ID   A0A1G9W8S3_9ACTN        Unreviewed;       350 AA.
AC   A0A1G9W8S3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SAMN05444921_113206 {ECO:0000313|EMBL:SDM80912.1};
OS   Streptomyces wuyuanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM80912.1, ECO:0000313|Proteomes:UP000199063};
RN   [1] {ECO:0000313|Proteomes:UP000199063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNHI01000013; SDM80912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9W8S3; -.
DR   STRING; 1196353.SAMN05444921_113206; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000199063; 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; 3.10.170.10; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
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; PTHR43579; -; 1.
DR   PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 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|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          70..176
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          179..347
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        270
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   350 AA;  37160 MW;  990CEF0712B41FD7 CRC64;
     MDSFTPVFCG IVPPHLLDKL ARAGDPAVAA AARRTLVADA AHRTGRRLTT VTGAPAPADE
     VVPGPQRTLY DAGNTTGLPG TKVRSEGDEP VQDATVNRAY AGLGATFDLL MTAYGHDSID
     GAGLPLDATV HYDEEYGNAF WNGEQMVFGD GDGEIFLDFT GPVDVIAHEL AHGFTQYSAN
     FTYFGQPGAL NESVSDVFGS LVKQYTLDQS ADRADWLIGA GLLAPRVSGV ALRSMKAPGT
     AYDDDVLGKD PQPATMADYV RTGRDNGGVH INSGIPNHAF YLLATQLGGK AWERAGRIWY
     DTMTSGRLQV DASFADFAAE TVEAATARYG RGEEREAVVK AWSQVGVPAN
//