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Database: UniProt
Entry: A0A0D0NB86_KITGR
LinkDB: A0A0D0NB86_KITGR
Original site: A0A0D0NB86_KITGR 
ID   A0A0D0NB86_KITGR        Unreviewed;       533 AA.
AC   A0A0D0NB86;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=TR51_16775 {ECO:0000313|EMBL:KIQ65515.1};
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ65515.1, ECO:0000313|Proteomes:UP000032066};
RN   [1] {ECO:0000313|EMBL:KIQ65515.1, ECO:0000313|Proteomes:UP000032066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ65515.1,
RC   ECO:0000313|Proteomes:UP000032066};
RA   Arens J.C., Haltli B., Kerr R.G.;
RT   "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT   terpentecin and satosporin producer.";
RL   Submitted (FEB-2015) 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}.
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:KIQ65515.1}.
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DR   EMBL; JXZB01000002; KIQ65515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0NB86; -.
DR   STRING; 2064.TR51_16775; -.
DR   MEROPS; M04.017; -.
DR   PATRIC; fig|2064.6.peg.3596; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000032066; 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; 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:SF1; BACILLOLYSIN; 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:UP000032066};
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..30
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           31..533
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039754875"
FT   DOMAIN          65..112
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          215..358
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          361..533
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        438
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   533 AA;  54810 MW;  A4FCDB17F54AED68 CRC64;
     MKRKLTAGAV LSAAALLAGV VQVGAAPAQA GVPSVGQQRD ALLSLAGAEA APIAGALALG
     GQERLIVKDA VVDADGDRHL RYERTFAGLP VIGGDLVVHQ RTDGSITSVD RAFAGRLSLP
     SLTPRLSADQ AATGAADAVR GTLGTADGAG AALARVGATG AAQLVVWAGG GSPRLAYRTV
     VEGVRSDGVP SSRRLITDAA TGAVLAGDDG IRTATGTGTG VQVGAVTLTT TQTGATYQLK
     DATRGNQSTV DAGNKNALFT STTNIWGNGL PSNRQSAAVD AQFDAAATWD YFKNTFGRVG
     LRGNGVGITS RVHYGSNLMD LFWDDTCFCI SYGDGPSGNK PMTELDVAGH EMAHGVTSAT
     AGLVYSGEAG GLDEATSDIF GTMIEWYAGL PADPPDYLIA EKLDLAGNGT PVRYLDRPSR
     DGYSKDFWYP GIGGLDPHYS SGVANHFFYL LSEGSGAKVV NGVNYNSPTA DGSTLVGIGR
     DKAAAIWYRA LTVYFTSTTT YANARSATLR AALDLYGAPE YNAVAAAWKA VNV
//
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