GenomeNet

Database: UniProt
Entry: A0A0N1GGM0_9ACTN
LinkDB: A0A0N1GGM0_9ACTN
Original site: A0A0N1GGM0_9ACTN 
ID   A0A0N1GGM0_9ACTN        Unreviewed;       548 AA.
AC   A0A0N1GGM0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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};
DE   Flags: Precursor;
GN   ORFNames=OV320_1054 {ECO:0000313|EMBL:KPI23006.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI23006.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI23006.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI23006.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-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:KPI23006.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJCX01000034; KPI23006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1GGM0; -.
DR   PATRIC; fig|1592329.3.peg.8871; -.
DR   Proteomes; UP000037870; 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; 3.10.450.40; -; 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; 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:UP000037870};
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..36
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           37..548
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023117328"
FT   DOMAIN          70..114
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          211..369
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          372..547
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   548 AA;  57774 MW;  5DB4054AE4620EC2 CRC64;
     MSRIRQHVRG SRLATAGIAA TTATLLAAVL SPVADAADRP TRATALDNAA AVLADYAATL
     GLTSVQGTSV RDVVVDKDGT QHVRYDRTYR QLPVLGGDFV VHLAPDGAYR SANRATRATI
     SLTSITPKVS APKAADVAVN ALRAANLGET LKQVKAKPQL VVDALHGAPK LAWRTDVVAL
     DTLGNPVARA VLTDARTGAQ IDAWDTIETA TGDGKSLYGG TVPLETTLSG STYQLKDPTR
     GNTYTGDAAN KTDLCIFGIC ISRAPATLFT DTDNHWGTGA TADRSTAAVD AQYGTDVTWD
     YYKNVHGRNG IGNDGKGSYN RVHYGNSYNN AFWDDSCFCM TYGDGDGTQL GPLVALDVAG
     HEMSHGVTSK TAKLTYSGES GGLNEATSDI FGSLVEFYAG NSSDTGDYLI GEKIVRSGFG
     RDALRYMDKP SKDGNSADYW SSSVGNLDVH YSSGVANHFA YLLAEGSGTK TVNGVTYNSP
     TYNGSTLTGI GRDKLGAIWY RALTVYMTSS TNYAAARTAT LNAARDLYGT GTTEYNAVAA
     AWTAVNVN
//
DBGET integrated database retrieval system