ID A3P727_BURP0 Unreviewed; 585 AA.
AC A3P727;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN OrderedLocusNames=BURPS1106A_A2104 {ECO:0000313|EMBL:ABN94645.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN94645.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) 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; CP000573; ABN94645.1; -; Genomic_DNA.
DR AlphaFoldDB; A3P727; -.
DR MEROPS; M04.022; -.
DR KEGG; bpl:BURPS1106A_A2104; -.
DR HOGENOM; CLU_008590_5_1_4; -.
DR Proteomes; UP000006738; Chromosome II.
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 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..44
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 45..585
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023088474"
FT DOMAIN 90..136
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 242..404
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 407..584
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 485
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 585 AA; 62221 MW; 7BDC8FE6D6F17BE7 CRC64;
MLAVNAFSII NAVIHYLGDY MKKLSCLLSV TAISLACLSA FAQADDPPAA ADRALQLIRQ
NPSAFHLAAG SAARTLKFAG AQAKAPADGD QFQVRDVIVD ADGTEHVRFD RFYAGLPVIG
GDVVVHSNQG QLKQASLTQP APIDLAGKIG KVGERFVVRN APDVGADAAR RVASKRFGAD
VRRVDGADLV VFARDAAPTL AYAVRVYGKA TDAHGEAVIY YVDARTGNVL DAQDLIKTAS
VTGTGRSLYY GNLSLTTDQT GTNAYRMLDP TRGSGSVYDG RGLSSDEVEQ ASDLPIFTSS
TNVWGNNTTS DRQTVAADID YGLALTWDYY KTTHNRNGIF NDGRGVRSYA HVVFDTGSGT
TGANAAWLSS RVMVYGDGEP GTRLPKPVVS VDVAGHEMSH GVTEATSNLY YSGDAGGLNE
STSDIFGTLV KYYANNPNDP GNYVIGARIT SGGLRKMYKQ DLDGRSYSCY PSGGFSWANP
RHDPHYTSGV GNRFFYLLAE GPVAPSTDTG LSRSQLVCNG DTGFSGLGRD KAGKIWYRTL
TVYLTTNSSY PGARRASIQA ANDLYGVNSL ESATVARAWS AAGVN
//
