ID I3QI50_9VIBR Unreviewed; 607 AA.
AC I3QI50;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=vcpA {ECO:0000313|EMBL:AFK08680.1};
GN ORFNames=F0224_10560 {ECO:0000313|EMBL:NOI76120.1};
OS Vibrio coralliilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=190893 {ECO:0000313|EMBL:AFK08680.1};
RN [1] {ECO:0000313|EMBL:AFK08680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BH3 {ECO:0000313|EMBL:AFK08682.1}, BH5
RC {ECO:0000313|EMBL:AFK08680.1}, P2 {ECO:0000313|EMBL:AFK08689.1}, and
RC P5 {ECO:0000313|EMBL:AFK08687.1};
RA Wilson B., Muirhead A., Bazanella M., Huete-Stauffer C., Vezzulli L.,
RA Bourne D.G.;
RT "An Improved Detection and Quantification Method for the Coral Pathogen
RT Vibrio coralliilyticus.";
RL PLoS ONE 8:E81800-E81800(2013).
RN [2] {ECO:0000313|EMBL:NOI76120.1, ECO:0000313|Proteomes:UP000528382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIC-5 {ECO:0000313|EMBL:NOI76120.1,
RC ECO:0000313|Proteomes:UP000528382};
RA Kehlet-Delgado H., Mueller R.S.;
RT "Draft genome sequencing and comparative genomics of hatchery-associated
RT Vibrios.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR EMBL; JQ345034; AFK08680.1; -; Genomic_DNA.
DR EMBL; JQ345036; AFK08682.1; -; Genomic_DNA.
DR EMBL; JQ345041; AFK08687.1; -; Genomic_DNA.
DR EMBL; JQ345043; AFK08689.1; -; Genomic_DNA.
DR EMBL; VTXB01000003; NOI76120.1; -; Genomic_DNA.
DR RefSeq; WP_019274242.1; NZ_VTXP01000006.1.
DR STRING; 190893.BA953_18665; -.
DR MEROPS; M04.003; -.
DR Proteomes; UP000528382; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 23..607
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5011417672"
FT DOMAIN 51..90
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 114..189
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 207..349
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 352..496
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 528..595
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 424
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 607 AA; 65525 MW; D7D5C78AEABE35C3 CRC64;
MKQRQMLWLI AAGLGVSLPV TAAEMVKVEN DALLQQALKA QSNSVVPLET GFAEVKRVVL
PNGKVKVRYQ QTHMGLPVFN TSVVATQTKS SQNEVYGVMA QGISGDLATV APTLDEKQAI
AAAKNAFKKH SLGASDAPFE NSQSKLMVWL DDSQTAKVVY MVDFFVAAKV PRRPFYLVDA
TTGEVLKHWE GINHAQATGT GPGGNQKTGQ YNFGTDYPGF IVDKSGTTCT MNNSAVKTVD
LNGGTSGSTA FSYPCNDDTN FNDHKYVNGA YSPLNDAHYF GKVVFDMYQD WMNTSPLTFQ
LTMRVHYGNN YENAFWNGSS MTFGDGQNTF YPLVDINVSA HEVSHGFTEQ NSGLVYSNMS
GGMNEAFSDI AGEAAEFYMK GSVDWVVGAD IFKSEGGLRY FDLPSKDGRS IDHASQYYDG
LNVHYSSGVY NRAFYLLANK AGWDVRKGFE IFTLANQLYW TANSTFDAGA CGVAKAAADM
GYNVSDVEDA FTTVGVNASC GTTPPPTGDV LVKGTPVTDL AGARSSETFY TFTVDSASSV
AVSISGGTGD ADLYVKAGSK PTTSSYDCRP YRYGNTEQCS LSATPGTTYH VMLRGYSSYS
GVTLRLD
//
