ID   A0A285QQN1_9ACTN        Unreviewed;       356 AA.
AC   A0A285QQN1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SAMN06272789_4515 {ECO:0000313|EMBL:SOB84270.1};
OS   Streptomyces sp. 1331.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB84270.1, ECO:0000313|Proteomes:UP000219030};
RN   [1] {ECO:0000313|Proteomes:UP000219030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA   Varghese N., Submissions S.;
RL   Submitted (JUL-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|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; OBMJ01000001; SOB84270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285QQN1; -.
DR   Proteomes; UP000219030; 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:UP000219030};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          99..181
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          184..353
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        275
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   356 AA;  37288 MW;  02903D116B4E1E80 CRC64;
     MSKVVTSGHR SLTLGRMTAA VPICAIVPPY VLDRLAEAGH EAAAHTLTLD AAHRAARLSP
     PPATGGAPGL NRVISDAGHG QRLPGRTVRT EGQAAVSDAS VNHAYDGLGA TFALYADVFG
     RHSIDDRGLR LDASVHYGRN YDNAFWNGHQ MVFGDGDGRI FGDFTACIDV IGHELTHGVT
     QFTAGLDYQD QPGALNESVS DVFGSLVKQY ALHQSAADAD WLIGAGLLAP GIQGVALRSM
     KAPGTAYDDP QLGKDPQPAH MRDYVNTSED NGGVHINSGI PNHAFYLLAT ALGGSSWERA
     GRIWYDALTG HAVPADADFA AFARATVAAA KARYPDQGAV ADTVTASWAQ VGVSPG
//