BLAB_BACCE
ID BLAB_BACCE Reviewed; 256 AA.
AC P14488;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 102.
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:3131315};
DE AltName: Full=Cephalosporinase {ECO:0000250|UniProtKB:P04190};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:3131315};
DE AltName: Full=Metallothioprotein beta-lactamase II {ECO:0000303|PubMed:3131315};
DE AltName: Full=Penicillinase {ECO:0000250|UniProtKB:P04190};
DE AltName: Full=Zinc-requiring beta-lactamase II {ECO:0000303|PubMed:3131315};
DE Flags: Precursor;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=5/B/6;
RX PubMed=3131315; DOI=10.1128/jb.170.6.2873-2878.1988;
RA Lim H.M., Pene J.J., Shaw R.W.;
RT "Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6
RT beta-lactamase II structural gene.";
RL J. Bacteriol. 170:2873-2878(1988).
RN [2]
RP FUNCTION, MUTAGENESIS OF HIS-57; GLU-66; HIS-117; GLY-177 AND GLU-241, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=2501295; DOI=10.1016/s0021-9258(18)80118-1;
RA Lim H.M., Pene J.J.;
RT "Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-
RT lactamase II.";
RL J. Biol. Chem. 264:11682-11687(1989).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-110 AND ASP-119.
RX PubMed=1904717; DOI=10.1042/bj2760401;
RA Lim H.M., Iyer R.K., Pene J.J.;
RT "Site-directed mutagenesis of dicarboxylic acids near the active site of
RT Bacillus cereus 5/B/6 beta-lactamase II.";
RL Biochem. J. 276:401-404(1991).
CC -!- FUNCTION: Confers resistance to the different beta-lactams antibiotics
CC (penicillin, cephalosporin and carbapenem) via the hydrolysis of the
CC beta-lactam ring. Benzylpenicillin is a better substrate than
CC cephalosporin C and ampicillin (PubMed:3131315, PubMed:2501295).
CC {ECO:0000269|PubMed:1904717, ECO:0000269|PubMed:2501295,
CC ECO:0000269|PubMed:3131315}.
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 -!- ACTIVITY REGULATION: Inhibited by chelating agents such as EDTA.
CC {ECO:0000269|PubMed:3131315}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:3131315};
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; M19530; AAA22562.1; -; Genomic_DNA.
DR PIR; A32017; A32017.
DR RefSeq; WP_000799232.1; NZ_NTMO01000006.1.
DR PDB; 6DJA; X-ray; 2.48 A; A=35-256.
DR PDBsum; 6DJA; -.
DR AlphaFoldDB; P14488; -.
DR SMR; P14488; -.
DR STRING; 1396.DJ87_1499; -.
DR BindingDB; P14488; -.
DR ChEMBL; CHEMBL1744488; -.
DR PATRIC; fig|1396.421.peg.2543; -.
DR eggNOG; COG0491; Bacteria.
DR OMA; THWHADR; -.
DR SABIO-RK; P14488; -.
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; IMP: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 3D-structure; Antibiotic resistance; Hydrolase; Metal-binding; Periplasm;
KW Signal; Zinc.
FT SIGNAL 1..29
FT /evidence="ECO:0000255, ECO:0000305|PubMed:3131315"
FT CHAIN 30..256
FT /note="Metallo-beta-lactamase type 2"
FT /id="PRO_0000016943"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04190"
FT MUTAGEN 57
FT /note="H->Y: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:2501295"
FT MUTAGEN 66
FT /note="E->Q: No change in activity."
FT /evidence="ECO:0000269|PubMed:2501295"
FT MUTAGEN 110
FT /note="D->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:1904717"
FT MUTAGEN 117
FT /note="H->Y: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:2501295"
FT MUTAGEN 119
FT /note="D->N,E: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:1904717"
FT MUTAGEN 177
FT /note="G->E: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:2501295"
FT MUTAGEN 241
FT /note="E->Q: No change in activity."
FT /evidence="ECO:0000269|PubMed:2501295"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6DJA"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6DJA"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6DJA"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6DJA"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6DJA"
SQ SEQUENCE 256 AA; 28038 MW; 670F62378C355C2D CRC64;
MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL NKNVWVHTEL
GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV EKKFKKRVTD VIITHAHADR
IGGMKTLKER GIKAHSTALT AELAKKNGYE EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE
DNIVVWLPQY QILAGGCLVK SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG
EVGDRGLLLH TLDLLK