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Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase II) (Cephalosporinase) (Metallo-beta-lactamase type II) (Metallothioprotein beta-lactamase II) (Penicillinase) (Zinc-requiring beta-lactamase II)

 BLAB_BACCE              Reviewed;         256 AA.
P14488;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
EC=3.5.2.6 {ECO:0000250|UniProtKB:P25910};
AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
AltName: Full=Beta-lactamase II {ECO:0000303|PubMed:3131315};
AltName: Full=Cephalosporinase {ECO:0000250|UniProtKB:P04190};
AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:3131315};
AltName: Full=Metallothioprotein beta-lactamase II {ECO:0000303|PubMed:3131315};
AltName: Full=Penicillinase {ECO:0000250|UniProtKB:P04190};
AltName: Full=Zinc-requiring beta-lactamase II {ECO:0000303|PubMed:3131315};
Flags: Precursor;
Bacillus cereus.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1396;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
STRAIN=5/B/6;
PubMed=3131315; DOI=10.1128/jb.170.6.2873-2878.1988;
Lim H.M., Pene J.J., Shaw R.W.;
"Cloning, nucleotide sequence, and expression of the Bacillus cereus
5/B/6 beta-lactamase II structural gene.";
J. Bacteriol. 170:2873-2878(1988).
[2]
FUNCTION, MUTAGENESIS OF HIS-57; GLU-66; HIS-117; GLY-177 AND GLU-241,
AND SUBSTRATE SPECIFICITY.
PubMed=2501295;
Lim H.M., Pene J.J.;
"Mutations affecting the catalytic activity of Bacillus cereus 5/B/6
beta-lactamase II.";
J. Biol. Chem. 264:11682-11687(1989).
[3]
FUNCTION, AND MUTAGENESIS OF ASP-110 AND ASP-119.
PubMed=1904717; DOI=10.1042/bj2760401;
Lim H.M., Iyer R.K., Pene J.J.;
"Site-directed mutagenesis of dicarboxylic acids near the active site
of Bacillus cereus 5/B/6 beta-lactamase II.";
Biochem. J. 276:401-404(1991).
-!- FUNCTION: Confers resistance to the different beta-lactams
antibiotics (penicillin, cephalosporin and carbapenem) via the
hydrolysis of the beta-lactam ring. Benzylpenicillin is a better
substrate than cephalosporin C and ampicillin (PubMed:3131315,
PubMed:2501295). {ECO:0000269|PubMed:1904717,
ECO:0000269|PubMed:2501295, ECO:0000269|PubMed:3131315}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000250|UniProtKB:P25910}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P04190};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:P04190};
-!- ENZYME REGULATION: Inhibited by chelating agents such as EDTA.
{ECO:0000269|PubMed:3131315}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Thermostable. {ECO:0000269|PubMed:3131315};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P04190}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
Class-B beta-lactamase family. {ECO:0000305}.
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EMBL; M19530; AAA22562.1; -; Genomic_DNA.
PIR; A32017; A32017.
RefSeq; WP_000799232.1; NZ_NIRE01000047.1.
ProteinModelPortal; P14488; -.
SMR; P14488; -.
BindingDB; P14488; -.
ChEMBL; CHEMBL1744488; -.
PATRIC; fig|1396.421.peg.2543; -.
SABIO-RK; P14488; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0017001; P:antibiotic catabolic process; IMP:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR001018; Beta-lactamase_class-B_CS.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
PROSITE; PS00744; BETA_LACTAMASE_B_2; 1.
1: Evidence at protein level;
Antibiotic resistance; Hydrolase; Metal-binding; Periplasm; Signal;
Zinc.
SIGNAL 1 29 {ECO:0000255,
ECO:0000305|PubMed:3131315}.
CHAIN 30 256 Metallo-beta-lactamase type 2.
/FTId=PRO_0000016943.
METAL 115 115 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P04190}.
METAL 117 117 Zinc 1; via pros nitrogen.
{ECO:0000250|UniProtKB:P04190}.
METAL 119 119 Zinc 2. {ECO:0000250|UniProtKB:P04190}.
METAL 178 178 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P04190}.
METAL 197 197 Zinc 2. {ECO:0000250|UniProtKB:P04190}.
METAL 239 239 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P04190}.
BINDING 200 200 Substrate.
{ECO:0000250|UniProtKB:P04190}.
BINDING 209 209 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P04190}.
MUTAGEN 57 57 H->Y: Inactivates the enzyme.
{ECO:0000269|PubMed:2501295}.
MUTAGEN 66 66 E->Q: No change in activity.
{ECO:0000269|PubMed:2501295}.
MUTAGEN 110 110 D->N: No change in activity.
{ECO:0000269|PubMed:1904717}.
MUTAGEN 117 117 H->Y: Inactivates the enzyme.
{ECO:0000269|PubMed:2501295}.
MUTAGEN 119 119 D->N,E: Inactivates the enzyme.
{ECO:0000269|PubMed:1904717}.
MUTAGEN 177 177 G->E: Inactivates the enzyme.
{ECO:0000269|PubMed:2501295}.
MUTAGEN 241 241 E->Q: No change in activity.
{ECO:0000269|PubMed:2501295}.
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


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