UniProt: W6S1V1

Database: UniProt
Entry: W6S1V1_9CLOT

LinkDB:  W6S1V1_9CLOT 
Original site:  W6S1V1_9CLOT

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (3)   
All databases (15)   

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ID   W6S1V1_9CLOT            Unreviewed;       560 AA.
AC   W6S1V1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=CM240_2757 {ECO:0000313|EMBL:CDM69874.1};
OS   Clostridium bornimense.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM69874.1, ECO:0000313|Proteomes:UP000019426};
RN   [1] {ECO:0000313|EMBL:CDM69874.1, ECO:0000313|Proteomes:UP000019426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Complete genome sequence of Clostridum sp. M2/40.";
RL   Submitted (NOV-2013) 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|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; HG917869; CDM69874.1; -; Genomic_DNA.
DR   RefSeq; WP_051483861.1; NZ_HG917869.1.
DR   AlphaFoldDB; W6S1V1; -.
DR   STRING; 1216932.CM240_2757; -.
DR   KEGG; clt:CM240_2757; -.
DR   PATRIC; fig|1216932.3.peg.2720; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_2_9; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000019426; Chromosome 2.
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; 3.10.170.10; -; 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; 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:SF3; NEUTRAL PROTEASE B; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
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   Reference proteome {ECO:0000313|Proteomes:UP000019426};
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}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           28..560
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039754492"
FT   DOMAIN          112..161
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          250..398
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          401..554
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   560 AA;  61973 MW;  91BB765976B56C05 CRC64;
     MGKRTKRLLS LITVCLSIMV TFNGSTAKAM SGGNFLTTNI SSIFEKGVKE YSNTRDLGTI
     NNGEAPEVYL DEEDSCKFID GSYTNIKVEN EDDAIESINS IKKLMKINYP EDEFEVSKVN
     STGDLVSYKL QQIYNDIPLY GREIVVVTDG EGNTTSVGGN YLEGVSVDTN AEISKENIAS
     YITKIYGSDA KVNNEELVIY SLNDVEPTLC WKVTVEGAKN GELYTVNSFI NAKTGELVNE
     VSLITKGAEQ GTGVDLKGET KTFNVNKKDI LMSTLYELFD TERNIKIYKA NLGYIPGIPI
     TSRNNTWNDP VAVSAIHNFG HVYDYYYNKF NRVSFDNKGA SIVASIHYKD IYNWRGLDNA
     FWSSTNSQFI FGDGYQLCTP LIGALDVVGH EYTHAVVEYT AGLEYQGESG ALNESYADIL
     GNIIEGKDDE QWLVGEDIMK NGDIAIRSMA NPEELHQPSV IGGEYYVDPN DTTYDNGGVH
     INSGILNHAA YLMWENGISD KDKLAKLFYN SLFIMNSTAN FQDCRIAVTS AANNLGMSSE
     ELDIINNAFD EVGISVKTLE
//

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