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Database: UniProt
Entry: A0A2G3JGB8_9NEIS
LinkDB: A0A2G3JGB8_9NEIS
Original site: A0A2G3JGB8_9NEIS 
ID   A0A2G3JGB8_9NEIS        Unreviewed;       603 AA.
AC   A0A2G3JGB8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=CSQ88_01145 {ECO:0000313|EMBL:PHV03569.1};
OS   Iodobacter sp. BJB302.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Iodobacter.
OX   NCBI_TaxID=1506510 {ECO:0000313|EMBL:PHV03569.1, ECO:0000313|Proteomes:UP000224670};
RN   [1] {ECO:0000313|EMBL:PHV03569.1, ECO:0000313|Proteomes:UP000224670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJB302 {ECO:0000313|EMBL:PHV03569.1,
RC   ECO:0000313|Proteomes:UP000224670};
RA   Jude B.A., Perron G.P., O'Brien K., Doing G., Bettina A.M.;
RT   "Draft genomes of phenotypically distinct violacein producing isolates
RT   cultured from the Hudson Valley Watershed.";
RL   Submitted (OCT-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHV03569.1}.
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DR   EMBL; PDZG01000002; PHV03569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G3JGB8; -.
DR   OrthoDB; 5378341at2; -.
DR   Proteomes; UP000224670; 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; 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..26
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           27..603
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023159852"
FT   DOMAIN          60..97
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          125..194
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          210..345
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          348..492
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   DOMAIN          522..587
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        420
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   603 AA;  64431 MW;  F1A6EBC0CB046867 CRC64;
     MKQALNRVAR PLLMVVLLAG AFNAMAAERV DLENYVAPAG LTTRGLADEG VHNLLGLKAD
     ELQAARSQTY PDGKVVTRYQ QFHQGVPVWG EGVVENRAAG LAQPALSGAL LRDLSNDLPS
     AKPAYSQTQI LSIAKTQAKA IKTENEQAKL YVKLGSNNVA QLIYVVSFVN GSAMKPSRPH
     FIIDANTGVV LDRWEGIAHK DATGPGGNAK TGQYEYGTKY GPLVVTDDCK MDSGNVITVD
     LKNGTTGSTP YQFTCPRNTY KSVNGAFSPL NDAHYFGNVV FNLYKDWFSL RPISQNLSMK
     VHYGNSYENA FWDGSAMHFG DGANTFYPLV SLDVSAHEVS HGFTEQNSGL VYSKQSGGMN
     EAFSDMAGEA AEFYMKGAND FLVGAEIFKA NGALRYMADP TKDGRSIGHA SQYNDSLDVH
     LSSGVYNKAF YLLASKAGWG TRKAFEVMVD ANRLHWTANS TFDQGACGVE KAAASRGYTV
     ADVTSAFEAV GVSCIVKPPV VKVLTKGVPV TGLALASNAT VTYTIVVPAG ARNLTFKTSG
     GTGDADIYAK FGAAPTTTVY DAKSDGGTNT ETITVAAPKA GTYYLLLKAY NAFSNVTLVG
     NYQ
//
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