ID   U4JZ72_9VIBR            Unreviewed;       829 AA.
AC   U4JZ72;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative Zinc-dependent metalloprotease {ECO:0000313|EMBL:CCO58245.1};
GN   ORFNames=VIBNI_A2166 {ECO:0000313|EMBL:CCO58245.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO58245.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO58245.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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DR   EMBL; FO203526; CCO58245.1; -; Genomic_DNA.
DR   RefSeq; WP_022551050.1; NC_022528.1.
DR   AlphaFoldDB; U4JZ72; -.
DR   STRING; 28173.VIBNI_A2166; -.
DR   KEGG; vni:VIBNI_A2166; -.
DR   PATRIC; fig|1260221.3.peg.2057; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG3637; Bacteria.
DR   OrthoDB; 5242130at2; -.
DR   Proteomes; UP000016895; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd12215; ChiC_BD; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   SMART; SM00736; CADG; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:CCO58245.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Protease {ECO:0000313|EMBL:CCO58245.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..829
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004650288"
FT   DOMAIN          237..437
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
SQ   SEQUENCE   829 AA;  90460 MW;  4F38364345266797 CRC64;
     MKKNMNRWIN VCFALSATAL GVSQAIAAND VHLPVLEKEY INQPSSAQFW LETVEHSSAS
     EVDRQRYIKP AKFRLIQLEL DQLKHHLNQT VAASTDLVNE RAASVDLSIP LPNGGYETFV
     VAPNQVLPAE LAARYPEIKT FSGTSAETKN TRIVLDYTSQ GFHAMVTSEK YGTFYIDPYE
     SGNTRTYISY FKKDYHKTKD LRLIEETLTH SDSQLNNTPS FRSGRSGFGT SDMYPLRTYR
     LAIATTYEYS RFHGGTKQSV MSAVATTINR VNEIYERDLA IRLQLIPTTD QLFSLDVNDY
     YTNNRSDLMQ GESQIVIDKV IGQQGYDVGH LFSTTGGGSA LIGSVCTRGK GSGVSGLGMP
     MGDAFDIDIV AHEIGHQFGA EHTHNTGCNR VSYNAVEPGS GSTIMGYAGV CGPNVQVNSD
     AMFHSYSIGN VRHFMDRGYG SGCGTSEMSL NTPPVVRAGP DVTIPKETPF VLTGSAADTE
     DQASLTYSWE QIDRGDLVAR PTANQVTGPT FRAKLPTVSP TRYLPNLDAI INNQTPTWEV
     LSSVARSYKF RLVARDNNAE SPQVSWDERV ITVDGTAGPF VVSEPNTKVN WLPGSTQTVR
     WQVAGTHLPP VSVSLVNILL SLDGGKTYPH TLATNAPNTG KAEVVLPNSI SNTARIKVEA
     VDNIFFDISN VDFSISEGLG LNQAPEFTSV APVNATSGTA YHYQVSAKDV DSPEIRFRAK
     TKPAWLSFDA STLVLSGTPT DADIGSHQVV LQVSDSQIVT SQTFQITVTG GATQTCGTVE
     PWSASQVYVT GDQVSYGNKT FEARWWTKGQ QPDASKVDGD WKLIDPCQP
//