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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
 
 
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