZ_CP032471_1
• CRISPR_location: 270504-270573
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP032471_1

Consensus_repeat	Method
TTTCTTTTTAAGGGATTTCTTTTT	CRISPRCasFinder

spacers of NZ_CP032471_1

>1.1|270528|22|NZ_CP032471|CRISPRCasFinder
AAGGGATTTCTTTTTTAAAACT

CRISPR arrays and Neighbor proteins around NZ_CP032471_1

CRISPR arrays

The CRISPR arrays of NZ_CP032471_1

>merge|NZ_CP032471|1|270504-270573|CRISPRCasFinder
CTTTTTTTAAAGGGATTTCTTTTTAAGGGATTTCTTTTTTAAAACTCTTTTTTTTAAAGGCATTTCTTTT

>NZ_CP032471|1|1|270504-270573|CRISPRCasFinder
CTTTTTTTAAAGGGATTTCTTTTT	AAGGGATTTCTTTTTTAAAACT
CTTTTTTTTAAAGGCATTTCTTTT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP032471.1|WP_139518134.1|262417_263209_+|shikimate-dehydrogenase	unknown	unknown	gnl|CDD|161904
NZ_CP032471.1|WP_001237418.1|278139_278691_-|DUF507-family-protein	unknown	unknown	gnl|CDD|225502
NZ_CP032471.1|WP_000301323.1|281318_281780_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518145.1|280020_280917_-|EamA-family-transporter	unknown	unknown	gnl|CDD|307170
NZ_CP032471.1|WP_139518141.1|274890_275367_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518142.1|275841_276846_-|formamidase	unknown	unknown	gnl|CDD|183950
NZ_CP032471.1|WP_139518140.1|274207_274780_+|septum-formation-inhibitor-Maf	unknown	unknown	gnl|CDD|179732
NZ_CP032471.1|WP_139518144.1|278769_280017_-|glycosyltransferase-family-39-protein	unknown	unknown	gnl|CDD|379080
NZ_CP032471.1|WP_139518143.1|277012_278140_-|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit	unknown	unknown	gnl|CDD|223579
NZ_CP032471.1|WP_139518139.1|271671_274206_+|alanine--tRNA-ligase	unknown	unknown	gnl|CDD|234701
NZ_CP032471.1|WP_139518136.1|265132_266155_+|hypothetical-protein	unknown	unknown	gnl|CDD|236276
NZ_CP032471.1|WP_139518133.1|261822_262410_+|SH3-domain-containing-protein	unknown	unknown	gnl|CDD|214600
NZ_CP032471.1|WP_139523635.1|268287_270426_+|Hop-family-adhesin-BabB	unknown	unknown	gnl|CDD|375731
NZ_CP032471.1|WP_139518131.1|258983_260771_+|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|173862
NZ_CP032471.1|WP_001216698.1|266307_266736_+|30S-ribosomal-protein-S6	unknown	unknown	gnl|CDD|179034
NZ_CP032471.1|WP_139518137.1|266745_267291_+|single-stranded-DNA-binding-protein	unknown	unknown	gnl|CDD|236275
NZ_CP032471.1|WP_000440196.1|267313_267571_+|30S-ribosomal-protein-S18	unknown	unknown	gnl|CDD|178997
NZ_CP032471.1|WP_139518132.1|260767_261814_+|microcin-C-ABC-transporter-permease-YejB	unknown	unknown	gnl|CDD|226642
NZ_CP032471.1|WP_139518135.1|263208_265143_+|RNB-domain-containing-ribonuclease	unknown	unknown	gnl|CDD|223631
NZ_CP032471.1|WP_000468322.1|271321_271552_-|YdcH-family-protein	unknown	unknown	gnl|CDD|225397

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP032471.1|WP_139518134.1|262417_263209_+|shikimate-dehydrogenase	gnl|CDD|161904	TIGR00507, Shikimate_dehydrogenase, shikimate dehydrogenase. This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family].	2.68711e-111
NZ_CP032471.1|WP_001237418.1|278139_278691_-|DUF507-family-protein	gnl|CDD|225502	COG2952, COG2952, Uncharacterized protein conserved in bacteria [Function unknown].	5.26568e-81
NZ_CP032471.1|WP_139518145.1|280020_280917_-|EamA-family-transporter	gnl|CDD|307170	pfam00892, EamA, EamA-like transporter family. This family includes many hypothetical membrane proteins of unknown function. Many of the proteins contain two copies of the aligned region. The family used to be known as DUF6. Members of this family usually carry 5+5 transmembrane domains, and this domain attempts to model five of these.	1.966e-13
NZ_CP032471.1|WP_139518142.1|275841_276846_-|formamidase	gnl|CDD|183950	PRK13287, amiF, formamidase; Provisional.	0
NZ_CP032471.1|WP_139518140.1|274207_274780_+|septum-formation-inhibitor-Maf	gnl|CDD|179732	PRK04056, PRK04056, septum formation inhibitor Maf.	6.12262e-95
NZ_CP032471.1|WP_139518144.1|278769_280017_-|glycosyltransferase-family-39-protein	gnl|CDD|379080	pfam13231, PMT_2, Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366.	2.63701e-05
NZ_CP032471.1|WP_139518143.1|277012_278140_-|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit	gnl|CDD|223579	COG0505, CarA, Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism / Nucleotide transport and metabolism].	0
NZ_CP032471.1|WP_139518139.1|271671_274206_+|alanine--tRNA-ligase	gnl|CDD|234701	PRK00252, alaS, alanyl-tRNA synthetase; Reviewed.	0
NZ_CP032471.1|WP_139518136.1|265132_266155_+|hypothetical-protein	gnl|CDD|236276	PRK08487, PRK08487, DNA polymerase III subunit delta; Validated.	4.45065e-130
NZ_CP032471.1|WP_139518133.1|261822_262410_+|SH3-domain-containing-protein	gnl|CDD|214600	smart00287, SH3b, Bacterial SH3 domain homologues.	4.03698e-12
NZ_CP032471.1|WP_139523635.1|268287_270426_+|Hop-family-adhesin-BabB	gnl|CDD|375731	pfam18304, SabA_adhesion, SabA N-terminal extracellular adhesion domain. This is the N-terminal extracellular adhesion domain of Sialic acid binding adhesin (SabA) present in Helicobacter pylori. The N-terminal domain of SabA functions as a sugar-binding adhesion domain with conserved disulfide bonds. Notably, these amino acid residues are not only conserved among SabA orthologs but also between SabA and BabA.	1.19561e-95
NZ_CP032471.1|WP_139518131.1|258983_260771_+|ABC-transporter-substrate-binding-protein	gnl|CDD|173862	cd08497, PBP2_NikA_DppA_OppA_like_14, The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold. This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. 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_CP032471.1|WP_001216698.1|266307_266736_+|30S-ribosomal-protein-S6	gnl|CDD|179034	PRK00453, rpsF, 30S ribosomal protein S6; Reviewed.	9.76773e-42
NZ_CP032471.1|WP_139518137.1|266745_267291_+|single-stranded-DNA-binding-protein	gnl|CDD|236275	PRK08486, PRK08486, single-stranded DNA-binding protein; Provisional.	2.67381e-109
NZ_CP032471.1|WP_000440196.1|267313_267571_+|30S-ribosomal-protein-S18	gnl|CDD|178997	PRK00391, rpsR, 30S ribosomal protein S18; Reviewed.	2.41298e-32
NZ_CP032471.1|WP_139518132.1|260767_261814_+|microcin-C-ABC-transporter-permease-YejB	gnl|CDD|226642	COG4174, COG4174, ABC-type uncharacterized transport system, permease component [General function prediction only].	0
NZ_CP032471.1|WP_139518135.1|263208_265143_+|RNB-domain-containing-ribonuclease	gnl|CDD|223631	COG0557, VacB, Exoribonuclease R [Transcription].	1.42599e-131
NZ_CP032471.1|WP_000468322.1|271321_271552_-|YdcH-family-protein	gnl|CDD|225397	COG2841, COG2841, Uncharacterized protein conserved in bacteria [Function unknown].	4.94958e-24

Protein sequences

>NZ_CP032471.1|WP_139523635.1|268287_270426_+|Hop-family-adhesin-BabB
MSRRKHEKNPFTLSLSLSFLLHAEDDGFYTSVGYQIGEAAQMVKNTKGIQELSDNYEKLNNLLNNYSTLNTLIKLSADPSAINDARDNLGSSGRNLLDVKTNSPAYQAVLLALNAAVGLWQVTSYAFTACGPGSNESANGGIQTFNNVPGQNTTTITCNSYYEPGHGGPISTANYAKINRAYQIIQKALTANGSNGDGVPVLSNTTTKLDFTINGDKRTGGKPNEPLIYSWSHGKAIHTQWIHTTSTSTTENINTENNAQELLKQASIIITTLNEACPNFQNGGGGYWQGISGNGTMCGMFKNEISAIQGMIANAQEAVAQSKIVSENAQNQNNLDTGKPFNPYTDASFAQSMLKNAQAQAEMLNQAEQVVKNFEKIPKNFVSDSLGVCYEVQGGERRGTNPGQVTSNTWGAGCAYVGQTITNLENSIAHFGTQEQQIQQAENIADTLVHFKSRYSELGNTYNNITTALSKVPNAQSLQNVVSKKNNPYSPQGIETNYYLNQNSYNQIQTINQELGRNPFRKVGIVSSQTNNGAMNGIGIQVGYKQFFGQKRKWGARYYGFFDYNHAFIKSSFFNSASDVWTYGFGADALYNFINDKATNFLGKNNKLSVGLFGGIALAGTSWLNSEYVNLATVNNVYNAKMNVANFQFLFNMGVRMNLARSKKKGSDHAAQHGIELGLKIPTINTNYYSFMGAELKYRRLYSVYLNYVFAY
>NZ_CP032471.1|WP_000440196.1|267313_267571_+|30S-ribosomal-protein-S18
MERKRYSKRYCKYTEAKISFIDYKDLDMLKHTLSERYKIMPRRLTGNSKKWQERVEVAIKRARHMALIPYIVDRKKVVDSPFKQH
>NZ_CP032471.1|WP_139518137.1|266745_267291_+|single-stranded-DNA-binding-protein
MFNKVIMVGRLTRNVELKYLPSGSAAATIGLATSRRFKKQDGTLGEEVCFIDARLFGRTAEIANQYLSKGSSVLIEGRLTYESWMDQTGKKNSRHTITADSLQFMDKKSDNPQANAMQDSIMHENFNNAYPANHNTPSQDPFNQAPSYAQNAYAKENLQAQPSKYQNSVPEINIDEEEIPF
>NZ_CP032471.1|WP_001216698.1|266307_266736_+|30S-ribosomal-protein-S6
MRHYETMFILKPTLVEEEIKSKIEFYKEVITKHHGVIETSLDMGMRNLAYEIKKHKRGYYYVAYFKAEPSMILELERLYRINEDVLRFIVIKYESKKEVEAWHALVDRANKKPSHAKEKHEKTEHTHSHHTEEAESVGSHSE
>NZ_CP032471.1|WP_139518136.1|265132_266155_+|hypothetical-protein
MYRKDLDHYLKQRLPKAVFLYGEFDFFIHYYTQTISTLFKLSNPDTETSLFYASDYEKSQIATLLEQDSLFGGSSLVVLKLDFALHKKFKENDINLFLKALERPSHNRLIIGLYNAKSDTTKYKYTSDAIVKFFQKSPLKDEAICVRFFTPKTWESLKFLQERANFLHLDISGHLLNALFEINNEDLSVSFNDLDKLAILNAPITLEDIQELSSNAGDMDLQKLILGLFLKKSVLDIYDYLLKEGKKDADILRGLERYFYQLFLFFAHIKTTGLMDAKEVLGYAPPKEIAENYAKNAMRLKEAGYKRVFEIFRLWHIQSMQGQKELGFLYLTSIQKIINP
>NZ_CP032471.1|WP_139518135.1|263208_265143_+|RNB-domain-containing-ribonuclease
MQGFLRSLFFGVKKIPKRFAPLVEKGVLKEALQSNKDRYFLKEGFDIGKIEWAENKAFFVSLAKNYPKDPLIKNLPPSFKTDALILCQIECSKKRPIAFFKAALFDTQDMMIAYLAKEKNQIVAIPFKEPFKKPISLKHSQRSLLALPRHCVVKIDLKKREISGILGALEDPLIDENLSLSLFDRVKDFSKDCLNLAQHYAQLKASDFKDRINYSHIPFITIDPKDAKDFDDAIFYDQEKRVLFVAVADVSEFVPKHSSLDKEARLRGFSVYFPNSVYPMLPLSLSQGACSLKAFEKRLALVYEIPLDDLKNARLSQGVIEVRANCTYEEINYFLSANQSSLDKDLQQSLLGFLEVALRLKKERLKKGFNFNSFENKLYLNKEGRIEKIETQTESDAHTLIEEAMLLANQSSARLLDEHFHNKGIYRTHKEPSLEQQKRLYDKLFDYEIVRPKNMGFFPFLEHALKIAKEKSIEREVSRLIIKSQNLALYSPMQESHFGLGFASYTHFTSPIRRYSDLALHRLLKELLFHQAKGCSYLLEETPELCSELNALQKKAALIERDFIKRKFARLALEFLEKEFLGVVLEVKDWVVVGLKEFIGLKVLVKTNKVFKSLEKVHVTITHADLILGQVRGEITERVKEHVS
>NZ_CP032471.1|WP_139518134.1|262417_263209_+|shikimate-dehydrogenase
MKLKSFGVFGNPIKHSKSPLIHNACFLTFQKKLGFLGHYHPILLPLESYIKNEFLHLGLSGANVTLPFKERAFQVCDKIKGIALECGAVNTLVLENDELVGYNTDASGFWLSLGGESYQSALILGSGGSAKALACELKKQGLEVSVLNRSARGLDFFQRLGCDCFMEPPKSAFDLIINATSASLHHELPLNKEVLKGYFKEAKLAYDLAYGFLTPFLSLAKELKTPFQDGKGMLIYQAALSFEKFSASQIPYSKAFEVMRSVF
>NZ_CP032471.1|WP_139518133.1|261822_262410_+|SH3-domain-containing-protein
MKTEMKSSLKLFMRPLLVVLAFMLLYALVHAALGFYVKKDSAPISQNVEKTETERQNGVLSPKEEANTTTTATEESPTKDTAPPLETTAQEKETKQENKQEQEKENEPKQDSVPPVQNNQKTPTTPLIGKKPLEYKVAVNSVNVRAFPSTKSKIIGSLAKDKSVKVLEIQNDWAKIEFSNKTKGYVFLKLLKKAE
>NZ_CP032471.1|WP_139518132.1|260767_261814_+|microcin-C-ABC-transporter-permease-YejB
MIAYILKRLLLIIPTLLAIMTINFFLIQSAPGGPIEQMMAKINNTQSKETQGLVKERSYRASQGLESDLLENLKKLYGFDKPIGERYLLMLKKYVQFDFGESFYRQIKVVDLIKEKLPVSISLGLFSTLLIYLISIPLGIFKAKRNNEPLDVLSSVVIIVANAIPAFLFAVVLIVFFAGGNYWHWFPLKGLVSDNFESLSTLGKIKDYLWHITLPVLCISLGGFASLTLLVKNSFLDEMGKLYVLSAKAKGCSVGRIFYVHVFRNAILLVVAGFPQAFLGMFFSSSLLIEIVFSLDGLGLLGYESIVSRDYPVVFGSLYIFTLLGLVASLISDLLCVVIDPRIDFEKR
>NZ_CP032471.1|WP_139518131.1|258983_260771_+|ABC-transporter-substrate-binding-protein
MVFKILGLWLGVFCFLKATPYLYLGEEPKYKDNFTHFEYANPDAKKGGVLRNDAIGTFDSLNPFALKGTKAEGLDLIYDTLMVQSLDEPFAEYPLIAKDAEVAKDNSYVIFTLDKRARFSNNAPILASDVKFSFDTIMKLGSPIYRQYYQDVKKAVVLDKHHVKFIFKTTENKELPLILGQLQIFSKKAFQKDYFEKNPLLIPVSSGPYVIASFDVGKKITYQRNPNYWARNLPSRKGQFNFDEIKFEYYKDETIALQAFLSGAYDWRIESTAKIWARGYVGKAMDNKKITKYLIAHKMPSGMQGFFFNTRREIFKDKRVREALFYAFDFEWANKNLFFSQYKRTTSFFSNSVYASPPLPSPEEKVLLAPYEKSLDERVFKEPYVVPRTDGVDVLGYNLRENLKYAQKLLESAGFSYKNMRLVDKNDKPFSFTLLLNSPAFERLALAFAKNLRVLGIEMKIQRVDLSQYVNRIKSYDFDMIVGVIGQSSFPGNEQRFYFGSLSAKEKGTRNYAGISSKAVDDLIEKIINAKDYKEQLAAIQAMDRVLLWGFYVIPHFYLPNYRIAAYNYIGMPEISPSYGFSPYLWWIKKEKDLQ
>NZ_CP032471.1|WP_000468322.1|271321_271552_-|YdcH-family-protein
MFHEFRDEISVLKANNPHFDKIFEKHNQLDDDIKTAEQQNASDAEISHMKKQKLKLKDEIHGMIIEYREKQKSERA
>NZ_CP032471.1|WP_139518139.1|271671_274206_+|alanine--tRNA-ligase
MDIRNEFLQFFQNKGHEIYPSMPLVPNDATLLFTNAGMVQFKDIFTGMVPRPSIPRATSSQLCMRAGGKHNDLENVGYTARHHTLFEMLGNFSFGDYFKEEAILFAWEFVTKNLGFKPKDLYISVHEKDDEAVKLWGKFVPVERIKKMGDKDNFWQMGDSGPCGPCSEIYIDQGEKHFKGSEDYFGGEGDRFLEIWNLVFMQYERSNDGVLSPLPKPSIDTGMGLERVQALLEHKLNNFDSSLFAPLMGEISELTSLDYASEFQPSFRVVADHARAVAFLLAQGVHFNKEGRGYVLRRILRRALRHGYLMGLKEAFLYKVVGVVCEQFSNTHAYLKESKEMVMKECFEEEERFLETLESGMELFNLSLKHLNENKIFDGKIAFKLYDTFGFPLDLTNDMLRSHGACVDMQGFELCMQEQVKRSKASWKGKQNNADFSAILNAYAPNEFVGYETTECCAKALGFFDSDFKEITDANPNQEVWVLLEKTPFYAEGGGAIGDKGALLKDNEEVALVLDTKNFFGLNFSLLEIKKALKKGDQVIAQVSDERLEIAKHHSATHLLQSALREVLGSHVSQAGSLVESKRLRFDFSHPKALNDEELEKVEDLVNAQIFKHLNSQVEHMPLNQAKDKGALALFSEKYAENVRVVSFKEASIELCGGIHVENTGLIGGFRIVKESGVSSGVRRIEAVCGKAFYQLAKEENKELKNAKIVLKNNDVIAGINKLKENSQKAPVSMDLPVEKIHGVNLVVGVVEQGDIKEMIDRLKSKHERLLAMVFKKENERITLACGVKNAPIKANAWANEVAQILGGKGGGRGDFASAGGKDIENLQAALNLAKNTALKALEG
>NZ_CP032471.1|WP_139518140.1|274207_274780_+|septum-formation-inhibitor-Maf
MELVLGSQSSARANLLKEHGIKFEQKALYFDEENLKTTDPREFVYLACKGKLEKAKELLANNCVIVVADSVVSVGNRMQRKAKNKREALEFLKLQNGNEIEVLTCSALISPKLEWLDLSVFRVRLKAFDPSEIEKYLESGLWQESAGCVRLEDFHKPYIKSSSENLSVGLGLNVEGLLRALKLGAKLSSL
>NZ_CP032471.1|WP_139518141.1|274890_275367_+|hypothetical-protein
MAHFIFSVVVVLLWLVAWGIYLVFGKNLKREMEEIENSDPNQNNPFITAAMGIGGAAISIFFPDTKPIVDGVKPLAEKGLQEAFRKDKLTEGQKISISSLRFLSLFCIVVAAMIGVCLIWSFNGWSFWKVTGYFLFYVVVCSASTLPNISINGILDDR
>NZ_CP032471.1|WP_139518142.1|275841_276846_-|formamidase
MGSIGSMGKPIEGFLVAAIQFPVPIVNSRKDIDHNIESIIRTLHATKAGYPGVELIIFPEYSTQGLNTAKWLSEEFLLDVPGKETELYAQACKEAKVYGVFSIMERNPDSNKNPYNTAIIINPQGEIVLKYRKLFPWNPIEPWYPGDLGMPVCEGPGGSKLAVCICHDGMIPELAREAAYKGCNVYIRISGYSTQVNDQWILTNRSNAWHNLMYTVSVNLAGYDNVFYYFGEGQICNFDGTTLVQGHRNPWEIVTGEIYPKMADNARLSWGLENNIYNLGHRGYVAKLGGEHDAGLTYIKDLAAGKYKLPWEDHMKIKDGSIYGYPTTGGRFGK
>NZ_CP032471.1|WP_139518143.1|277012_278140_-|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit
MVSLYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGANSKDDESFFSCAGILARHYNEFFSNSRADFSLSAYLKERGVLGICGVDTRSLIKTLRHHGCLMMVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRTTFDFKTLDYKPFDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKANELIKAYEKKEISGIFLSNGPGDPLSLQQEIKEIKQLINAKIPMFGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNLKTNAVEITAQNHNYCVPEEIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGPKESHYIFKEFVELLKDF
>NZ_CP032471.1|WP_001237418.1|278139_278691_-|DUF507-family-protein
MRLKLTHINHISHKIANDFIHSKLLELKAPRELLCELIEGILEKSVKKENAIDEQARELLEENTDEIEFMRMDERQLFWMIKRQIAQKEGFHLFWEERCNDLSHQILNKILDEDLIMFSVSENLIRNLIYKSIDTYSKAYESIENEVHEKIKHYKRKLPVGSDEYELVFERLYEEELRRKGFL
>NZ_CP032471.1|WP_139518144.1|278769_280017_-|glycosyltransferase-family-39-protein
MQLSPLQSALLYFSYFIYPEKKTRSFDLSDLVFIIMVFLVLALGLLMSGEISISYNEAKDFFYSSAWFVQIAQKSTEILGQNDLALRLPFLIAHLINMFLFYLIGRKILKKPKDALYVVLTYALLPGVNLFAILLAKSVLVLSLGLLISYLYIKTQKIPYLTLSACAFLDGAFIPLLLGVFTYALRRRYFKSAIFILVVLGVNTALFSGSFNKGLPSGYFIDTCLELMLLYSPLFFLYYPYTIYKALFDKKPSLLAFMSASGWLFPLLLSMRQEIDLKTFAPLALIGLPLFVKSVLNSLRVRLKEFRGQYYLRVFSLYLLMLTETLFLWGSKISGTNEKLLNRHFLAKEVATALQLRGIHQIRTNDKQLALRLQFYGIKEGGRLRLINAKISKKRPDITIIYADKILQSYSLVRH
>NZ_CP032471.1|WP_139518145.1|280020_280917_-|EamA-family-transporter
MRNTILFGVSMILLANLCFGIMSAFVKITADYFSPMENVFYRSITMTLLLLLIYPFKPYRLKSYKQGGFKKLAFRVVVGGLAMLAFFYNIEKISLATATAFSQCAPIYTVLLSPLLLKEKLKRSALISACIGIVGVVLISDPSVENVGPVEIFMGILSGIFVSLAYITLRDLREYYDKQAVILAFAFGMSLLGLVGMFIDIPFLSTGIHIPRKEDILWISLIGISGTLGQYFLTYAYMNAPAGIIAPIEYTRIVWGLLFGLYLGDKFLDLKSSLGVALILCSGLLIALPALLKELKKI
>NZ_CP032471.1|WP_000301323.1|281318_281780_+|hypothetical-protein
MAVSSINQFDSNLYGLLNAKSAPKEDLAPVENTEKIEREKKDAPTENLPFNPDKRETYGFLVLELMSDREYEAFLRATAGMDESQKRLAAQSLYSLTDFYNGKFSKEVENAPKQPINGLHKKALQTFNATNHNAFLQRYQNAYNNPSTMDVTL

Crispr_ID: NZ_CP032471_2

• CRISPR_ID: NZ_CP032471_2
• CRISPR_location: 421347-421432
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP032471_2

Consensus_repeat	Method
GTTCTTGAACCACTACTTCTCGCATG	CRISPRCasFinder

spacers of NZ_CP032471_2

>2.1|421373|34|NZ_CP032471|CRISPRCasFinder
CCCATGCAGAGATCAAAGAAAACTCCCTTGAAGC

CRISPR arrays and Neighbor proteins around NZ_CP032471_2

CRISPR arrays

The CRISPR arrays of NZ_CP032471_2

>merge|NZ_CP032471|2|421347-421432|CRISPRCasFinder
GTTCTTGAACCACTACTTCTCGCATGCCCATGCAGAGATCAAAGAAAACTCCCTTGAAGCGTTCTTGAACCACTACTTCTCGCATG

>NZ_CP032471|2|2|421347-421432|CRISPRCasFinder
GTTCTTGAACCACTACTTCTCGCATG	CCCATGCAGAGATCAAAGAAAACTCCCTTGAAGC
GTTCTTGAACCACTACTTCTCGCATG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP032471.1|WP_128045459.1|417306_417867_-|pyruvate-flavodoxin-oxidoreductase-subunit-gamma	unknown	unknown	gnl|CDD|180284
NZ_CP032471.1|WP_139518227.1|428401_429274_+|Sel1-like-repeat-protein-HcpC	unknown	unknown	gnl|CDD|223861
NZ_CP032471.1|WP_139518223.1|423823_424507_-|6-phosphogluconolactonase	unknown	unknown	gnl|CDD|273494
NZ_CP032471.1|WP_139518225.1|425860_427687_+|phosphogluconate-dehydratase	unknown	unknown	gnl|CDD|130264
NZ_CP032471.1|WP_139518230.1|432589_433624_+|UDP-glucose-4-epimerase-GalE	unknown	unknown	gnl|CDD|273487
NZ_CP032471.1|WP_139518220.1|418824_420132_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518226.1|427705_428332_+|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	unknown	unknown	gnl|CDD|273490
NZ_CP032471.1|WP_139518215.1|410406_412383_+|excinuclease-ABC-subunit-B	unknown	unknown	gnl|CDD|235395
NZ_CP032471.1|WP_139518218.1|415665_416889_-|2-oxoacid:ferredoxin-oxidoreductase-subunit-alpha	unknown	unknown	gnl|CDD|181999
NZ_CP032471.1|WP_139518219.1|418155_418818_+|outer-membrane-beta-barrel-protein	unknown	unknown	gnl|CDD|280099
NZ_CP032471.1|WP_139518217.1|413277_414600_-|adenylosuccinate-lyase	unknown	unknown	gnl|CDD|181437
NZ_CP032471.1|WP_000656174.1|416898_417291_-|4Fe-4S-binding-protein	unknown	unknown	gnl|CDD|236596
NZ_CP032471.1|WP_139535462.1|409705_410356_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518228.1|429457_430210_-|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl|CDD|187604
NZ_CP032471.1|WP_000238149.1|414708_415653_-|pyruvate-ferredoxin-oxidoreductase-subunit-beta	unknown	unknown	gnl|CDD|239471
NZ_CP032471.1|WP_139518229.1|430231_431767_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518224.1|424517_425795_-|glucose-6-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|223441
NZ_CP032471.1|WP_001126887.1|422826_423837_-|glucokinase	unknown	unknown	gnl|CDD|129832
NZ_CP032471.1|WP_139518222.1|421610_422657_-|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl|CDD|176186
NZ_CP032471.1|WP_139518216.1|412379_413213_-|outer-membrane-beta-barrel-protein	unknown	unknown	gnl|CDD|280099

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP032471.1|WP_128045459.1|417306_417867_-|pyruvate-flavodoxin-oxidoreductase-subunit-gamma	gnl|CDD|180284	PRK05844, PRK05844, pyruvate flavodoxin oxidoreductase subunit gamma; Validated.	6.4426e-128
NZ_CP032471.1|WP_139518227.1|428401_429274_+|Sel1-like-repeat-protein-HcpC	gnl|CDD|223861	COG0790, COG0790, FOG: TPR repeat, SEL1 subfamily [General function prediction only].	2.46504e-47
NZ_CP032471.1|WP_139518223.1|423823_424507_-|6-phosphogluconolactonase	gnl|CDD|273494	TIGR01198, 6-phosphogluconolactonase_6PGL., 6-phosphogluconolactonase. This enzyme of the pentose phosphate pathway is often found as a part of a multifunctional protein with [Energy metabolism, Pentose phosphate pathway].	1.67984e-94
NZ_CP032471.1|WP_139518225.1|425860_427687_+|phosphogluconate-dehydratase	gnl|CDD|130264	TIGR01196, Phosphogluconate_dehydratase, 6-phosphogluconate dehydratase. A close homolog, designated MocB (mannityl opine catabolism), is found in a mannopine catabolism region of a plasmid of Agrobacterium tumefaciens. However, it is not essential for mannopine catabolism, branches within the cluster of 6-phosphogluconate dehydratases (with a short branch length) in a tree rooted by the presence of other dehydyatases. It may represent an authentic 6-phosphogluconate dehydratase, redundant with the chromosomal copy shown to exist in plasmid-cured strains. This model includes mocB above the trusted cutoff, although the designation is somewhat tenuous. [Energy metabolism, Entner-Doudoroff].	0
NZ_CP032471.1|WP_139518230.1|432589_433624_+|UDP-glucose-4-epimerase-GalE	gnl|CDD|273487	TIGR01179, UDP-glucose_4-epimerase, UDP-glucose-4-epimerase GalE. Alternate name: UDPgalactose 4-epimerase This enzyme interconverts UDP-glucose and UDP-galactose. A set of related proteins, some of which are tentatively identified as UDP-glucose-4-epimerase in Thermotoga maritima, Bacillus halodurans, and several archaea, but deeply branched from this set and lacking experimental evidence, are excluded from this model and described by a separate model. [Energy metabolism, Sugars].	0
NZ_CP032471.1|WP_139518226.1|427705_428332_+|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	gnl|CDD|273490	TIGR01182, KHG/KDPG_aldolase_., Entner-Doudoroff aldolase. 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff].	1.84804e-111
NZ_CP032471.1|WP_139518215.1|410406_412383_+|excinuclease-ABC-subunit-B	gnl|CDD|235395	PRK05298, PRK05298, excinuclease ABC subunit UvrB.	0
NZ_CP032471.1|WP_139518218.1|415665_416889_-|2-oxoacid:ferredoxin-oxidoreductase-subunit-alpha	gnl|CDD|181999	PRK09622, porA, 2-oxoacid:ferredoxin oxidoreductase subunit alpha.	0
NZ_CP032471.1|WP_139518219.1|418155_418818_+|outer-membrane-beta-barrel-protein	gnl|CDD|280099	pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.	1.72621e-36
NZ_CP032471.1|WP_139518217.1|413277_414600_-|adenylosuccinate-lyase	gnl|CDD|181437	PRK08470, PRK08470, adenylosuccinate lyase; Provisional.	0
NZ_CP032471.1|WP_000656174.1|416898_417291_-|4Fe-4S-binding-protein	gnl|CDD|236596	PRK09625, porD, pyruvate flavodoxin oxidoreductase subunit delta; Reviewed.	5.72644e-84
NZ_CP032471.1|WP_139518228.1|429457_430210_-|SDR-family-NAD(P)-dependent-oxidoreductase	gnl|CDD|187604	cd05346, SDR_c5, classical (c) SDR, subgroup 5. These proteins are members of the classical SDR family, with a canonical active site tetrad and a 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 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 (15-PGDH) numbering). 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) 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.	1.41717e-144
NZ_CP032471.1|WP_000238149.1|414708_415653_-|pyruvate-ferredoxin-oxidoreductase-subunit-beta	gnl|CDD|239471	cd03376, TPP_PFOR_porB_like, Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.	3.89415e-136
NZ_CP032471.1|WP_139518224.1|424517_425795_-|glucose-6-phosphate-dehydrogenase	gnl|CDD|223441	COG0364, Zwf, Glucose-6-phosphate 1-dehydrogenase [Carbohydrate transport and metabolism].	0
NZ_CP032471.1|WP_001126887.1|422826_423837_-|glucokinase	gnl|CDD|129832	TIGR00749, Glucokinase_Glucose_kinase., glucokinase, proteobacterial type. This model represents glucokinase of E. coli and close homologs, mostly from other proteobacteria, presumed to have equivalent function. This glucokinase is more closely related to a number of uncharacterized paralogs than to the glucokinase glcK (fromerly yqgR) of Bacillus subtilis and its closest homologs, so the two sets are represented by separate models. [Energy metabolism, Glycolysis/gluconeogenesis].	0
NZ_CP032471.1|WP_139518222.1|421610_422657_-|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl|CDD|176186	cd05283, CAD1, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	6.0542e-160
NZ_CP032471.1|WP_139518216.1|412379_413213_-|outer-membrane-beta-barrel-protein	gnl|CDD|280099	pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.	2.68724e-35

Protein sequences

>NZ_CP032471.1|WP_139518220.1|418824_420132_-|hypothetical-protein
MIFLKKSLCALLFSGFLTPPLMKAASFVYDLKFMSFNFNLVAPNNNPYWNSLTKMQGRLMPQIGVQLDKRQALMFGAWFIQNLHTHYSYFPYSWGVTMYYQYIGKNLRFFLGIVPRSYQIGHYPLSAFKKLFWFIDPTFRGGAFQFKPAYDPNRWWNGWFEGVVDWYGGRNWNNQPKKKNYDFDQFLYFVSSEFQFLKGYLGLGGQLVIFHNASPHSMGDNYPYGGNSYLKPGDATPQWPNGYPYFSQKNNPQGGEIGKYSNPTILDRVYYHAYLKADFKNLMPYMDNIFMTFGTQSSQTHYCVRYASECKNAQFYNSFGGEFYAQAQYKGFGIFNRYYFSNKPQMHFYATYGQSLYTGLPWYRAPNFDMIGLYYVYKNKWVSVRADAFFNFLGGGDGYHLYGKGGKWITTYQQFLTLTIDTRELIDFVKSKTSK
>NZ_CP032471.1|WP_139518219.1|418155_418818_+|outer-membrane-beta-barrel-protein
MDKTMVKILMGMALLSSLQAAEAELDEKSKKPKFADRNTFYLGIGYQLSAINTSFSTESVDKSYFMTGNGFGVVLGGKFVAKTQAVEHVGFRYGLFYDQTFSSHKSYISTYGLEFSGLWDAFNSPKMFLGLEFGLGIAGATYMPGGAMHGIIAQNLGKENSLFQLLVKVGFRFGFFHNEITFGLKFPVIPNKRTEIIDGLSATTLWHRLPVAYFNYIYNF
>NZ_CP032471.1|WP_128045459.1|417306_417867_-|pyruvate-flavodoxin-oxidoreductase-subunit-gamma
MFQIRWHARAGQGAITGAKGLADVISKTGKEVQAFASYGSAKRGAAMMAYNRVDDEPILNHERFMEPDYVLVIDPGLVFIENIFANEKEDTTYIITSYLSKEELFEKKPELKTRKVFLVDCLKISMETLKRPIPNTPMLGALMKVSGMLEIGAFKEAFKKVLGKKLTQEVIDANMLAIQRAYEEVQ
>NZ_CP032471.1|WP_000656174.1|416898_417291_-|4Fe-4S-binding-protein
MKDWNEFEMGAVLFPFEKNAQSEMEKHNDERHYTEQSYFTTSVAHWRVAKPVHNNNICINCFNCWVYCPDAAILSREGKLKGVDYSHCKGCGVCVDVCPTNPKSLWMFEEQIEPATALTQWPQKQEKKKS
>NZ_CP032471.1|WP_139518218.1|415665_416889_-|2-oxoacid:ferredoxin-oxidoreductase-subunit-alpha
MAKSIELQEIEVWDGNTASSNALRQAQIDVIAAYPITPSTPIVQNYGTFKDNGYIDGEFVLVESEHAAMSACVGAAAAGGRVSTATSSQGLALMVEVLYQASGMRLPIVLNLVNRALAAPLNIHGDHSDMYLSRDSGWVSLCTCNPQEAYDFTLMAFKIAEHQKVRVPTIVNQDGFLCSHTVQNVRPLSDAVAYQFVGEYQTKHSLLDFDKPVSYGAQAEEEWHYEHKAQLHHAIMSASSVIEEVFNDFAKLTGRQYHLTKTFQLEDAEIAIFALGTTYESAIVAAKEMRKKGIKAGVATIHSLRPFPYERLGQDLKNLKALAILDKSSPAGAMGAMFNEVTSAVYQTQGTKHPVVSNYIYGLGERDMTIAHLCEIFEEINEDALKGTLTHPTQQFVGLHGPKMSFF
>NZ_CP032471.1|WP_000238149.1|414708_415653_-|pyruvate-ferredoxin-oxidoreductase-subunit-beta
MVKEVKTLKGFSQSAEKFQGSHLLCPGCGHGIIVREVLNAVDGPIVLGNSTGCLEVCSAVYPHTSWDVPWIHIGFENGSTAISGVEAMYKALVNKGRYQGQKPKFVAFGGDGASYDIGFQFISGCMERGHDMTYICLDNENYANTGGQRSGSTPLGASTSTTPAGSVSFGKKEKKKDIVNIMASHGVPYVAQLSPNKWKDMNKKIKTALDTEGPCFINALSPCTTEWKFESNKTIELADMAVDSLMFPLFEIFNGRELKITYRPRNIIPVRDYLGAQKRFKHLFKKENEHIIEELQKDVNERWEYLQRREEAKV
>NZ_CP032471.1|WP_139518217.1|413277_414600_-|adenylosuccinate-lyase
MLERYANEEMKALWNEQTKFETYLEVEKAVVRAWNKLGQIQDSDCEKICTKAAFNLERIKEIEKTTKHDLIAFTTCVAESLGEESRFFHYGITSSDCIDTAMALLMTKSLKLIQKSVKNLYETLKNRALEHKDTLMVGRSHGVFGEPITFGLVLALFADEIKRHLKALDLTMEFISVGAISGAMGNFAHAPLELEELACEFLGLKTANISNQVIQRDRYARLACDLALLASSCEKIAVNIRHLQRSEVYEVEEAFSTGQKGSSAMPHKRNPILSENITGLCRVIRSFTTPMLENVALWHERDMSHSSVERFALPDLFITSDFMLSRLNSVIKNLVVYPKNMLKNLALSGGLVFSQRVLLELPKKGLSREESYSIVQENAMKIWKVLQQGAFKNADENLFLNALLNDERLKKYLSEDEIKACFDYSYYTKNVGAIFKRVFE
>NZ_CP032471.1|WP_139518216.1|412379_413213_-|outer-membrane-beta-barrel-protein
MKRALYLILGLSYALHADSFKDVLTKGDYTFFNKKVVSPIKRYADQSAFYLGIGYQLGSVQHNSSNLNLSQQFNKSQIIFSDGLSPVFKNSYVSNGLGVQVGYKWVGKHEETKWFGFRWGLFYDLSASLYGQKESQSIIISTYGTYMDLLLNAYNGDKFFAGFNLGIAFAGVYDKLSDALLYQALLLDTFGGKVDPNGFQFLVNLGVRLGNKRNQFGFGIKIPTYYFNHYYSMNNISNNSGDVLKVLRFLEYGINSLLYQVDFRRNYSVYFNYTYSF
>NZ_CP032471.1|WP_139518215.1|410406_412383_+|excinuclease-ABC-subunit-B
MPLFDLKSPYPPAGDQPQAIEALTKSLKNNNHYQTLVGVTGSGKTYTMANIIAQTNKPTLIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKCAYKSFLLKLVEMGYSRNEVVFDRGSFRAIGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALEKNEIRRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKMLEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARDERVLITTLTKKMAEELCKYYAEWGLKARYMHSEIDAIERNHIIRSLRLKEFDILIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFEITSYRRAKQEEFNKIHNITPKTVTRALEEELKLRDDEIRIAKALKKDKMPKSEREKIIKELDKKMRECAKNLDFEEAMRLRDEIAKLRTL
>NZ_CP032471.1|WP_139535462.1|409705_410356_+|hypothetical-protein
MNYLNLPNSVLEIIEQPEVKEITNELLKQLQNALNSNSLFTEQVELSLKGIVRILEVLLSLDFFKNANEIDSSLRNSIEWLSNAGESLKAKMKEYEGFFSEFNTSMKANEQEVTSILNANIENIKSEIKKLENQLIETTTRLLTSYQIFLNQARENATTQINTNKTASLEAIAQEKQQATSEINEAIGQPKEQAKNEISGAKKTDHYQNIDFFEIE
>NZ_CP032471.1|WP_139518222.1|421610_422657_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MRIQSKGFAIFSKDGHFKPHDFSRHAVGPKDVLIDILYAGICHSDVHSAYSEWKEGIYPMVPGHEIAGVIKEVGKEVKKFKVGDVVGVGCFVNSCKACKPCKEHQEQFCAKVVFTYDCLDSFHGNEPHMGGYSNNIVVDENYVISVDKNAPLEKVAPLLCAGITTYSPLKFSKVTKGTKVGVAGFGGLGSMAVKYAVAMGAEVSVFARNEHKKQNALSMGVKHFYTDPKQCKEELDFIISTIPTHYDLKDYLKLLTYSGELALVGLPPVEVAPVLSVFDFIHLGNRKVYGSLIGGIKETQEMMDFSIKHNIYPEIDLILGKDIDTAYHNLTHGKAKFRYVIDMKKSFD
>NZ_CP032471.1|WP_001126887.1|422826_423837_-|glucokinase
MPKTETYPRLLADIGGTNARFGLEVAPRQIECIEVLRCEDFESLSDAVRFYLSKCKESLKLHPIYGSFAVATPIMGDFVQMTNNHWTFSIETTRQCLTLKKLLVINDFVAQAYAISAMQENDLAQIGGIKCEINAPKAILGPGTGLGVSTLIQNSDGSLKVLPGEGGHVSFAPFDDLEILVWQYARSKFNHVSAERFLSGSGLVLIYEALSKRKGLEKVAKLSKAELTPQIISERALNGDYPICRLTLDTFCSMLGTLAADVALTLGARGGVYLCGGIIPRFIDYFKTSPFRARFETKGRMGAFLASIPVHVVLKKTPGLDGAGIALENYLLHDKI
>NZ_CP032471.1|WP_139518223.1|423823_424507_-|6-phosphogluconolactonase
MGYQLFEFENLKDCHKALIERFKEFFNTALKKHHQVSIAFSGGRSPIGLLQKLSVLDLKWHECLISLVDERIIDTSHEDSNTKLLHDYLLQNNALKASFIPLLPKKISNDTNALFHFANQHFKQPHLAILGMGTDGHTASLFPETSAFLNEEKENIVLTKPTNAPYERLSMSVNALENCEKLFLSISGVEKREILEKALKENAPYSLPIARILHSQKVTTEVFYAKN
>NZ_CP032471.1|WP_139518224.1|424517_425795_-|glucose-6-phosphate-dehydrogenase
MLDFDLVLFGATGDLAMRKLFVSLYEIYTHYGFKKDSKIIASGRKELSNEEFLALLCEKTQLRSREKGEEFLAHISYLRVRLDNPKDFEKLSKIATKNKPLIFYFSISPSFFATTAQNLAQNALNHANTRLILEKPLGHDLKTCKEIFQSISAFFKEEQIFRIDHYLGKKGVQNILELRLNNPILNILWDQISAVEICVYETLGVEERGEFYDKIGALRDMVQNHLLQVLSLIATDLPNDLKDLRKEKIKVLKTLQPPKDFKKQVIRAQYQGYRDENKVHKESQTETFVAIKAFLDTPKFKGVPFYLKHAKKMPRNQASVKIHFNAVNTLEFFLSQDKITLTLKDHQNPLILETHNKQEFLQPYAKLLYDAIQNNHNNFAHQLELEASWVFIDTLIEGFMNNATPLYSYESHNLNELEFLKPLYQ
>NZ_CP032471.1|WP_139518225.1|425860_427687_+|phosphogluconate-dehydratase
MPKHSLEQIKEKITERSKKTRELYLENIFNPKNQPKIESLGCANIAHVTASMPEHLKMPLGSHKRKHFAIITAYNDMLSAHQPFKNYPDWIKKELQEHNAYASVASGVPAMCDGITQGYDGMELSLFSRDVIALSTAVGLSHNVFDGAFFLGVCDKIVPGLLIGALSFGNLASVFVPSGPMVSGIENYKKAKARQDFAMGKINREELLKVEMQSYHDVGTCTFYGTANSNQMMMEFMGLHVANSSFINPNNPLRKVLVEESAKRLASGKVLPLAKLIDEKSILNALIGLMATGGSTNHTLHLIAIARSCGVILNWDDFDAVSNLIPLLAKVYPNGSADVNAFEACGGLAFVIKELLKEGLLFEDTHTIMDTETQKGMQNYTKTPFLENDQLVYKDAVNHSLNTDILRPVSEPFAANGGLKILKGNLGRAVIKISAIKDEHRKVRARAIVFKTQSEFLERFKNKELERDFVAVLPFQGPKSNGMPELHKLTTNLGALQDMGYKVALVTDGRMSGASGKVPSAIHLSPEGALNGAIIKIKDGDLIELDAPNNALNVLEKDFEDRGINPLFLETLENLEKPSFGLGRELFTSLRLNVNTAEEGGMSFGIKV
>NZ_CP032471.1|WP_139518226.1|427705_428332_+|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase
MQDKIIEVLQISPIVPVVVVEDIKDAVPLAQSLIEGGIPIIEVTLRSSCALEAIELIAKNVPKMRVGAGTILNPTQLEQAQNRGAEFLISPGLTIKLLEHAKKKDMPLIPGVSSSSEVMQALELGYNALKFFPAEYCGGVKLLNAFNGPFKGVKFCPTGGISADNMRSYLNLENVLCVGGSWLTPKNLIQNKEWDKITEICKRALTLR
>NZ_CP032471.1|WP_139518227.1|428401_429274_+|Sel1-like-repeat-protein-HcpC
MLENVKKSLFRVLCLGALCLGGLMAEQDPKELVGLGAKSYKEQDFTQAKKYFEKACDLKENSGCFNLGVLYYQGQGVEKNLKKAASFYAKACDLNYSNGCHLLGNLYYSGQGVSQNTNKALQYYSKACDLKYAEGCASLGGIYHDGKVVTRDFKKAVEYFTKACDLNDGDGCTILGSLYDAGRGTPKDLKKALASYDKACDLKDSPGCFNAGNMYHHGDGATKNFKEALARYSKACELENGGGCFNLGAMQYNGEGITRNEKQAIENFKKGCKLGAKGACDILKQLKIKV
>NZ_CP032471.1|WP_139518228.1|429457_430210_-|SDR-family-NAD(P)-dependent-oxidoreductase
MAHILVSGATSGFGLEIAKAFLQKNHVVFGAGRRKENLQKLQLAYPKHFIPLCFDLKNKLETKRAIETIFSMTDRIDALINNAGLALGLNKAYECELDDWEIMIDTNIKGLLYLTRLILPSMIEHNYGTIINLGSIAGTYAYPGGNVYGASKAFVKQFSLNLRADLAGTNIRVSNVEPGLCGETEFSMVRFKGDKIKAQSVYENTIYLKPQDIANIVLWIYEQPLHVNINRIEIMPISQTFAPLPTHKNP
>NZ_CP032471.1|WP_139518229.1|430231_431767_-|hypothetical-protein
MKKLLYTLLALLLIGLLTTYLILFTEWGNKIIASYIEKKINPNERYLSVKTFKLRFNSLDFKAQANDDSTLILKGDFSLLKQSVNLDYYIDIKNLRSFKDLIPYPLRGAIVTSGNIKGHRKALVIQGVSNAAQSHTAYNALLDDFKLSHLSLNAQDAHLEDLLYLFNRPAYANAKVSLQADFNSLKPLEGHLILTANNALINNALINQMFHLNLKDTLIFNLSHSSDFKENKAISDTTLTSPLANFTALKSEYLFSILKLNAPYTLEIPNLAKLYNITNHPLKGSLTLKGAIEQSPKLLKVSGHSNLLDGALDFTLLNKDLKGRFSNISTLKALDLFHYPKFFQSIADANLDYNLSTKQGVLKARLKNARFLKNAFSDFLYSISKFDITKEIYNDANLISQINQQRLLSSLSLKSPKTQLKIHNGLLDLNTKQMDMLMDAEILKFVFKMKLQGNMHQPKFSLILNEKAIQQNLQQGLKEILKNDTLKKGLDHLLKDDKLKEKLEKGLKGLF
>NZ_CP032471.1|WP_139518230.1|432589_433624_+|UDP-glucose-4-epimerase-GalE
MALLFTGACGYIGSHTARAFLEKTKENIIIVDDLSTGFLEHIKALEHYYPNRVVFIQANLNETHKLDAFLNKQQLKDPIEAILHFGAKISVEESTRLPLEYYTNNTLNTLELVKLCLKHAIKRFIFSSTAVVYGESDFSLNEESPLNPINPYGASKMMSERILLDTSKITDFKCVILRYFNVAGACMHNDYTTPYTLGQRTLNATHLIKIACECAVGKRKKMGIFGTNYPTRDGTCIRDYIHVDDLANAHLASYQTLLEKNKSEIYNVGYNQGHSVKEVIEKVKEISNNDFLVEILDERQGDPASLIANNAKILQNTPFKPLYNNLDTIIKSALDWEEHLLRFQ

Crispr_ID: NZ_CP032471_3

• CRISPR_ID: NZ_CP032471_3
• CRISPR_location: 582880-583077
• CRISPR_type: Orphan
• Repeat_type: I-B
• Spacer_info: 3 spacers

Consensus repeat of NZ_CP032471_3

Consensus_repeat	Method
ATTAAAATTATAAGTCCCTTGATTGAA	CRISPRCasFinder

spacers of NZ_CP032471_3

>3.1|582907|27|NZ_CP032471|CRISPRCasFinder
AGTGTCGTTATTAAAGCTGGCGTTGCC
>3.2|582961|30|NZ_CP032471|CRISPRCasFinder
AGCACTGTCATTAAAAGCAGATTGAGTGCT
>3.3|583018|33|NZ_CP032471|CRISPRCasFinder
GCTACTATTATCAAAGCTTGAACTTGCACTGTT

CRISPR arrays and Neighbor proteins around NZ_CP032471_3

CRISPR arrays

The CRISPR arrays of NZ_CP032471_3

>merge|NZ_CP032471|3|582880-583077|CRISPRCasFinder
ATTAAAGTCATAAGTCCCTTGATTGAAAGTGTCGTTATTAAAGCTGGCGTTGCCATTAAAATTATAAGTCCCTTGATTGAAAGCACTGTCATTAAAAGCAGATTGAGTGCTATTAAAATTGTAAGTCCCTTGATTGAAGCTACTATTATCAAAGCTTGAACTTGCACTGTTACTAAAGTTATAAGTGCCTTGATTGAA

>NZ_CP032471|3|3|582880-583077|CRISPRCasFinder
ATTAAAGTCATAAGTCCCTTGATTGAA	AGTGTCGTTATTAAAGCTGGCGTTGCC
ATTAAAATTATAAGTCCCTTGATTGAA	AGCACTGTCATTAAAAGCAGATTGAGTGCT
ATTAAAATTGTAAGTCCCTTGATTGAA	GCTACTATTATCAAAGCTTGAACTTGCACTGTT
ACTAAAGTTATAAGTGCCTTGATTGAA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP032471.1|WP_139518322.1|598697_600734_-|UvrD-helicase-domain-containing-protein	unknown	unknown	gnl|CDD|223288
NZ_CP032471.1|WP_139523661.1|594760_596323_-|Hop-family-adhesin-AlpB	unknown	unknown	gnl|CDD|280099
NZ_CP032471.1|WP_139518311.1|572481_573462_-|zinc-metalloprotease-HtpX	unknown	unknown	gnl|CDD|235081
NZ_CP032471.1|WP_139518316.1|585079_585772_+|Bax-inhibitor-1/YccA-family-protein	unknown	unknown	gnl|CDD|198414
NZ_CP032471.1|WP_139518319.1|589825_592267_+|TonB-dependent-receptor	unknown	unknown	gnl|CDD|273808
NZ_CP032471.1|WP_097689585.1|592522_594067_+|outer-membrane-beta-barrel-protein-HofG	unknown	unknown	gnl|CDD|334957
NZ_CP032471.1|WP_139518318.1|589132_589564_+|Sua5/YciO/YrdC/YwlC-family-protein	unknown	unknown	gnl|CDD|376519
NZ_CP032471.1|WP_139535476.1|575510_576614_-|Hop-family-outer-membrane-protein-HopJ/HopK	unknown	unknown	gnl|CDD|280099
NZ_CP032471.1|WP_139518317.1|585870_589128_+|carbamoyl-phosphate-synthase-large-subunit	unknown	unknown	gnl|CDD|235393
NZ_CP032471.1|WP_139518323.1|600737_601877_-|N-6-DNA-methylase	unknown	unknown	gnl|CDD|223897
NZ_CP032471.1|WP_001099598.1|574542_575124_-|recombination-protein-RecR	unknown	unknown	gnl|CDD|273176
NZ_CP032471.1|WP_139518310.1|571938_572481_-|GTP-cyclohydrolase-I-FolE	unknown	unknown	gnl|CDD|129173
NZ_CP032471.1|WP_139518308.1|570211_571015_-|5'/3'-nucleotidase-SurE	unknown	unknown	gnl|CDD|234732
NZ_CP032471.1|WP_139518307.1|568951_569554_-|6-pyruvoyl-tetrahydropterin-synthase-family-protein	unknown	unknown	gnl|CDD|223792
NZ_CP032471.1|WP_001115888.1|575252_575459_+|4-oxalocrotonate-tautomerase-family-protein	unknown	unknown	gnl|CDD|129125
NZ_CP032471.1|WP_139535478.1|596344_597868_-|Hop-family-adhesin-AlpA	unknown	unknown	gnl|CDD|280099
NZ_CP032471.1|WP_000042188.1|569555_570215_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518315.1|583936_584935_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|273675
NZ_CP032471.1|WP_139518309.1|571011_571923_-|polyprenyl-synthetase-family-protein	unknown	unknown	gnl|CDD|223220
NZ_CP032471.1|WP_139518312.1|573400_574546_-|tRNA-pseudouridine(13)-synthase-TruD	unknown	unknown	gnl|CDD|272903

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP032471.1|WP_139518322.1|598697_600734_-|UvrD-helicase-domain-containing-protein	gnl|CDD|223288	COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].	3.2867e-134
NZ_CP032471.1|WP_139523661.1|594760_596323_-|Hop-family-adhesin-AlpB	gnl|CDD|280099	pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.	1.77259e-53
NZ_CP032471.1|WP_139518311.1|572481_573462_-|zinc-metalloprotease-HtpX	gnl|CDD|235081	PRK02870, PRK02870, heat shock protein HtpX; Provisional.	0
NZ_CP032471.1|WP_139518316.1|585079_585772_+|Bax-inhibitor-1/YccA-family-protein	gnl|CDD|198414	cd10432, BI-1-like_bacterial, Bacterial BAX inhibitor (BI)-1/YccA-like proteins. This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.	1.673e-52
NZ_CP032471.1|WP_139518319.1|589825_592267_+|TonB-dependent-receptor	gnl|CDD|273808	TIGR01786, hemoglobin-haptoglobin-binding_protein, TonB-dependent hemoglobin/transferrin/lactoferrin receptor family protein. This model represents a family of TonB-dependent outer membrane receptor/transporters acting on iron-containing proteins such as hemoglobin, transferrin and lactoferrin. Two subfamily models with a narrower scope are contained within this model, the heme/hemoglobin receptor family protein model (TIGR01785) and the transferrin/lactoferrin receptor family model (TIGR01776). Accessions which score above trusted to this model while not scoring above trusted to the more specific models are most likely to be hemoglobin transporters. Nearly all of the species containing trusted hits to this model have access to hemoglobin, transferrin or lactoferrin or related proteins in their biological niche. [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins].	8.83716e-44
NZ_CP032471.1|WP_097689585.1|592522_594067_+|outer-membrane-beta-barrel-protein-HofG	gnl|CDD|334957	pfam02521, HP_OMP_2, Putative outer membrane protein. This family consists of putative outer membrane proteins from Helicobacter pylori (campylobacter pylori).	1.96126e-179
NZ_CP032471.1|WP_139518318.1|589132_589564_+|Sua5/YciO/YrdC/YwlC-family-protein	gnl|CDD|376519	pfam01300, Sua5_yciO_yrdC, Telomere recombination. This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.	8.09679e-05
NZ_CP032471.1|WP_139535476.1|575510_576614_-|Hop-family-outer-membrane-protein-HopJ/HopK	gnl|CDD|280099	pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.	3.74797e-47
NZ_CP032471.1|WP_139518317.1|585870_589128_+|carbamoyl-phosphate-synthase-large-subunit	gnl|CDD|235393	PRK05294, carB, carbamoyl-phosphate synthase large subunit.	0
NZ_CP032471.1|WP_139518323.1|600737_601877_-|N-6-DNA-methylase	gnl|CDD|223897	COG0827, COG0827, Adenine-specific DNA methylase [DNA replication, recombination, and repair].	6.78088e-53
NZ_CP032471.1|WP_001099598.1|574542_575124_-|recombination-protein-RecR	gnl|CDD|273176	TIGR00615, Recombination_protein_RecR, recombination protein RecR. All proteins in this family for which functions are known are involved in the initiation of recombination and recombinational repair. RecF is also required. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair].	4.16127e-98
NZ_CP032471.1|WP_139518310.1|571938_572481_-|GTP-cyclohydrolase-I-FolE	gnl|CDD|129173	TIGR00063, GTP_cyclohydrolase_1, GTP cyclohydrolase I. alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].	1.57691e-105
NZ_CP032471.1|WP_139518308.1|570211_571015_-|5'/3'-nucleotidase-SurE	gnl|CDD|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	1.03381e-125
NZ_CP032471.1|WP_139518307.1|568951_569554_-|6-pyruvoyl-tetrahydropterin-synthase-family-protein	gnl|CDD|223792	COG0720, COG0720, 6-pyruvoyl-tetrahydropterin synthase [Coenzyme metabolism].	6.25641e-22
NZ_CP032471.1|WP_001115888.1|575252_575459_+|4-oxalocrotonate-tautomerase-family-protein	gnl|CDD|129125	TIGR00013, Probable_tautomerase_K2, 4-oxalocrotonate tautomerase family enzyme. 4-oxalocrotonate tautomerase is a homohexamer in which each monomer is very small, at about 62 amino acids. Pro-1 of the mature protein serves as a general base. The enzyme functions in meta-cleavage pathways of aromatic hydrocarbon catabolism. Because several Arg residues located near the active site in the crystal structure of Pseudomonas putida are not conserved among all members of this family, because the literature describes a general role in the isomerization of beta,gamma-unsaturated enones to their alpha,beta-isomers, and because of the presence of fairly distantly related paralogs in Campylobacter jejuni, the family is regarded as not necessarily uniform in function. [Energy metabolism, Other].	4.5194e-26
NZ_CP032471.1|WP_139535478.1|596344_597868_-|Hop-family-adhesin-AlpA	gnl|CDD|280099	pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.	4.61705e-54
NZ_CP032471.1|WP_139518315.1|583936_584935_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl|CDD|273675	TIGR01534, Glyceraldehyde-3-phosphate_dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, type I. This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis].	1.33296e-160
NZ_CP032471.1|WP_139518309.1|571011_571923_-|polyprenyl-synthetase-family-protein	gnl|CDD|223220	COG0142, IspA, Geranylgeranyl pyrophosphate synthase [Coenzyme metabolism].	1.83426e-76
NZ_CP032471.1|WP_139518312.1|573400_574546_-|tRNA-pseudouridine(13)-synthase-TruD	gnl|CDD|272903	TIGR00094, tRNA_pseudouridine_synthase_D, tRNA pseudouridine synthase, TruD family. an EGAD loading error caused one member to be called surE, but that's an adjacent gene. MJ11364 is a strong partial match from 50 to 230 aa. [Protein synthesis, tRNA and rRNA base modification].	6.99411e-141

Protein sequences

>NZ_CP032471.1|WP_139535476.1|575510_576614_-|Hop-family-outer-membrane-protein-HopJ/HopK
MPKTLLHSSFFLPLFLSFCSAEENGAYASVGFEYSISHAIQHNDPFLNQERIQIISNAQNKIYKLNQVKNEIKGMPNTFNYINNALKNNAKLTPTEMQAEKYYLQSSFENIEKIVMLSGGVASNPQLAQALEKMQEPITNPLELVENLKNLELQFAQSQNRMLSSLSSQIAAISNSLNALDPSSYSKNISSMYGVSLSVGYKHFFTKKKNQGLRYYLFYDYGYTNFGFVCNGFDGLGKMNNHLYGLGIDYLYNFIDNAQKHSSVGFYVGFALAGSSWVGSGLGMWVSQRDFINNYLTDYQAKMHTSFFQIPLNFGVRVNVNRHNGFEMGLKIPLVVNSFYETHGKGLNTSLFFKRLVVFNVSYVYSF
>NZ_CP032471.1|WP_001115888.1|575252_575459_+|4-oxalocrotonate-tautomerase-family-protein
MPFINIKLVPENGGPTNEQKQQLIEGVSDLMVKVLNKNKASVVVIIDEVDSNNYGLGGESVHHLRQKN
>NZ_CP032471.1|WP_001099598.1|574542_575124_-|recombination-protein-RecR
MNTYKNSLNHFLNLVDCLEKIPNVGKKSAFKMAYHLGLENPYLALKITHALENALENLKTCASCNALSESEVCEICSDESRQNSQLCMVLHPRDVFILEDLKDFLGRYYVLNSIEEVDFNALEKRLIEENIKEIIFAFPPTLANDSLMLYIEDKLQHFHLTFTKIAQGVPTGVNFENIDSVSLSRAFNSRIKA
>NZ_CP032471.1|WP_139518312.1|573400_574546_-|tRNA-pseudouridine(13)-synthase-TruD
MNLNFMPLLHAYNHASIDFHFNSSARDFCVHEVPLYEFSNTGEHAVIQVRKSGLSTLEMLQIFSQILGVKIAELGYAGLKDKNALTTQFVSLPKKYAPLLEKNTSNFQERNLKILSLNYHHNKIKLGHLKGNRFFMRFKKMTPLNAQKTKQVLEQIAQFGMPNYFGSQRFGKFNDNHKEGLKILQNETKFAHQKLNAFLISSYQSYLFNSLLSKRLEISKIISAFSLKENLEFFKQKNLSVNSNALKALKNQAHPFKILEGDVMCHYPYGKFFDALELEKESERFLKKEAVPTGLLDGKKALYAKNLSLEIEKEFQHNLLNSHAKTLGSRRFFWVFAENVTSQYIKEKAQFELGFYLPKGSYASALLKEIKHEKGENNDEF
>NZ_CP032471.1|WP_139518311.1|572481_573462_-|zinc-metalloprotease-HtpX
MRARCSKKSSMRKEKIMTNFEKIIAQNRIKTNAVLATYCVIFAFIGLLVDVIRINANDLGIALFKLMTFQIFPTITMIMFLAAFVIIVVCIQNFSSIMLSGDGYKLIDTSKVLSSKENQIHRLLLELLEEAKLHFEPKLYIINAPYMNAFASGWNESNSLIALTSALIERLDKDELKAVIAHELSHIRHNDIRLTMCVGILSNIMLLVANFSVYFFMGNRKNSGANLARMILWALQIVLPFLTLILQMYLSRTREYMADSGAAFLMHDNKPMIRALQKISNDYANNDYKGIDQNSTRSAAYLFNAEMFSTHPSVKNRIQSLRKRVI
>NZ_CP032471.1|WP_139518310.1|571938_572481_-|GTP-cyclohydrolase-I-FolE
MENFFNQFFESIGEDKNREGLKETPKRVQELWKFLYKGYKEDPKVALKSAYFQGVCDEMIVAQNIEFYSTCEHHLLPFLGNISLGYIPKEKIVGISAIAKLIEIYSKRLQIQERLTTQIAETFDEIIEPRGVIVVCEAKHLCMSMQGVQKQNAIIKTSVLKGLFKKDPKTRAEFMQLLKS
>NZ_CP032471.1|WP_139518309.1|571011_571923_-|polyprenyl-synthetase-family-protein
MSSPNLSFYYNECERFESFLNHHHLHLESFHPYLEKAFFEMVLNGGKRFRPKLFLAVLCALVGQKDYSNQQTEYFKIALSIECLHTYSLIHDDLPCMDNAALRRNHPTLHAKYDETTAVLIGDALNTYSFELLSNSLLESHIIVELIKILSVNGGIKGMVLGQALDCYFENTPLNLEQLTFLHEHKTAKLISASLMMGLVASGIKDEELFKWLQAFGLKTGLCFQVLDDIIDVTQDEEESGKTTHLDSAKNSFVNLLGLKKASDYAQTLKTEVLNDLNLLKPAYPLLQENLNALLNTLFKGKT
>NZ_CP032471.1|WP_139518308.1|570211_571015_-|5'/3'-nucleotidase-SurE
MKRILLTNDDGYHAKGIKALEQALENMAEVYVVAPKHEKSACSQCITITAPLRAEKIKGKEGRHYRIDDGTPSDCVYLAINELFKHVCFDLVISGINLGSNMGEDTIYSGTVAGAIEGTIQGVPSIAISQILSNKNKNTPLSFDLAQKIIQDLVQNIFTNGYPLKGRKLLNVNIPNCSLQEYKGERITPKGYRLYKKEVHKRTDPKNESYFWLGLHPLEWQKRENEDRLSDFDAIASNHASITPLNLDLTSYDDLKSLESWHEGMLK
>NZ_CP032471.1|WP_000042188.1|569555_570215_-|hypothetical-protein
MSKNRRLAFLGLIVGVFFFFNACQHRLHMGYYSEVTGDYLFNYNSTIVVAYDRSDAMTSYYINVIVYELQKLGFYNVFTQAEFPLDKAKNVIYARIVRNISAVPFYQYNYQLIDQVNKPCYFLGGQFYCSQTPTDYYAINGFSEQILMSANSHFILDWYDVVLQKRVLYVDGSVSGRTCGYQMLYRDLIKSTIKRIDFNRPERYYYNLRLPLYQPCYRQ
>NZ_CP032471.1|WP_139518307.1|568951_569554_-|6-pyruvoyl-tetrahydropterin-synthase-family-protein
MVIRRLYQFCASHVVRNCSSLKCAQNIHGHNYEVEVFIETDRLDSANMALDFGLMQQEMQVFIESFDHAHHFWDKESDEFQRFIENHCVRYVKCSFNLSAESYALMFLYYLTKILQKSVFSNSEGELKVSSVRVHETKNGYAESFLKDLENPHFKSLVHNHCISFSQGIQNLWHDKDFFNKIISDEKQCFFHAKPLHQIL
>NZ_CP032471.1|WP_139518315.1|583936_584935_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MKIFINGFGRIGRCVLRAILERNDTNPKLEVIGINDPANWEILAYLLEHDSVHGLLPKEVRYSNCKLIIGSLEIPVFNSIKDLKGVDVILECSGKFLEPKTLENYLLLGAKKVLLSAPFMGEYDEKQYPTLVYGVNHFLYQNQAIVSNASCTTNAIAPICAILDKAFNIKEGMLTTIHSYTSDQKLIDLAHPLDKRRSRAAASNIIPTTTKAALALHKVLPNLKNKMHGHSVRVPSLDVSMIDLSLFLEKKAPKDPINDLLIEASKGVLKGVLEIDLKERVSSDFISNPSSVIIAPDLTFTLENMVKIMGWYDNEWGYSHRLVDMAQFVYHY
>NZ_CP032471.1|WP_139518316.1|585079_585772_+|Bax-inhibitor-1/YccA-family-protein
MALYDRANSRNAYAEDSLLHESELVSFVKTTYKFFAGSLLLATIGALLGLMNFQAVVQYKWVFFIAEIAALFGLMFSKSKPGLNLFMLFAFTSLSGVTLVPLLGMVIAKAGLGAVWQALGMTTIVFGLMSVYALKTKNDLANMGKMLFIALIVVLVCSLINLFLGSPMFQVVIAGSSAILFSLYIAYDTQNIVKGMYDSPIDAAVDLYLDFLNVFISILQIIGIFSDRDK
>NZ_CP032471.1|WP_139518317.1|585870_589128_+|carbamoyl-phosphate-synthase-large-subunit
MPKRTDISNILLIGSGPIVIGQACEFDYSGTQSCKTLKSLGYRVILINSNPATVMTDPEFSHQTYIQPITGENIAAIIEKEKIDAILPTMGGQTALNAVMQMHQKGMLEGVELLGAKIEAIKKGEDRQAFKEAMLKIGMDLPKGRYAYNELEALEAINEIGFPAIIRASFTLAGGGSGVAYNIEEFQELAKNALDASPINEILIEESLLGWKEYEMEVIRDSKDNCIIVCCIENIDPMGVHTGDSITIAPSLTLTDKEYQRMRDASFAILREIGVDTGGSNVQFAIHPETLRMVVIEMNPRVSRSSALASKATGFPIAKVATMLAVGFSLDEIQNDITNTPASFEPSLDYIVVKIPRFAFEKFAGVSSTLGTSMKSIGEVMAIGGNFLEALQKALCSLENNWLGFESLSKDLEMIKKEIRRPNPKRLLYIADAFRLGVCVDEVFELCQIDRWFLSQIQKLVKAEESINSSVLTDAKKLRELKNLGFSDARIAAKIKENENLEVSPFEVELARSNLQIAPNFEEVDTCAAEFLSLTPYLYSTYAPNPLPPIGNKQEKKEKKILIIGSGPNRIGQGIEFDYCCVHASFALKDLNIKSVMLNCNPETVSTDYDTSDTLYFEPIHFECVKSIIQRERVDGIIVHFGGQTPLKLAKDLAKMQAPIIGTPFKVIDIAEDREKFSLFLKELDIKQPKNGMAKSVDEAYSIANVIGFPIIVRPSYVLGGQHMQILENIEELHHYLESVTHSLEISPKNPLLIDKFLEKAVELDVDVICDKKEVYIAGILQHIEEAGIHSGDSACFIPSTLNPEILDEIERVSAKIALHLGVVGLLNIQFAVHQNSLYLIEVNPRASRTVPFLSKALGVPLAKVATRVMVLEDLKEALKFYDKKNIVEYSNGVYKPKMPHFVALKEAVFPFNKLYGSDLILGPEMKSTGEVMGIARSLGLAFFKAQTACFNPIKNKGLIFVSIKDKDKEEACVLMKRLVQLGFELCATEGTHKALEKAGVKSLKVLKISEGRPNIMDLMMNGEISMAINTSDHKSQDDAKLIRASVLKNHVSYFTTLSAIEVLLLALEESSKEDELLALQDYLK
>NZ_CP032471.1|WP_139518318.1|589132_589564_+|Sua5/YciO/YrdC/YwlC-family-protein
MALVYLVQSDTTIGLLSKDSEKLNALKNRPKNQSVLIESADFTTLKSLVRAPNAFKNLIRRSLKTTFIYPNSKAVRVIRGRHGDFLKRFKTLYSTSANLTQCAYDKEIASNLADAIVSDERGLFESSSSKIFRLYKNKKVRIR
>NZ_CP032471.1|WP_139518319.1|589825_592267_+|TonB-dependent-receptor
MNDKRFRKYCSFSIFLSLLGMFELEAKEEEKEERKTERKKDKKKNAQHTLGKVTTQAAKIFNYNNQTTISSKELERRQANQISDMFRRNPNINVGGGAVIAQKIYVRGIEDRLARVTVDGAAQMGASYGHQGNTIIDPGMLKSVVVTKGAAQASAGPMALIGAIKMETRSAGDFIPKGKDYAISGAATFLTNFGDRETIMGAYRNHHFDALLYYTHQNIFYYRDGDNAMKNLFDPKADNKVTASPSEQNNVMAKINGYLSERDTLTLSYNMTRDNANRPLRANFTGTFLPYSCGDFNAFPNEKNPSDCLFENDASLFKTYSVNLVHNVSLNYEREGGSRFGDPKLKINGYTSVRNVQIDPLFKPNDIAAIIPFTPNPKLSEENECVAQGGIYDALKQTCSITFKSLGGGSVVANKNLFIINSGFNANMIHTIDHKNDNLFEYGLNYQNLTTFDKAIPNSELVKPGDAPDACLRVTSPNDPNMNGRCQRNGATANVVGVYAQANYTLHPMVTLGAGTRYDVYTLVDKDWQLHITQGFSPSAALNVSPLENLNFRLSYAYVTRGPMPGGLVWMRQDNLRYNRNLKPEIGQNAEFNTEYSSQYFDFRAAGFVQLISNYINQFSSTLFVTNLPAQDIIYVPGYEVSGTAKYKGFSLGLSVARSWPSLKGRLIADVYELAATTGNVFILTASYTIPRTGLSITWLSRFVTNLSYCSYSPYRNGPTDIDRRPSHCPKTPGIFYVHKPGYGVSSFFITYKPTYKKLEGLSLNAVFNNVFNQQYIDQASPVMSPDEPNQDKYARGMAEPGFNARFEISYKF
>NZ_CP032471.1|WP_097689585.1|592522_594067_+|outer-membrane-beta-barrel-protein-HofG
MRQEKYFLTSSLSLLSFLLCPVEAFDYRFSGRVENFSKIGFNNSQINTKKGIYPTESFIDIVTLAQVKVNLLPKGTENHRLSVSLGGAIAAIPYDKTKYDINQANGKVFGSIVENFIGGYHGYFFNKYLGPAYAGTSQSASYHARPYVVDTAFLRYDYKDVFGFKAGRYEANIDFMSGSNQGWEVYYQPYKTETQRLRFWWWSSFGRGLAFNSWIYEFFATVPYLKKGGNPNNSNDFINYGWHGITTTYSYKGLDAQFFYYFAPKTYNAPGFKLVYDTNRNFENVGFRSQSMIMTTFPLYYRGWYNPETNTYSLEDSTPHGSLLGRNGVTLNIRQVFWWDNFNWSIGFYNTFGNSDAFLGSHTMPRGNNTSYIGSEISITTRHAGMIGYDFWDNTAYDGLADAITNANTFTFYTSVGGIHKRFAWHVFGRVSHANKNALGQVGRANEYSLQFNASYAFTESVLLNFRITYYGARINKGYQAGYFGAPKFNNPDGDFSANYQDRSYMMTNLTLKF
>NZ_CP032471.1|WP_139523661.1|594760_596323_-|Hop-family-adhesin-AlpB
MKQNLKPFKMIKENLMTQSQKVRFLAPLSLALSLSFNPVGAEEDGGFMTFGYELGQVVQQVKNPGKIKAEELAGLLNSNTTAGTGGNVAGTLGNLFMNQLGNLIDLYPTLKTSNIHQCGATNSSSSATTAATTNNNPCFQGNLPLYNGMVSSIKTLSQNISKNIFQGNNNTTSQNLSNQLSELNTASVYLTYMNSFLNANNQAGGIFQNNTNQAYGNGVTAQRIAYILKQASITMGPSGDSGAAAAFLDAALAQHVFNSANAGNDLSAKEFTSLVQNIVNNSQNALTLANNANISNSTGYQVSYGGNIDQARSTQLLNNTTNTLAKVTALNNELKANPWLGNFAAGNSSQVNAFNGFITKIGYKQFFGENKNVGLRYYGFFSYNGAGVGNGPTYNQVNLLTYGVGTDVLYNVFSRSFGSRSLNAGFFGGIQLAGDTYISTLRNSPQLASRPTATKFQFLFDLGLRMNFGILKKDLKSHNQHSIEIGVQIPTIYNTYYKAGGAEVKYFRPYSVYWVYGYAF
>NZ_CP032471.1|WP_139535478.1|596344_597868_-|Hop-family-adhesin-AlpA
MIKKNRTLFLSLALCASISYAEDDGGFFTVGYQLGQVMQDVQNPGGAKADELARELNADVTNNILNNNTGGNVAGALSNAFSQYLYSLLGAYPTKLNSNDVSANALLSGAVGSGTCAAAGTAGGTSLNTQSACTAAGYYWLPSLTDRILSTIGSQTNYGTNTNFPNMQQQLTYLNAGNVFFNAMNKALTNGATGSDGQTYSQKAIQYLQGQQNILNNAANLLKQDELLLEAFNSAVAANIGNKKFNSAAFTGLVQGIIDQSQSVYNELTKNTISGSAVNNAGINSNQANAVNTRASQLPNALYNAQVTLDKINALNNQVRSMPYLPQFRAGNSRSTNILNGFYTKIGYKQFFGKKRNIGLRYYGFFSYNGASVGFRSTQNNVGLYTYGVGTDVLYNIFSRSYQNRSVDMGFFSGIQLAGETFQSTLRDDPNVKLHGKINNTHFQFLFDFGMRMNFGKLDGKSNRHNQHTVEFGVVVPTIYNTYYKSAGTTVKYFRPYSVYWSYGYSF
>NZ_CP032471.1|WP_139518322.1|598697_600734_-|UvrD-helicase-domain-containing-protein
MLETLQLNPEQLKAASALQGYNLVIASAGTGKTSTIVGRILYLLDNGIKPEEILLLTFTNKASNEMIARVAKYFKLSSKIEAGTFHAVAYRYLKEHYPNLSLKQPKELRKLLESIVDTKNALNATDEDKKPYTSQHLYALYSLYTNALKQEDFSAWLSTKNPEHAPYAALYENILDEFENTKKKHNYIDYNDLLLLFKKAMLERPSPYKEVLCDEFQDTNPLQESILDAINPPSLFCVGDYDQSIYAFNGADISIISNFTQKYKNAQVFTLTKNYRSSKEILDLANQVIQRNERIYPKNLEVVKSGKFNKPTLLNYNDNIAQCQDIAKRIVMRKNFKEVAVIFRNNASADQLEAALRSHNVPSKRKGSASFFESKEVALALDICALLFNPKDIMAAIHVLSYISDIGSNTAKDIHEALMLLGNGDLKLALTHPSKEAKIYTKKKEITSMGLFEEIFALENSSRFNSVIDKAFHSHPVLMHPKISLNGAKMLSDFFILYTKAPIHSPSALIKHIIESAFFQTFKTRLLKERSKNKDGSYNEFKKLQAQKRFNEKMDLLSSLAKNYQNLGRFLNGTLIGSSEATQGEGVNLLSVHASKGLEFKDVYIIDLMEGRFPNHKLMNTGGGIEEERRLFYVAITRAKENLWLSYAKNELRENAKPKEHKPSVFLYEAGLLKPDSK
>NZ_CP032471.1|WP_139518323.1|600737_601877_-|N-6-DNA-methylase
MNNLDIKTLGQVFTPKKIVDFMLTLKHNQGSVLEPSAGDGSFLKRLKKAVGIEIDPKICPKNALCMDFFDYPLENQFDTIIGNPPYVKHKDIAPSTKEKLHYSLFDERSNLYLFFIEKAIRHLKPKGELIFITPRDFLKSTSSVKLNEWIYKEGTITHFFELGDQKIFPNAMPNCVIFRFCKGDFSRIANDGLQFLCKKGILYFLNQSYTQKLSEVFQVKVGAVSGCDKIFKNEKYGNLEFVTSITKRTNVLEKMVFVNEPNDYLLQHKDSLMQRKIKKFNENNWFEWGRMHHISPKKRIYVNAKTRQKNPFFIHQCPNYDGSILALFPYDQNLDLQNLCDKLNAINWQELGFVCDGRFLFSQRSLENALLPKDFLNLG

Crispr_ID: NZ_CP032471_4

• CRISPR_ID: NZ_CP032471_4
• CRISPR_location: 615744-615813
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP032471_4

Consensus_repeat	Method
TTTCTTTTTAAGGGATTTCTTTTT	CRISPRCasFinder

spacers of NZ_CP032471_4

>4.1|615768|22|NZ_CP032471|CRISPRCasFinder
AAGGGATTTCTTTTTTAAAACT

CRISPR arrays and Neighbor proteins around NZ_CP032471_4

CRISPR arrays

The CRISPR arrays of NZ_CP032471_4

>merge|NZ_CP032471|4|615744-615813|CRISPRCasFinder
CTTTTTTTAAAGGGATTTCTTTTTAAGGGATTTCTTTTTTAAAACTCTTTTTTTTAAAGGCATTTCTTTT

>NZ_CP032471|4|4|615744-615813|CRISPRCasFinder
CTTTTTTTAAAGGGATTTCTTTTT	AAGGGATTTCTTTTTTAAAACT
CTTTTTTTTAAAGGCATTTCTTTT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP032471.1|WP_108346554.1|611191_611428_+|HypC/HybG/HupF-family-hydrogenase-formation-chaperone	unknown	unknown	gnl|CDD|223375
NZ_CP032471.1|WP_139518331.1|610224_610347_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518341.1|627449_629294_+|DUF342-domain-containing-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_000921457.1|618594_619575_+|iron-ABC-transporter-permease	unknown	unknown	gnl|CDD|376439
NZ_CP032471.1|WP_139518327.1|605344_606886_-|flagellar-hook-length-control-protein-FliK	unknown	unknown	gnl|CDD|376734
NZ_CP032471.1|WP_139535479.1|613584_615666_+|Hop-family-adhesin-BabB	unknown	unknown	gnl|CDD|375731
NZ_CP032471.1|WP_139518339.1|624498_625896_-|cysteine--tRNA-ligase	unknown	unknown	gnl|CDD|234705
NZ_CP032471.1|WP_139518326.1|604358_605294_-|flagellar-hook-assembly-protein-FlgD	unknown	unknown	gnl|CDD|235621
NZ_CP032471.1|WP_139518328.1|607024_608035_+|phosphate-acetyltransferase	unknown	unknown	gnl|CDD|223926
NZ_CP032471.1|WP_139518337.1|619574_620342_+|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|224045
NZ_CP032471.1|WP_077232038.1|610463_611192_+|hydrogenase-nickel-incorporation-protein-HypB	unknown	unknown	gnl|CDD|272891
NZ_CP032471.1|WP_139518332.1|611446_612559_+|hydrogenase-formation-protein-HypD	unknown	unknown	gnl|CDD|272892
NZ_CP032471.1|WP_139518329.1|608627_609509_+|acetate/propionate-family-kinase	unknown	unknown	gnl|CDD|234680
NZ_CP032471.1|WP_139518336.1|617747_618602_+|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl|CDD|187632
NZ_CP032471.1|WP_000525388.1|630548_630935_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518335.1|616231_616624_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_001135603.1|617083_617608_-|acyl-CoA-thioesterase	unknown	unknown	gnl|CDD|224523
NZ_CP032471.1|WP_127976588.1|629319_629871_+|Holliday-junction-branch-migration-protein-RuvA	unknown	unknown	gnl|CDD|129193
NZ_CP032471.1|WP_139518330.1|609914_610214_+|cupin-domain-containing-protein	unknown	unknown	gnl|CDD|380358
NZ_CP032471.1|WP_139518340.1|625896_627357_-|murein-biosynthesis-integral-membrane-protein-MurJ	unknown	unknown	gnl|CDD|367301

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP032471.1|WP_108346554.1|611191_611428_+|HypC/HybG/HupF-family-hydrogenase-formation-chaperone	gnl|CDD|223375	COG0298, HypC, Hydrogenase maturation factor [Posttranslational modification, protein turnover, chaperones].	8.96684e-31
NZ_CP032471.1|WP_127976588.1|629319_629871_+|Holliday-junction-branch-migration-protein-RuvA	gnl|CDD|129193	TIGR00084, Holliday_junction_ATP-dependent_DNA_helicase_RuvA, Holliday junction DNA helicase, RuvA subunit. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair].	8.27969e-68
NZ_CP032471.1|WP_000921457.1|618594_619575_+|iron-ABC-transporter-permease	gnl|CDD|376439	pfam01032, FecCD, FecCD transport family. This is a sub-family of bacterial binding protein-dependent transport systems family. This Pfam entry contains the inner components of this multicomponent transport system.	1.97223e-66
NZ_CP032471.1|WP_139518327.1|605344_606886_-|flagellar-hook-length-control-protein-FliK	gnl|CDD|376734	pfam02120, Flg_hook, Flagellar hook-length control protein FliK. This is the C terminal domain of FliK. FliK controls the length of the flagellar hook by directly measuring the hook length as a molecular ruler. This family also includes YscP of the Yersinia type III secretion system, and equivalent proteins in other pathogenic bacterial type III secretion systems.	5.41409e-12
NZ_CP032471.1|WP_139535479.1|613584_615666_+|Hop-family-adhesin-BabB	gnl|CDD|375731	pfam18304, SabA_adhesion, SabA N-terminal extracellular adhesion domain. This is the N-terminal extracellular adhesion domain of Sialic acid binding adhesin (SabA) present in Helicobacter pylori. The N-terminal domain of SabA functions as a sugar-binding adhesion domain with conserved disulfide bonds. Notably, these amino acid residues are not only conserved among SabA orthologs but also between SabA and BabA.	5.01788e-95
NZ_CP032471.1|WP_139518339.1|624498_625896_-|cysteine--tRNA-ligase	gnl|CDD|234705	PRK00260, cysS, cysteinyl-tRNA synthetase; Validated.	0
NZ_CP032471.1|WP_139518326.1|604358_605294_-|flagellar-hook-assembly-protein-FlgD	gnl|CDD|235621	PRK05842, flgD, flagellar hook assembly protein FlgD.	1.2902e-173
NZ_CP032471.1|WP_139518328.1|607024_608035_+|phosphate-acetyltransferase	gnl|CDD|223926	COG0857, Pta, BioD-like N-terminal domain of phosphotransacetylase [General function prediction only].	6.45617e-51
NZ_CP032471.1|WP_139518337.1|619574_620342_+|ATP-binding-cassette-domain-containing-protein	gnl|CDD|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	8.00022e-99
NZ_CP032471.1|WP_139518330.1|609914_610214_+|cupin-domain-containing-protein	gnl|CDD|380358	cd02230, cupin_HP0902-like, Helicobacter pylori HP0902 and related proteins, cupin domain. This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.	8.98508e-20
NZ_CP032471.1|WP_139518332.1|611446_612559_+|hydrogenase-formation-protein-HypD	gnl|CDD|272892	TIGR00075, Hydrogenase_isoenzymes_formation_protein_HypD, hydrogenase expression/formation protein HypD. HypD is involved in the hyp operon which is needed for the activity of the three hydrogenase isoenzymes in Escherichia coli. HypD is one of the genes needed for formation of these enzymes. This protein has been found in gram-negative and gram-positive bacteria and Archaea. [Protein fate, Protein modification and repair].	0
NZ_CP032471.1|WP_139518329.1|608627_609509_+|acetate/propionate-family-kinase	gnl|CDD|234680	PRK00180, PRK00180, acetate kinase A/propionate kinase 2; Reviewed.	3.47662e-174
NZ_CP032471.1|WP_139518336.1|617747_618602_+|SDR-family-NAD(P)-dependent-oxidoreductase	gnl|CDD|187632	cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 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 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). 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) 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.	1.00338e-90
NZ_CP032471.1|WP_001135603.1|617083_617608_-|acyl-CoA-thioesterase	gnl|CDD|224523	COG1607, COG1607, Acyl-CoA hydrolase [Lipid metabolism].	3.3739e-64
NZ_CP032471.1|WP_077232038.1|610463_611192_+|hydrogenase-nickel-incorporation-protein-HypB	gnl|CDD|272891	TIGR00073, nickel_incorporation_protein_HypB, hydrogenase accessory protein HypB. A GTP hydrolase for assembly of nickel metallocenter of hydrogenase. A similar protein, ureG, is an accessory protein for urease, which also uses nickel. hits scoring 75 and above are safe as orthologs. [SS 1/05/04 I changed the role_ID and process GO from protein folding to to protein modification, since a protein folding role has not been established, but HypB is implicated in insertion of nickel into the large subunit of NiFe hydrogenases.] [Protein fate, Protein modification and repair].	1.66669e-107
NZ_CP032471.1|WP_139518340.1|625896_627357_-|murein-biosynthesis-integral-membrane-protein-MurJ	gnl|CDD|367301	pfam03023, MVIN, MviN-like protein. Deletion of the mviN virulence gene in Salmonella enterica serovar. Typhimurium greatly reduces virulence in a mouse model of typhoid-like disease. Open reading frames encoding homologs of MviN have since been identified in a variety of bacteria, including pathogens and non-pathogens and plant-symbionts. In the nitrogen-fixing symbiont Rhizobium tropici, mviN is required for motility. The MviM protein is predicted to be membrane-associated.	4.91898e-115

Protein sequences

>NZ_CP032471.1|WP_139535479.1|613584_615666_+|Hop-family-adhesin-BabB
MLHAEDDGFYTSVGYQIGEAAQMVKNTKGIQELSDNYEKLNNLLNNYSTLNTLIKLSADPSAINDARDNLGSSGRNLLDVKTNSPAYQAVLLALNAAVGLWQVTSYAFTACGPGSNESANGGIQTFNNVPGQNTTTITCNSYYEPGHGGPISTANYAKINRAYQIIQKALTANGSNGDGVPVLSNTTTKLDFTINGDKRTGGKPNEPLIYSWSHGKAIHTQWIHTTSTSTTENINTENNAQELLKQASIIITTLNEACPNFQNGGGGYWQGISGNGTMCGMFKNEISAIQGMIANAQEAVAQSKIVSENAQNQNNLDTGKPFNPYTDASFAQSMLKNAQAQAEMLNQAEQVVKNFEKIPKNFVSDSLGVCYEVQGGERRGTNPGQVTSNTWGAGCAYVGQTITNLENSIAHFGTQEQQIQQAENIADTLVHFKSRYSELGNTYNNITTALSKVPNAQSLQNVVSKKNNPYSPQGIETNYYLNQNSYNQIQTINQELGRNPFRKVGIVSSQTNNGAMNGIGIQVGYKQFFGQKRKWGARYYGFFDYNHAFIKSSFFNSASDVWTYGFGADALYNFINDKATNFLGKNNKLSVGLFGGIALAGTSWLNSEYVNLATVNNVYNAKMNVANFQFLFNMGVRMNLARSKKKGSDHAAQHGIELGLKIPTINTNYYSFMGAELKYRRLYSVYLNYVFAY
>NZ_CP032471.1|WP_139518332.1|611446_612559_+|hydrogenase-formation-protein-HypD
MSVDHLISPFRDKQTLLALSNAIKKLAFKLEKKLVIMEVCGGHTHSIMKYGLLDLMPNNLEFVHGPGCPVCVMPRARLDEAYELATIKDSIILSLGDMMKVPGSYGSLIQAREKGLDARFLYSPMQALEIAKENPTKKVIYIAIGFETTTPMSASVLLNAKKEKINNLFFHINHLLVPPSVSAILKDPACQINALLAPSHVSVISGAQIYSPLVDRFKIPIIVSGFEPVDILESVLMLLKQALNKEAKLEIQYKRAVSFEGNVKAQELVNACMEVRENFEWRGLGNIKHSALKLKETFASYDAEKVFKEHLTHKIIKENKACKCGEILKGIAKPLDCSLFATTCTPQNPIGSCMVSSEGACAAYYRYKRV
>NZ_CP032471.1|WP_108346554.1|611191_611428_+|HypC/HybG/HupF-family-hydrogenase-formation-chaperone
MCLAIPSKVIAINDNVALLETLGVQREASLDLMGESVKVGDYVLLHIGYVMSKIDEKEALESIELYEEMIAKMNETHE
>NZ_CP032471.1|WP_077232038.1|610463_611192_+|hydrogenase-nickel-incorporation-protein-HypB
MSEQRKESLQNNPNLSKKDVKIVEKILSKNDIKAAEMKERYLKEGLYVLNFMSSPGSGKTTMLENLADFKDFKFCVVEGDLQTNRDADRLHKKGVSAHQITTGEACHLEASMIEGAFDLLKDEGALEKSDFLIIENVGNLVCPSSYNLGAAMNIVLLSVPEGDDKVLKYPTMFMCADAVIISKADMIEVFNFRVSQVKEDMQKLKPEAPIFLMSSKDPKSLEDFKNFLLEKKRENYQSTHSF
>NZ_CP032471.1|WP_139518331.1|610224_610347_+|hypothetical-protein
MMKVVFMNTWYLLLTIILLIIIWRIIKLVLKDKNDSNERD
>NZ_CP032471.1|WP_139518330.1|609914_610214_+|cupin-domain-containing-protein
MKMVHFLEGVCFEKLHIETLNENSSNKEIRICMPKGAIMDKHKAPGAISVQVLEGKIIFEVENEKIEMPKGALISLEAQVLHRLDALENSVIRLSLSKK
>NZ_CP032471.1|WP_139518329.1|608627_609509_+|acetate/propionate-family-kinase
MEILVLNLGSSSIKFKLFDMKENKPLASGLAEKIGEEIGQLKIKSHLHHNDQELKEKLVIKDHASGLLMIRENLTKMGIIKDFNQIDAIRHRVVQGGDKFHAPVLVDEKVMQEIGNLSILAPLYNPANLAGIEFVQKARPHIPQIAVFDTAFHATMPSYAYMYALPYELYEKYQIRRYGFHGTSHHYVAKEAAKFLNIAYEEFNAISLHLGNGSSAAAIQKGKSVDTSMGLTPLEGLIMGTRCGDIDPTVVEYTAQCANKSLEEVMKILNHESGLKGICGDNEKHRSQKRKRR
>NZ_CP032471.1|WP_139518328.1|607024_608035_+|phosphate-acetyltransferase
MLQLNKNDNFMEIGMQSLWIYPEDTEVLGVACKSLLKALKPRYQKIALFSPISGGCEGFWECEGLNPLEIHSAIDKQKALELVSTAQEELLFETILKRYDELQSVHDFVVCLGYAPKFFLNALLDLNTILAKHLNAPMVAVAQTSLEYLKAMHSHILKKETPFAVGLFLGEMPEKPNFLSASLCKQQCELEADLIESVLQTKSEITTPLAFQMGLEKKAKKQIKKVVLPESEDERILKAAHRLNAMGAVGLILLGDKEVINSQAKNLNLNLDNAEIIDPNTSHYREEFAKSLYELRKSKGLSEQEAKQLALDKTYFATMLVHSGYAHAMVSGVNHS
>NZ_CP032471.1|WP_139518327.1|605344_606886_-|flagellar-hook-length-control-protein-FliK
MPSPINPIHTNANALSGGAKNEVKDAKNAPKSASKDFSKILNQKISKDKTAPKENPNALKATPKDAKENAKALEKTPTLPHQHAQNPAKDQQAPTLKDWLNHQKTTASHEAQHETHEANETNPKTPNETLNKNEKKPNGVTSNAHQTNLTNKNPLTPTNNAIKNPTTPTHNAKEPKTLKDIQTLSQKHDLNASNIQTTTTPENKTPLNTSDQLALKTTQTPINHTLAKNDAKNTANLSSVLQSLGKKESHNKDHATPPNNEKKTPPLKEALQMNAIKRDKTLSKKKSEKTQTKAQTTAPSATPENAPKIPLKTPPLMPLIGANPPNDNIPTLLEKEETTKEASDNKEKIKETNNSAQSAQNTQASDKTSENKSVTPKETIKHFAQQLKQEIQEYKPPMSRISMDLFPKELGKVEVVIQKVGKNLKVSVISHNNSLQTFLDNQQDLKNSLNALGFDGVDLSFSQDSSKEQHKEPFKEPFKEQELTPLKENALKSYQENTDNENQETSMQITLYA
>NZ_CP032471.1|WP_139518326.1|604358_605294_-|flagellar-hook-assembly-protein-FlgD
MAIDLAEVTGAKAAQERKKEQPTIANGLDKNAFMKLFLEQLKNQDPTAPMETDKIITQTAQLTQVEMQEENKKTMQEVASAMKSNKETNESLKDFQGALKDTMENLNKGMDDSLKANNALREVSALNSVSMIGKIAETDVSGANFDGNNKLSFSLFFDEKIDASKGVPAIQILNENNELVKTIPLKDYNGQKGYINFEWDGTNEKGEKVPKGNYKIKAEYNLDSQSKQYLQTRIGRGEVESVIFDKGKPMLRMGEMILPIDSAIEFYKPDQKPIDQKLSDQRPIDQKPLEQKLSDQRPIEQKPQTSPKETA
>NZ_CP032471.1|WP_139518335.1|616231_616624_+|hypothetical-protein
MPNTTAKKDYTQYSEKQLFNLIHQLERKIKKMQNDRVSFKEKMAKELEKRDQNFKDKIDALNGLLQKISQAFDDKRDCCLGCKIPNIQTQQAMRDAVNGVNLTQIDSLDDLTNELKRENNKGFENVCFSV
>NZ_CP032471.1|WP_001135603.1|617083_617608_-|acyl-CoA-thioesterase
MPQIQSSHSNHFDFTIDTADRTKLLMSYLVVPTTANFNNVMHGGELLNLLDKVAYVCSTRYCAKGTVTLSVDGVTFKYPIPVGNLLTFLASINYVGNTSCEVGIKVLSEDIKTREITHTNSCYFTMVAVENGKPTPMPKYEPKTEVEIRRYEGALKRKEMRTRGYLKSGKHEGV
>NZ_CP032471.1|WP_139518336.1|617747_618602_+|SDR-family-NAD(P)-dependent-oxidoreductase
MGVGEKKESQKVAIITGASSGIGLECTLMLLDQGYKVYALSRHATLCVALNHVLCECVDIDVSDSNALKEVFLNISAKEDHCDVLINSAGYGVFGSVEDTPIEEVKKQFGVNFFALCEVVQLCLPLLKNKPYSKIFNLSSIAGRVSMLFLGHYSASKHALEAYSDALRLELKPFNIQVCLIEPGPVKSNWEKTAFSVENFESENGLYALEMDAAKTFYASVYENALSAKEVAQKIVFLSMSQKIKARYLIGLKTQLLLALYQILPSSWYDSLFRLIVLKRKRDA
>NZ_CP032471.1|WP_000921457.1|618594_619575_+|iron-ABC-transporter-permease
MLKTYHIALACVILAVVVLLFGGESLSLEEWQEVCLNVKNHFLHDEELSSLSVIILEIRLPRVILALLVGASLSGSGVVMQTIFRNPLVDPFLLGISSGAMLGVAMAIAVVESNIAILAFFGAILASLAVLAMNRVLGNSVLSLVLSGVVLSAFLSALAGAIKFFVIPQKAQAIVVWLLGSLSLSSYKDCLIAFIGLSLGFIPLFLLRWRINLLSLSDAQSLSLGINPVLLRSLCLVCVSVASALAVSVSGTIGWIGLVIPHVARLFFGANLQKLLLSSLLMGAFFLLLADVVAKTITPYDLPVGIATSVLGAPFFLWLLFRTRGV
>NZ_CP032471.1|WP_139518337.1|619574_620342_+|ATP-binding-cassette-domain-containing-protein
MVLEVKNLSFKYSQKLILDKLSFSVPKNSITSILAPNGSGKTTLLKCLLGLLKPLEETEIKACNKDILPLKPYEKAKLIAYIPQVEYYAFNFSVLDFVLMGKATHLNLFAMPKAKHIKEATSVLERLDLESLKDQGINDLSGGQRQMVLLARSLLQRTPLLLLDEPTSALDLKNQALFFDAIKDEMKKRELSVLVNIHDPNLVARHSTHVVMLKDKKLFLQASTPIAMTSHNLSTLYDTPLEAIWYDNKLVVYAL
>NZ_CP032471.1|WP_139518339.1|624498_625896_-|cysteine--tRNA-ligase
MFIYDTKLKQKVPFEPLVEKKANIYVCGPTVYDDAHLGHARSAIAFDLLRRTLELSGYEVMLVRNFTDIDDKIINKAFKENKSIQELSSIYIESYTRDLNALNVKKPSLEPKASEYLDAMVGMIETLLEKNIAYQVSNGDIYLDTSKDKDYGSLSVHNSSIEFGRIGLVQEKRLEQDFVLWKSYKGDNDVGFDSPLGKGRPGWHIECSSMVFETLALTNTPYQIDIHAGGADLLFPHHENEACQTRCAFGVELAKYWMHNGFVNINNEKMSKSLGNSFFIKDALKNYDGEILRNYLLGVHYRSVLNFNEEDLLVSKKRLDKIYRLKQRVLGTLGGINPNFKKEILECMQDDLNISKALSVLESMLSSTNEKLDQNPKNKALKGEILANLKFIEELLGIGFKDPSAYFQLGVSESEKQEIENKIEERKRAKEQKDFLKADSIREELLNHKIALMDTPQGTIWEKLF
>NZ_CP032471.1|WP_139518340.1|625896_627357_-|murein-biosynthesis-integral-membrane-protein-MurJ
MLKKIFLTNSLGILCSRIFGFLRDLMMANILGAGVYSDIFFVAFKLPNLFRRIFAEGSFSQSFLPSFIRSSIKGSFAGLVGLIFCGVLFMWCLLVALNPLWLTKLLAYGFDEETIKLCAPIVAINFWYLLLVFITTFLGALLQYKHSFFASAYSASLLNLCMISALLISKEKTHLEALYYLSYGVLLGGVAQILLHFYPLVKLGLLNLLFKGFLSFKTKNAAKKKYRSKRAKKDLKAFFKQFLPSVLGNSSAQIASFLDTTIASFLASGSVSYLYYANRVFQLPLALFAIAISSALFPSIAIALKNNQQDLILERLQKAWFFLVGVLLLCSIGGIMLSKEITELLFERGQFSPKDTLITSQVFSLYLLGLLPFGLTKLFSLWLYAKLEQKKAAKISLISLFLGLAASLSLMPLLGVLGLALANSLSGLFLFVLTIKAFGFQAFLGIIKNLKLWLVILFLACVEILLLLAFKSWVTHLYLFYYFQGF
>NZ_CP032471.1|WP_139518341.1|627449_629294_+|DUF342-domain-containing-protein
MSLERFAPIKVERCKDIQKELKKVAAENKLQTEDLWFEILKTSIFIKNSAKDDFSEAFGGELQQLEEDEYYEKKELTLYQTHDIKIKSNAYKRFFEVKVDEDLSKIEIILDECFIVLDTEEHYQEMFAYIKECLAFQGVVFRHLSQMYENLKTELRKYQKEAQNKRFILYASLTFIPNVEEQSHFLLEEEYLPTHTIFLSDQEESLVKENNYIAKENQKVACVNYPKQGRDGRNLKGLYIELPKVANSPTPIGHDKNAFEEREENNALVYYSKALQGVKMEKGRLVSKQNFIFKNGIKSIETPNLLGGVESDLVLEIQAKDELSDAIDSNLILEASAINIRGNVGKNVILVAKEITIEGQIHPESYVYANKARITNHKGVCYAKEFECKYLERAKVYANSVKVEASAGSVVYAKEIALEKLKSDNKLYFSKQCWIDEVDGNGNRFIFYAFGGRENQEELKIAKQKLNALGVKSKKIIAQHQSLNHLVKNHQAIMEKLKNATEEIKRSLMQQESVKDAYSEFMFALKRLKILKAQMLELQKINNECYAKLISIENSFQHASITTKNPFKQENIVIYHRNYPKVSNLSTMLSHNESVNVIYEDHKIKKVPKSAIKG
>NZ_CP032471.1|WP_127976588.1|629319_629871_+|Holliday-junction-branch-migration-protein-RuvA
MIVGLIGVVEKISALEAHIEVQGVVYGVQVSMRTAALLQAGQKARLKILQVIKEDAHLLYGFLEESEKILFERLLKINGVGGRIALAILSSFSPNEFENIIATKEVKRLQQVPGIGKKLADKIMVDLIGFFIQDENRPVRNEVFLALESLGFKSTEINQVLKTLKPNLSIEAAIKEALQQLRS
>NZ_CP032471.1|WP_000525388.1|630548_630935_+|hypothetical-protein
MGMIKRASLVLMVVFGLVLFVGCNDNNTKKILEALGVKPPMDVEMTEYIELDPLMGLPIYFYKISIISNVDNIVMVSAKINRGNCRRIKIGEKLVFGNSYEFSFLVNSCRHVKEVSVKTDKGTWDFTF

Crispr_ID: NZ_CP032471_5

• CRISPR_ID: NZ_CP032471_5
• CRISPR_location: 1180143-1180286
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP032471_5

Consensus_repeat	Method
AATTCTTCTAGTTTTTTTGAAATAATCTCTTCAGTAACGCTAGAGAGCCTTTCT	CRISPRCasFinder

spacers of NZ_CP032471_5

>5.1|1180197|36|NZ_CP032471|CRISPRCasFinder
CCATCATGCTTACCCTCTTTGGTTTCTTTGCTCTGT

CRISPR arrays and Neighbor proteins around NZ_CP032471_5

CRISPR arrays

The CRISPR arrays of NZ_CP032471_5

>merge|NZ_CP032471|5|1180143-1180286|CRISPRCasFinder
AATTCTTCTAGTTTTTTTGAAATAATCTCTTCAGTAACGCTAGAGAGCCTTTCTCCATCATGCTTACCCTCTTTGGTTTCTTTGCTCTGTAATTCTTCTTGTTTTTTTGAAATAATCTCTTCAGTAACGCTAGAGAGCCTTTCT

>NZ_CP032471|5|5|1180143-1180286|CRISPRCasFinder
AATTCTTCTAGTTTTTTTGAAATAATCTCTTCAGTAACGCTAGAGAGCCTTTCT	CCATCATGCTTACCCTCTTTGGTTTCTTTGCTCTGT
AATTCTTCTTGTTTTTTTGAAATAATCTCTTCAGTAACGCTAGAGAGCCTTTCT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP032471.1|WP_139518684.1|1176040_1176937_+|RluA-family-pseudouridine-synthase	unknown	unknown	gnl|CDD|223638
NZ_CP032471.1|WP_000699933.1|1180664_1180970_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_000051414.1|1182869_1183103_-|cell-division-topological-specificity-factor-MinE	unknown	unknown	gnl|CDD|188120
NZ_CP032471.1|WP_139518692.1|1182062_1182863_-|DNA-protecting-protein-DprA	unknown	unknown	gnl|CDD|273238
NZ_CP032471.1|WP_139518687.1|1178123_1178909_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518682.1|1174490_1176041_+|single-stranded-DNA-specific-exonuclease-RecJ	unknown	unknown	gnl|CDD|273193
NZ_CP032471.1|WP_139518685.1|1177936_1178140_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_139518699.1|1186829_1187372_-|UDP-4-amino-4,-6-dideoxy-N-acetyl-beta-L-altrosamine-N-acetyltransferase	unknown	unknown	gnl|CDD|274661
NZ_CP032471.1|WP_139523725.1|1183929_1184922_-|ketol-acid-reductoisomerase	unknown	unknown	gnl|CDD|235491
NZ_CP032471.1|WP_139518680.1|1171942_1172611_-|PAP2-family-protein	unknown	unknown	gnl|CDD|239486
NZ_CP032471.1|WP_139518696.1|1185179_1185962_+|NAD+-synthase	unknown	unknown	gnl|CDD|184435
NZ_CP032471.1|WP_139518679.1|1170195_1171899_-|flagellar-basal-body-M-ring-protein-FliF	unknown	unknown	gnl|CDD|129310
NZ_CP032471.1|WP_139518681.1|1172865_1174482_+|CTP-synthase-(glutamine-hydrolyzing)	unknown	unknown	gnl|CDD|235437
NZ_CP032471.1|WP_139518697.1|1185958_1186897_+|tetraacyldisaccharide-4'-kinase	unknown	unknown	gnl|CDD|224577
NZ_CP032471.1|WP_139518693.1|1183099_1183906_-|septum-site-determining-protein-MinD	unknown	unknown	gnl|CDD|225447
NZ_CP032471.1|WP_139518688.1|1179596_1179857_-|lysozyme	unknown	unknown	unknown
NZ_CP032471.1|WP_000599172.1|1181661_1182066_-|Holliday-junction-resolvase-RuvX	unknown	unknown	gnl|CDD|234639
NZ_CP032471.1|WP_139519039.1|1176930_1177713_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP032471.1|WP_000201853.1|1169146_1170178_-|flagellar-motor-switch-protein-FliG	unknown	unknown	gnl|CDD|272961
NZ_CP032471.1|WP_139518691.1|1181095_1181554_-|sel1-repeat-family-protein	unknown	unknown	gnl|CDD|276807

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP032471.1|WP_139518684.1|1176040_1176937_+|RluA-family-pseudouridine-synthase	gnl|CDD|223638	COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].	2.06229e-65
NZ_CP032471.1|WP_139518692.1|1182062_1182863_-|DNA-protecting-protein-DprA	gnl|CDD|273238	TIGR00732, Protein_smf, DNA protecting protein DprA. Disruption of this gene in both Haemophilus influenzae and Helicobacter pylori drastically reduces the efficiency of transformation with exogenous DNA, but with different levels of effect on chromosomal (linear) and plasmid (circular) DNA. This difference suggests the DprA is not active in recombination, and it has been shown not to affect DNA binding, leaving the intermediate step in natural transformation, DNA processing. In Strep. pneumoniae, inactivation of dprA had no effect on the uptake of DNA. All of these data indicated that DprA is required at a later stage in transformation. Subsequently DprA and RecA were both shown in S. pneumoniae to be required to protect incoming ssDNA from immediate degradation. Role of DprA in non-transformable species is not known. The gene symbol smf was assigned in E. coli, but without assignment of function. [Cellular processes, DNA transformation].	1.44603e-94
NZ_CP032471.1|WP_139518693.1|1183099_1183906_-|septum-site-determining-protein-MinD	gnl|CDD|225447	COG2894, MinD, Septum formation inhibitor-activating ATPase [Cell division and chromosome partitioning].	1.18802e-148
NZ_CP032471.1|WP_000051414.1|1182869_1183103_-|cell-division-topological-specificity-factor-MinE	gnl|CDD|188120	TIGR01215, Cell_division_topological_specificity_factor, cell division topological specificity factor MinE. This protein is involved in the process of cell division. This protein prevents the proteins MinC and MinD to inhibit cell division at internal sites, but allows inhibiton at polar sites. This allows for correct cell division at the proper sites. [Cellular processes, Cell division].	1.07135e-25
NZ_CP032471.1|WP_139518699.1|1186829_1187372_-|UDP-4-amino-4,-6-dideoxy-N-acetyl-beta-L-altrosamine-N-acetyltransferase	gnl|CDD|274661	TIGR03585, PseH, UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase. Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.	1.53011e-59
NZ_CP032471.1|WP_139523725.1|1183929_1184922_-|ketol-acid-reductoisomerase	gnl|CDD|235491	PRK05479, PRK05479, ketol-acid reductoisomerase; Provisional.	3.92661e-179
NZ_CP032471.1|WP_139518680.1|1171942_1172611_-|PAP2-family-protein	gnl|CDD|239486	cd03392, PAP2_like_2, PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.	1.29848e-14
NZ_CP032471.1|WP_139518696.1|1185179_1185962_+|NAD+-synthase	gnl|CDD|184435	PRK13980, PRK13980, NAD synthetase; Provisional.	3.15845e-125
NZ_CP032471.1|WP_139518679.1|1170195_1171899_-|flagellar-basal-body-M-ring-protein-FliF	gnl|CDD|129310	TIGR00206, Flagellar_M-ring_protein, flagellar basal-body M-ring protein/flagellar hook-basal body protein (fliF). Component of the M (cytoplasmic associated) ring, one of four rings (L,P,S,M) which make up the flagellar hook-basal body which is a major portion of the flagellar organelle. Although the basic structure of the flagella appears to be similar for all bacteria, additional rings and structures surrounding the basal body have been observed for some bacteria (eg Vibrio cholerae and Treponema pallidum). [Cellular processes, Chemotaxis and motility].	0
NZ_CP032471.1|WP_139518681.1|1172865_1174482_+|CTP-synthase-(glutamine-hydrolyzing)	gnl|CDD|235437	PRK05380, pyrG, CTP synthetase; Validated.	0
NZ_CP032471.1|WP_139518697.1|1185958_1186897_+|tetraacyldisaccharide-4'-kinase	gnl|CDD|224577	COG1663, LpxK, Tetraacyldisaccharide-1-P 4'-kinase [Cell envelope biogenesis, outer membrane].	5.89481e-89
NZ_CP032471.1|WP_139518682.1|1174490_1176041_+|single-stranded-DNA-specific-exonuclease-RecJ	gnl|CDD|273193	TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP032471.1|WP_000599172.1|1181661_1182066_-|Holliday-junction-resolvase-RuvX	gnl|CDD|234639	PRK00109, PRK00109, Holliday junction resolvase RuvX.	3.93084e-36
NZ_CP032471.1|WP_000201853.1|1169146_1170178_-|flagellar-motor-switch-protein-FliG	gnl|CDD|272961	TIGR00207, Flagellar_motor_switch_protein_FliG, flagellar motor switch protein FliG. The fliG protein along with fliM and fliN interact to form the switch complex of the bacterial flagellar motor located at the base of the basal body. This complex interacts with chemotaxis proteins (eg CHEY). In addition the complex interacts with other components of the motor that determine the direction of flagellar rotation. The model contains putative members of the fliG family at scores of less than 100 from Agrobacterium radiobacter and Sinorhizobium meliloti as well as fliG-like genes from treponema pallidum and Borrelia burgdorferi. That is why the suggested cutoff is set at 20 but was set at 100 to construct the family. [Cellular processes, Chemotaxis and motility].	6.16419e-166
NZ_CP032471.1|WP_139518691.1|1181095_1181554_-|sel1-repeat-family-protein	gnl|CDD|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	1.50947e-34

Protein sequences

>NZ_CP032471.1|WP_139518688.1|1179596_1179857_-|lysozyme
MLKLGGCEKHCKKKYTTEKVIKEVGLELKSKSVMPYFFNEYDLTKNANRKEPERLRSQIISILMKTPKGREILKEYLNEGCILLGE
>NZ_CP032471.1|WP_139518687.1|1178123_1178909_-|hypothetical-protein
MSYFFKIILGTSVIVGVLLGLWRWTYDKFCFSLVFVLLILGIVAYSYISLKMHQRKCFAKCFVNSESFLSKMLHSPIMVICFYFIFSIFTSISIAYSVLDYNWMMWGLVFCTIVVCAAVFGTLEKMLKSIIKEDYLMLMSREVSAFVGTLLFIGLSCYVIYHGNMPDYLRPALMDTIQEAGNSIYSSCDCMDYFLKAKKMLEGVTWWGMHKAESMGLNKGFMVAGWVAFIIYNALSGIAISRLSAQIIFWLSKYFRSDCGK
>NZ_CP032471.1|WP_139518685.1|1177936_1178140_-|hypothetical-protein
MIVENDVKEDLEQARPKLEPEKQKLEQEKPTQEKECLESKEQEKQRKQKKSNRMFWGDNYCFTCRLF
>NZ_CP032471.1|WP_139519039.1|1176930_1177713_-|hypothetical-protein
MDKFLDWHYSIKGDYSELALFAAKKTGLSAEDAVANVLQEKLLGKDYKQRLDAITKRLSKTYASLLNQHEKFVSETALKGVDTDLSQNAKILDTLGDEVARKLKANFTGAIGATAGVSGLATVAKLTPKLVAKIGAKLGAKVGGKFLAKIGTALSGSWTCGPFAPACAITLWFGSDAAINFIDERLHRDKFKKEILNNINEVKENLKNSYKQQFNDSFVKISQELQESYKNAPVVEKKTIKEHIDDLNQTPEENNQKINQ
>NZ_CP032471.1|WP_139518684.1|1176040_1176937_+|RluA-family-pseudouridine-synthase
MPFVEEEFEILKPTKALFFVCDVLKCSLKEAQRHLDKQRLKHNQQAVRKSQMIQGVVSLIHFKPNEKTQALVFETKDFGVFDKPAQVYTHPKGYFYHESLLDCIQSHLGKNAHPAHRLDYETSGLVLAGKTLQSVKDLKALFMQKKVKKTYLALAHGLVEKSMKIDKPILTPQNIQKDLRIRSKISPLGKPSITLVDPLSYNPFLDISLLKITPLTGRTHQIRLHLSSVGHRIMGEGLYGVADEEAREYLQLKRENNAPLLMLHAASLEFEFKGAIYKIASPMPERFMPFLKDLPLFY
>NZ_CP032471.1|WP_139518682.1|1174490_1176041_+|single-stranded-DNA-specific-exonuclease-RecJ
MKQKLKAQIKERLTSIAYNEKGFPSPFLFKDLKKAALKIIEAMRANTEILVVGDYDADGVISSAIMAKFFESLNYKHVRIIIPNRFIDGYGISKKFLEKHHAPLIITVDNGINAFEAARFCKEKNYTLIITDHHCLNNDEVPDAYAVINPKQPDCDFIQKEVCGALVAFYLCYGIHQLLGKEKSRSSELLCLAGVATIADMMPLTFFNRFLVSKALYFLQKESLGAMGFLRQREVFRKRSLKASDISFNIAPLINSAGRMQDAKMALDFLSTNNFQDGYSLYERLKACNTKRKMIQQQVFEEAFKHAMVGEKIIIAFKDNWHEGVLGIVASKLVEATQKPSLVFTFKEGVYKGSGRSSPNIDLIDALNGVSSLLLGYGGHRQACGLSVGKNNIISLFETLENFDFKVLPFCEKEPPLTLKLKDIDRELLEIIEMGEPYGQENPEPLFQAQNLEVIEEKIIKESHQILRFKDKECVKEAIYFNAERFLKAGEKVSAIFSVELDEYSNEPKMFVKSLL
>NZ_CP032471.1|WP_139518681.1|1172865_1174482_+|CTP-synthase-(glutamine-hydrolyzing)
MDRAKFIFVTGGVLSSLGKGISSSSIATLLQHCNYQVSILKIDPYINIDPGTMSPLEHGEVFVTSDGAETDLDIGHYERFLNRNLTRLNNFTTGQIFSSVIENERKGEYLGKTIQIVPHVTDEIKRRIKSAAKGLDFLIVEVGGTVGDMEGMFYLEAIRQLKLELGNEKVINVHVTLIPYIQTTNELKTKPTQHSVQELRRLGVTPQIILARSPKPLDKELKNKIALSCDVEQDSVIVATDTKSIYACPILFLQEGILTPIARRFNLNKLHPKMAAWNTLVEKIIAPKHKVKIGFVGKYLSLKESYKSLIEALIHAGAHLDAQVNIEWLDSENFNEKTDLEGVDAILVPGGFGERGIEGKICAIQRARVEKLPFLGICLGMQLAIVEFCRNVLGLKGANSTEFNQRCEYPVVYLIGDFMDQNHQKQVRTYNSPLGGTMRLGEYECEIMPNSLLEKAYKKPSVKERHRHRYEINPKYRQEWENKGLKVVGFGANHLIEAIELEDHPFFVGVQFHPEFTSRLQSPNPIILDFIKSALSKS
>NZ_CP032471.1|WP_139518680.1|1171942_1172611_-|PAP2-family-protein
MAENSFKNVSTQPKAFFLLPAKTLFLLGGVFSAFFILIAGLVLFGCTNSMDNAIFNFVRSTPFNSSPILTLILQNTARLGSSQFVLPLSLLVGVFLSLYRRNLALGVWFVLSVILFEALLESLKHLFAYPVQWLSHSTNFPNATALSLTLFYGLLILLIPHLITHQTLKNVLFYSLFGLIFLIGLVLILLGVSFSSVLGGFCLGALGACFSIGIYLSVFQKI
>NZ_CP032471.1|WP_139518679.1|1170195_1171899_-|flagellar-basal-body-M-ring-protein-FliF
MDLKVLLQRIVDFFIKLNKKQKIALIAAGVLITALLVFLLLYPFKEKDYTQGGYGVLFEGLDSSDNALILQHLQQNQIPYKVSRDDTILIPKDKVYEERITLASQGIPKTSKVGFEIFDTKDFGATDFDQNIKLIRAIEGELSRTIESLNPILKANVHIAIPKDSVFVAKEVPPSASVMLKIKPDMKLSPTQILGIKNLIAAAVPKLTIENVKIVNENGESIGEGDILENSKELALEQLHYKQNFENILENKIVNILAPIVGGKNKVVARVNAEFDFSQKKSTKETFDPNNVVRSEQNLEEKKEGAPKKQVGGVPGVVSNIGPVQGLKDNKEPEKYEKSQNTTNYEVGKTISEIKGEFGTLVRLNAAVVVDGKYKIALKDGANALEYEPLSDESLQKINALVKQAIGYNQNRGDDVAVSNFEFNPMAPMIDNATLSEKIMHKTQKILGSFTPLIKYVLVFIVLFIFYKKVIVPFSERMLEVVPDEDKEVKSMFEEMDEEEDELNKLGDLRKKVEDQLGLNASFSEEEVRYEIILEKIRGTLKERPDEIATLFKLLIKDEISSDSAKG
>NZ_CP032471.1|WP_000201853.1|1169146_1170178_-|flagellar-motor-switch-protein-FliG
MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE
>NZ_CP032471.1|WP_000699933.1|1180664_1180970_-|hypothetical-protein
MKIMHQVRDFLDSCKQTIQKNSSEVFQKTKRAFFKEESQKIREQAVKIVEKRLKKEGMKLSDFNEEELKIMFEAEEKRLLEQIQTKHFKEVWEKGDNEQGK
>NZ_CP032471.1|WP_139518691.1|1181095_1181554_-|sel1-repeat-family-protein
MAEPNPEELFDLGVKSIEAKDYIQAKKYFKKACDLKYGGGCGALGDLYDDVEKNLIKAAQLYTKACELKEGLGCKRLGSLYYYGRGVEKNLTKATQYLSKACDLKEGMGCGNLGVLYYNGDGVKRDSKKADQYFSKACKLGNQEACEALKEK
>NZ_CP032471.1|WP_000599172.1|1181661_1182066_-|Holliday-junction-resolvase-RuvX
MILACDVGLKRIGIAALLNGVILPLEAILRHNRNQASRDLSDLLREKNIQVLVVGKPNESYADTNARIEHFIKLVDFKGEIVFINEDRSSIEAYENLEHLGKKNKRLAIKDGRLDSLSACRILERYCQKVLKNH
>NZ_CP032471.1|WP_139518692.1|1182062_1182863_-|DNA-protecting-protein-DprA
MKSHFQYSALENIPKVFDTLKDPPKKLYCVGDIKLLEAPLKVAIIGTRRPTPYSKQHTITLARELAKNGAVIVSGGALGVDIIAQENALPKTIMLSPCSLDLIYPTNNHKVIQEIAQNGLILSEYEKDFMPIKGSFLARNRLVIALSDAVIIPQADLKSGSMSSARLAQKYQKPLFVLPQRLNESDGTNELLEKGQAQGIFNIQNFINTLLKDYHLKEMPEMKDEFLEYFAKNPSYEEAYLKFGDKLLEYELLGKIKRINHIVVLA
>NZ_CP032471.1|WP_000051414.1|1182869_1183103_-|cell-division-topological-specificity-factor-MinE
MSLFDFFKNKGSAATATDRLKLILAKERTLNLPYMEEMRKEIIAVIQKYTKSSDIHFKTLDSNQSVETIEVEIILPK
>NZ_CP032471.1|WP_139518693.1|1183099_1183906_-|septum-site-determining-protein-MinD
MAIVVTITSGKGGVGKSTTTANLAIGLAESGKKVVAVDFDIGLRNLDMILGLENRIVYDVVDVMEKNCNLSQALIMDKKTKNLSFLAASQSKDKNILDKEKVAILINALRADFDYILIDSPAGIESGFEHAILHADMALVVVTPEVSSLRDSDRVVGIIDAKSNRAKKGMEVHKHLIINRLKPELVANGEMIPIEEVLKILCLPLIGIIPEDHHIISATNKGEPVIRTDCESAKAYQRITRRILGEEVEYVEFKAKRGFFSALKGIFS
>NZ_CP032471.1|WP_139523725.1|1183929_1184922_-|ketol-acid-reductoisomerase
MALPVYYDKDIDLGVIQSLQVGIIGYGAQGEAQALNLRDSKVRVRIGLYQGSLSVSKAKAEGFEMLEVKELVQQSDVIMALLPDELHKEVLEKEVIPFLKEGQIVGFAHGFSVHFNQVVLPKGVGAILVAPKGPGSALREEYLKNRGLYHLIAIEQESSKNNAKAVALSYAKAMGGGRMGVLETSFKEECESDLFGEQAVLCGGLEAIVRMGFETLIKAGYPEELAYFECVHEVKLVADLLHYKGVEGLRKHISNTAEFGAIKNREPMGNLLEKRMQKILKKIQNGSFAKDFLLEKSLNYPRLNTERKALKETKIEQIGEILRAPFNHKK
>NZ_CP032471.1|WP_139518696.1|1185179_1185962_+|NAD+-synthase
MQKDYQKLIVYLCDFLEKEAQKRGFKKVVYGLSGGLDSAVVGVLCQKVFKENAHALLMPSSVSMPESKTDALILCETFSIPYTEYSIAPYDAIFGSHFKDASLTRKGNFCARLRMAFLYDYSLKSDSLVIGTSNKSERMLGYGTLFGDLACAINPIGELFKTEVYELACHLNIPKKILNKPPSADLFVGQSDEKDLGYSYSVIDPLLKDIEALFQTKPIDAETLTQLGYDEILVKNITSRIQKNAFKLELPTIAKRFNPK
>NZ_CP032471.1|WP_139518697.1|1185958_1186897_+|tetraacyldisaccharide-4'-kinase
MKSDKPFLERYFYDPTLLQKGLIFALYPFSLIYQGIATLKRKTAKKHDFKIPLISIGNLIAGGSGKTPFILEIAPRYQEVAIVSRGYQRDSQGLVVVSVKGNILVPQQTAGDEAYLLALNLKQASVIVSEKRELGVLKALELGAKIVFLDDGFRFNFNQFNLLLKPKVPPYYPFCLPSGLYRESIKSYKEAHLVITEDKDYQRITSISHPTKRMLLVTAIANPSRLDAFLPKEVVKKLYFRDHAPFNLELLEKEFYQNNATSLLVTPKDLVKLQDCSLPLSVLDLKLEIDPNILERIDHYILSYPCNTKEHL
>NZ_CP032471.1|WP_139518699.1|1186829_1187372_-|UDP-4-amino-4,-6-dideoxy-N-acetyl-beta-L-altrosamine-N-acetyltransferase
MKKNYSYGNIQAIDFTHLNDGEKLLVLEFRNHPNTALWMYSAFISLKTHLQFIEDLKNSPSHRYFLFKEESVYLGVGSITKINFFHKHGYLGIYKNPFLKNGGETILKALERIAFEEFQLNSLHLEVMESNFKAIAFYEKNHYELEGRLKGFISKEKEFIDVLLYYKDKKGYNDQFSLKY

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP032471_1	1.1|270528|22|NZ_CP032471|CRISPRCasFinder	270528-270549	22	NZ_CP032471.1	270560-270581	1	0.955
NZ_CP032471_1	1.1|270528|22|NZ_CP032471|CRISPRCasFinder	270528-270549	22	NZ_CP032471.1	615800-615821	1	0.955
NZ_CP032471_4	4.1|615768|22|NZ_CP032471|CRISPRCasFinder	615768-615789	22	NZ_CP032471.1	270560-270581	1	0.955
NZ_CP032471_4	4.1|615768|22|NZ_CP032471|CRISPRCasFinder	615768-615789	22	NZ_CP032471.1	615800-615821	1	0.955
NZ_CP032471_1	1.1|270528|22|NZ_CP032471|CRISPRCasFinder	270528-270549	22	NZ_CP032471.1	270799-270820	2	0.909
NZ_CP032471_1	1.1|270528|22|NZ_CP032471|CRISPRCasFinder	270528-270549	22	NZ_CP032471.1	616067-616088	2	0.909
NZ_CP032471_1	1.1|270528|22|NZ_CP032471|CRISPRCasFinder	270528-270549	22	NZ_CP032471.1	1198623-1198644	2	0.909
NZ_CP032471_4	4.1|615768|22|NZ_CP032471|CRISPRCasFinder	615768-615789	22	NZ_CP032471.1	270799-270820	2	0.909
NZ_CP032471_4	4.1|615768|22|NZ_CP032471|CRISPRCasFinder	615768-615789	22	NZ_CP032471.1	616067-616088	2	0.909
NZ_CP032471_4	4.1|615768|22|NZ_CP032471|CRISPRCasFinder	615768-615789	22	NZ_CP032471.1	1198623-1198644	2	0.909

1. spacer 1.1|270528|22|NZ_CP032471|CRISPRCasFinder matches to position: 270560-270581, mismatch: 1, identity: 0.955

aagggatttcttttttaaaact	CRISPR spacer
aaggcatttcttttttaaaact	Protospacer
**** *****************

2. spacer 1.1|270528|22|NZ_CP032471|CRISPRCasFinder matches to position: 615800-615821, mismatch: 1, identity: 0.955

aagggatttcttttttaaaact	CRISPR spacer
aaggcatttcttttttaaaact	Protospacer
**** *****************

3. spacer 4.1|615768|22|NZ_CP032471|CRISPRCasFinder matches to position: 270560-270581, mismatch: 1, identity: 0.955

aagggatttcttttttaaaact	CRISPR spacer
aaggcatttcttttttaaaact	Protospacer
**** *****************

4. spacer 4.1|615768|22|NZ_CP032471|CRISPRCasFinder matches to position: 615800-615821, mismatch: 1, identity: 0.955

aagggatttcttttttaaaact	CRISPR spacer
aaggcatttcttttttaaaact	Protospacer
**** *****************

5. spacer 1.1|270528|22|NZ_CP032471|CRISPRCasFinder matches to position: 270799-270820, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

6. spacer 1.1|270528|22|NZ_CP032471|CRISPRCasFinder matches to position: 616067-616088, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

7. spacer 1.1|270528|22|NZ_CP032471|CRISPRCasFinder matches to position: 1198623-1198644, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

8. spacer 4.1|615768|22|NZ_CP032471|CRISPRCasFinder matches to position: 270799-270820, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

9. spacer 4.1|615768|22|NZ_CP032471|CRISPRCasFinder matches to position: 616067-616088, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

10. spacer 4.1|615768|22|NZ_CP032471|CRISPRCasFinder matches to position: 1198623-1198644, mismatch: 2, identity: 0.909

aagggatttcttttttaaaact	CRISPR spacer
aagggatttctttttttgaact	Protospacer
**************** .****

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP032471_3	3.1|582907|27|NZ_CP032471|CRISPRCasFinder	582907-582933	27	NZ_CP034186	Deinococcus sp. S14-83 strain S14-83T plasmid unnamed2, complete sequence	116558-116584	3	0.889
NZ_CP032471_3	3.1|582907|27|NZ_CP032471|CRISPRCasFinder	582907-582933	27	NZ_CP022727	Erwinia persicina strain B64 plasmid pEP2, complete sequence	67408-67434	4	0.852
NZ_CP032471_3	3.2|582961|30|NZ_CP032471|CRISPRCasFinder	582961-582990	30	NC_014719	Caldicellulosiruptor kristjanssonii I77R1B plasmid pCALKR01, complete sequence	8121-8150	6	0.8

1. spacer 3.1|582907|27|NZ_CP032471|CRISPRCasFinder matches to NZ_CP034186 (Deinococcus sp. S14-83 strain S14-83T plasmid unnamed2, complete sequence) position: , mismatch: 3, identity: 0.889

-agtgtcgttattaaagctggcgttgcc	CRISPR spacer
cagt-tcgttattaaagctggggctgcc	Protospacer
 *** **************** *.****

2. spacer 3.1|582907|27|NZ_CP032471|CRISPRCasFinder matches to NZ_CP022727 (Erwinia persicina strain B64 plasmid pEP2, complete sequence) position: , mismatch: 4, identity: 0.852

agtgtcgttattaaagctggcgttgcc	CRISPR spacer
gctgtcggtattaacgctggcgttgcc	Protospacer
. ***** ****** ************

3. spacer 3.2|582961|30|NZ_CP032471|CRISPRCasFinder matches to NC_014719 (Caldicellulosiruptor kristjanssonii I77R1B plasmid pCALKR01, complete sequence) position: , mismatch: 6, identity: 0.8

----agcactgtcattaaaagcagattgagtgct	CRISPR spacer
gattagc----tcattcaaagctgattgagtgct	Protospacer
    ***    ***** ***** ***********