ID A0A073KM96_9BACI Unreviewed; 353 AA.
AC A0A073KM96;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=BAGA_09130 {ECO:0000313|EMBL:KEK23438.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK23438.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK23438.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK23438.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) 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|ARBA:ARBA00004613,
CC 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:KEK23438.1}.
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DR EMBL; JOTM01000016; KEK23438.1; -; Genomic_DNA.
DR RefSeq; WP_033675631.1; NZ_LTAQ01000070.1.
DR AlphaFoldDB; A0A073KM96; -.
DR STRING; 574375.AZF08_17435; -.
DR MEROPS; M04.025; -.
DR eggNOG; COG3227; Bacteria.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000027778; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT DOMAIN 59..181
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 185..350
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 353 AA; 39297 MW; 0571F5954945B06F CRC64;
METKRCSHRN CQCFIVPNYV LESLAQNEVE AARISLSKSR QVRKRRMLKE YDITGVVALT
DAGTGPRDES ARHVYDCKGG TKLRVNEVRK EGDRSNGDTV IDHAYDYVGV VRDYFKNVFH
RNSIDDKGLD LILNVHYGHN FQNAYWDGDE MVFGDGDGVI FTSFANSLDV IGHELTHGIT
QFTNGLEYEG QSGALNEHIS DVFGIAIKQA YLKQTAQDAD WLIGADIMGP TLKGQALRSM
KAPGTAFDNK LMGKDMQPDH MKNYYQGERD HHGVHINSGI PNKVFYLVSM EIGTDKAALI
WYNATHSLFA TTNFTQFAQI VIKAAQKLVD SGEVPKTATK TVESAFKTVG LSS
//
