BLA2_BAC17
ID BLA2_BAC17 Reviewed; 257 AA.
AC P10425;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:P25910};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
DE AltName: Full=Beta-lactamase II {ECO:0000303|PubMed:3938474};
DE AltName: Full=Cephalosporinase {ECO:0000250|UniProtKB:P04190};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:3938474};
DE AltName: Full=Metallothioprotein beta-lactamase II {ECO:0000250|UniProtKB:P04190};
DE AltName: Full=Penicillinase {ECO:0000303|PubMed:3938474};
DE AltName: Full=Zinc-requiring beta-lactamase II {ECO:0000250|UniProtKB:P04190};
DE Flags: Precursor;
OS Bacillus sp. (strain 170).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=74566;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-48.
RX PubMed=3938474; DOI=10.1099/00221287-131-12-3317;
RA Kato C., Kudo T., Watanabe K., Horikoshi K.;
RT "Nucleotide sequence of the beta-lactamase gene of alkalophilic Bacillus
RT sp. strain 170.";
RL J. Gen. Microbiol. 131:3317-3324(1985).
CC -!- FUNCTION: Confers resistance to the different beta-lactams antibiotics
CC (penicillin, cephalosporin and carbapenem) via the hydrolysis of the
CC beta-lactam ring. {ECO:0000250|UniProtKB:P04190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:P25910};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P04190};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P04190};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P04190}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Class-B
CC beta-lactamase family. {ECO:0000305}.
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DR EMBL; M15350; AAA22275.1; -; Genomic_DNA.
DR AlphaFoldDB; P10425; -.
DR SMR; P10425; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0017001; P:antibiotic catabolic process; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001018; Beta-lactamase_class-B_CS.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
DR PROSITE; PS00744; BETA_LACTAMASE_B_2; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Direct protein sequencing; Hydrolase; Metal-binding;
KW Periplasm; Signal; Zinc.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:3938474"
FT CHAIN 31..257
FT /note="Metallo-beta-lactamase type 2"
FT /id="PRO_0000016944"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P25910"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
SQ SEQUENCE 257 AA; 28153 MW; 23EEEBDC045AE571 CRC64;
MKKNTLLKVG LCVSLLGTTQ FVSTISSVQA SQKVEQIVIK NETGTISISQ LNKNVWVHTE
LGYFNGEAVP SNGLVLNTSK GLVLVDSSWD NKLTKELIEM VEKKFQKRVT DVIITHAHAD
RIGGITALKE RGIKAHSTAL TAELAKKSGY EEPLGDLQTV TNLKFGNTKV ETFYPGKGHT
EDNIVVWLPQ YQILAGGCLV KSAEAKNLGN VADAYVNEWS TSIENMLKRY RNINLVVPGH
GKVGDKGLLL HTLDLLK
