ID A0A3S8WFG7_9ACTN Unreviewed; 691 AA.
AC A0A3S8WFG7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=DMA15_26160 {ECO:0000313|EMBL:AZM55636.1};
OS Streptomyces sp. WAC 01529.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2203205 {ECO:0000313|EMBL:AZM55636.1, ECO:0000313|Proteomes:UP000269043};
RN [1] {ECO:0000313|EMBL:AZM55636.1, ECO:0000313|Proteomes:UP000269043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01529 {ECO:0000313|EMBL:AZM55636.1,
RC ECO:0000313|Proteomes:UP000269043};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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; CP029617; AZM55636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8WFG7; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000269043; Chromosome.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51829; P_HOMO_B; 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}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 45..691
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023150606"
FT DOMAIN 565..691
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 691 AA; 72397 MW; 210C6B7C4C40993B CRC64;
MLRNTSHRPS SHSRSARTRA TAVGALSAVA ALLAVAVQAG PASAEDPWKT AAKAPAQKLG
KVDPGALAVK LSPAQRAELI RDANATKAET AKDLGLGAKE KLVVRDVTKD RDGTVHTRYE
RTYDGLPVLG GDMVVDTAKS GKTEGVTKAT KARLKGIDMS AGIKASAAEK QALSAAKAEG
SKKTDADRAP RKVVWLAKGK PVLAYETVVG GLQHDGTPNE LHVVTDAATG KKLFQWQGIE
NGTGNTQYSG QVPLGTAQSG SNYTLTDTAR GNHKTYNLNR GTSGTGTLFS GADDVWGNGL
PSNLETAGAD AHYGAALTWD YYKNVHGRSG IRGDGVGAYS RVHYGNNYVN AFWSDGCFCM
TYGDGANNAK PLTSIDVAAH EMTHGVTAAT GNMTYSGESG GLNEATSDIF AAAVEFNANN
PQDVGDYNVG EKIDIRGDGT PLRYMDKPSK DGSSKDSWYS GIGNIDVHYS SGVANHFYYL
LSEGSGKKEI NGVQYDSPTS DGLPVTGIGR DKASLIWFKA LTTKFTTTTN YAAARTGTLA
VAGELYGTTS AEYKAVAHAW AAVNVGARPG GEEPGGTSFE NTTDVSIPDN GAAVTSSVNV
TGRTGNAPSA LKVGVDIVHT WRGDLQVDLV APDGTVYPLK PTSSSDSADN VKETYTVNAS
SEVANGTWKL KVQDKAAQDT GYINSWKVTF P
//
