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Database: UniProt
Entry: B4ENF7_BURCJ
LinkDB: B4ENF7_BURCJ
Original site: B4ENF7_BURCJ 
ID   B4ENF7_BURCJ            Unreviewed;       565 AA.
AC   B4ENF7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=zmpA {ECO:0000313|EMBL:CAR57339.1};
GN   ORFNames=BCAS0409 {ECO:0000313|EMBL:CAR57339.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR57339.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR57339.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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; AM747722; CAR57339.1; -; Genomic_DNA.
DR   RefSeq; WP_006481898.1; NC_011002.1.
DR   AlphaFoldDB; B4ENF7; -.
DR   SMR; B4ENF7; -.
DR   MEROPS; M04.022; -.
DR   KEGG; bcj:BCAS0409; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_1_4; -.
DR   BioCyc; BCEN216591:G1G1V-7406-MONOMER; -.
DR   Proteomes; UP000001035; Chromosome 3.
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..22
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           23..565
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023036220"
FT   DOMAIN          70..116
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          222..384
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          387..564
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        465
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   565 AA;  59904 MW;  95A43F82A6EC351B CRC64;
     MKKLSRLLPI TAITLASLSA FAQAGDQPAA VDKALQLIQQ NPSAFSLAAG GTARTLKFAG
     PQAGAPTDGD QFQVRDVIVD PDGTEHVRFD RFHAGLPVIG GDVVVHSSKG QLKQASVTQL
     APINLAGSIG KVGNRAVIRN APDVGATRAR HIAAARFNSD VRRVDDAELV VFARDVTPTL
     AYAVRVYGKA TETHGDAVLY YVDARTGTLL DAQDLIKTAA ATGTGRSLYY GNLTLTTDQT
     GTNAYRMLDP SRGGGSVYDG RGLSSDEVEQ ATDLPIFTSS TNVWGNNATT DRQTVAADID
     YGLALTWDYY KTTHNRNGIF NDGRGVKSYA HVVFNTGSGT TGANAAWLSS RVMAYGDGEP
     GTRLPKPVVS VDVAGHEMSH GVTEATANLN YSGDAGGLNE STSDIFGTLV KFYANNPNDP
     GNYVIGARVV SGGLRKMYKQ DLDGRSFSCY PSGGFSWSNP RHDPHFTSGV GNRFFYLLSE
     GPSVPPTDTG LSRTQLVCNG DTTFSGLGRD KAGKIWYRTL TVYLNANSSY PNARRASIQA
     ANDLYGANSA ESATVARAWS AVGVN
//
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