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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)

 BLA2_BACCE              Reviewed;         257 AA.
P04190;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
28-FEB-2018, entry version 124.
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:3930467};
AltName: Full=Cephalosporinase {ECO:0000303|PubMed:3930467};
AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:3930467};
AltName: Full=Metallothioprotein beta-lactamase II {ECO:0000303|PubMed:3930467};
AltName: Full=Penicillinase {ECO:0000303|PubMed:3930467};
AltName: Full=Zinc-requiring beta-lactamase II {ECO:0000303|PubMed:3930467};
Flags: Precursor;
Name=blm {ECO:0000303|PubMed:3930467};
Bacillus cereus.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1396;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, AND
SUBSTRATE SPECIFICITY.
STRAIN=569/H / NCTC 9945;
PubMed=3930467;
Hussain M., Carlino A., Madonna M.J., Lampen J.O.;
"Cloning and sequencing of the metallothioprotein beta-lactamase II
gene of Bacillus cereus 569/H in Escherichia coli.";
J. Bacteriol. 164:223-229(1985).
[2]
PROTEIN SEQUENCE OF 31-183; 187-210 AND 214-257.
STRAIN=569/H / NCTC 9945;
PubMed=3930290; DOI=10.1016/0014-5793(85)81024-3;
Ambler R.P., Daniel M., Fleming J., Hermoso J.M., Pang C., Waley S.G.;
"The amino acid sequence of the zinc-requiring beta-lactamase II from
the bacterium Bacillus cereus 569.";
FEBS Lett. 189:207-211(1985).
[3]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
PubMed=3124808; DOI=10.1042/bj2480181;
Sutton B.J., Artymiuk P.J., Cordero-Borboa A.E., Little C.,
Phillips D.C., Waley S.G.;
"An X-ray-crystallographic study of beta-lactamase II from Bacillus
cereus at 0.35-nm resolution.";
Biochem. J. 248:181-188(1987).
[4]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 37-257 OF WILD-TYPE AND
MUTANT CYS-177 IN COMPLEX WITH ZINC IONS, AND COFACTOR.
PubMed=7588620;
Carfi A., Pares S., Duee E., Galleni M., Duez C., Frere J.-M.,
Dideberg O.;
"The 3-D structure of a zinc metallo-beta-lactamase from Bacillus
cereus reveals a new type of protein fold.";
EMBO J. 14:4914-4921(1995).
[5]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 31-257 IN COMPLEX WITH
CADMIUM IONS.
Fabiane S.M., Sohi M.K., Sutton B.J.;
"Null.";
Submitted (SEP-1997) to the PDB data bank.
[6]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-257 IN COMPLEX WITH
SUBSTRATE ANALOGS AND ZINC IONS, AND COFACTOR.
PubMed=9761898; DOI=10.1107/S0907444997010627;
Carfi A., Duee E., Galleni M., Frere J.M., Dideberg O.;
"1.85 A resolution structure of the zinc (II) beta-lactamase from
Bacillus cereus.";
Acta Crystallogr. D 54:313-323(1998).
[7]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 31-257 IN COMPLEX WITH ZINC
IONS, AND COFACTOR.
PubMed=20677753; DOI=10.1021/bi100894r;
Gonzalez J.M., Buschiazzo A., Vila A.J.;
"Evidence of adaptability in metal coordination geometry and active-
site loop conformation among B1 metallo-beta-lactamases.";
Biochemistry 49:7930-7938(2010).
[8]
STRUCTURE BY NMR OF 31-257 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC
IONS, AND COFACTOR.
PubMed=24059435; DOI=10.1042/BJ20131003;
Karsisiotis A.I., Damblon C.F., Roberts G.C.;
"Solution structures of the Bacillus cereus metallo-beta-lactamase
BcII and its complex with the broad spectrum inhibitor R-thiomandelic
acid.";
Biochem. J. 456:397-407(2013).
[9]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 31-257 IN COMPLEX WITH
SUBSTRATE ANALOGS AND ZINC IONS, ENZYME REGULATION, AND COFACTOR.
PubMed=26482303; DOI=10.1128/AAC.01335-15;
Brem J., van Berkel S.S., Zollman D., Lee S.Y., Gileadi O.,
McHugh P.J., Walsh T.R., McDonough M.A., Schofield C.J.;
"Structural basis of metallo-beta-lactamase inhibition by captopril
stereoisomers.";
Antimicrob. Agents Chemother. 60:142-150(2015).
-!- FUNCTION: Confers resistance to the different beta-lactams
antibiotics (penicillin, cephalosporin and carbapenem) via the
hydrolysis of the beta-lactam ring. Active on cephalosporin and
penicillin. {ECO:0000269|PubMed:3930467}.
-!- 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:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303,
ECO:0000269|PubMed:7588620, ECO:0000269|PubMed:9761898};
Note=Binds 2 Zn(2+) ions per subunit. The enzyme can also function
with only 1 Zn(2+) ion (PubMed:9761898).
{ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:7588620,
ECO:0000269|PubMed:9761898};
-!- ENZYME REGULATION: Inhibited by captopril stereoisomers and
iodoacetate (PubMed:3930467, PubMed:26482303). Also inhibited by
chelating agents such as EDTA (PubMed:3930467).
{ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:3930467}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3124808}.
-!- 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; M11189; AAA22276.1; -; Genomic_DNA.
PIR; A91806; PNBSU2.
RefSeq; WP_000742468.1; NZ_NULI01000034.1.
PDB; 1BC2; X-ray; 1.90 A; A/B=31-257.
PDB; 1BMC; X-ray; 2.50 A; A=37-257.
PDB; 1BVT; X-ray; 1.85 A; A=31-257.
PDB; 1DXK; X-ray; 1.85 A; A=31-257.
PDB; 1MQO; X-ray; 1.35 A; A=31-257.
PDB; 2BC2; X-ray; 1.70 A; A/B=31-257.
PDB; 2BFK; X-ray; 2.00 A; A/B=31-257.
PDB; 2BFL; X-ray; 1.80 A; A/B=31-257.
PDB; 2BFZ; X-ray; 2.30 A; A/B=31-257.
PDB; 2BG2; X-ray; 2.40 A; A/B=31-257.
PDB; 2BG6; X-ray; 2.30 A; A/B=31-257.
PDB; 2BG7; X-ray; 2.10 A; A/B=31-257.
PDB; 2BG8; X-ray; 2.50 A; A/B=31-257.
PDB; 2BGA; X-ray; 2.70 A; A/B=31-257.
PDB; 2M5C; NMR; -; A=31-257.
PDB; 2M5D; NMR; -; A=31-257.
PDB; 2NXA; X-ray; 2.29 A; A=37-257.
PDB; 2NYP; X-ray; 1.84 A; A=37-257.
PDB; 2NZE; X-ray; 1.80 A; A/B=36-257.
PDB; 2NZF; X-ray; 2.28 A; A=37-257.
PDB; 2UYX; X-ray; 1.95 A; A=30-257.
PDB; 3BC2; X-ray; 1.70 A; A=31-257.
PDB; 3FCZ; X-ray; 2.80 A; A/B=36-247.
PDB; 3I0V; X-ray; 1.60 A; A=31-257.
PDB; 3I11; X-ray; 1.45 A; A=31-257.
PDB; 3I13; X-ray; 1.74 A; A=31-257.
PDB; 3I14; X-ray; 1.55 A; A=31-257.
PDB; 3I15; X-ray; 1.55 A; A=31-257.
PDB; 3KNR; X-ray; 1.71 A; A/B/C/D=31-257.
PDB; 3KNS; X-ray; 1.58 A; A/B/C/D=31-257.
PDB; 4C09; X-ray; 1.20 A; A=31-257.
PDB; 4C1C; X-ray; 1.18 A; A=31-257.
PDB; 4C1H; X-ray; 1.10 A; A=31-257.
PDB; 4NQ4; X-ray; 1.67 A; A=36-257.
PDB; 4NQ5; X-ray; 2.29 A; A=36-257.
PDB; 4NQ6; X-ray; 1.80 A; A=36-257.
PDB; 4TYT; X-ray; 1.80 A; A=31-257.
PDB; 5FQA; X-ray; 1.10 A; A=31-257.
PDB; 5FQB; X-ray; 1.90 A; A=31-257.
PDB; 5JMX; X-ray; 1.44 A; A=31-257.
PDB; 5W8W; X-ray; 2.25 A; A=36-257.
PDBsum; 1BC2; -.
PDBsum; 1BMC; -.
PDBsum; 1BVT; -.
PDBsum; 1DXK; -.
PDBsum; 1MQO; -.
PDBsum; 2BC2; -.
PDBsum; 2BFK; -.
PDBsum; 2BFL; -.
PDBsum; 2BFZ; -.
PDBsum; 2BG2; -.
PDBsum; 2BG6; -.
PDBsum; 2BG7; -.
PDBsum; 2BG8; -.
PDBsum; 2BGA; -.
PDBsum; 2M5C; -.
PDBsum; 2M5D; -.
PDBsum; 2NXA; -.
PDBsum; 2NYP; -.
PDBsum; 2NZE; -.
PDBsum; 2NZF; -.
PDBsum; 2UYX; -.
PDBsum; 3BC2; -.
PDBsum; 3FCZ; -.
PDBsum; 3I0V; -.
PDBsum; 3I11; -.
PDBsum; 3I13; -.
PDBsum; 3I14; -.
PDBsum; 3I15; -.
PDBsum; 3KNR; -.
PDBsum; 3KNS; -.
PDBsum; 4C09; -.
PDBsum; 4C1C; -.
PDBsum; 4C1H; -.
PDBsum; 4NQ4; -.
PDBsum; 4NQ5; -.
PDBsum; 4NQ6; -.
PDBsum; 4TYT; -.
PDBsum; 5FQA; -.
PDBsum; 5FQB; -.
PDBsum; 5JMX; -.
PDBsum; 5W8W; -.
ProteinModelPortal; P04190; -.
SMR; P04190; -.
DrugBank; DB02153; 3-Sulfinoalanine.
DrugBank; DB02863; Alpha Chlorophyll A.
DrugBank; DB04272; Citric Acid.
BRENDA; 3.5.2.6; 648.
SABIO-RK; P04190; -.
EvolutionaryTrace; P04190; -.
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; IDA:UniProtKB.
GO; GO:0017001; P:antibiotic catabolic process; IDA: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; RibonucZ/Hydroxyglut_hydro.
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;
3D-structure; Antibiotic resistance; Direct protein sequencing;
Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
SIGNAL 1 30 {ECO:0000269|PubMed:3930290}.
CHAIN 31 257 Metallo-beta-lactamase type 2.
/FTId=PRO_0000016942.
METAL 116 116 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303,
ECO:0000269|PubMed:7588620,
ECO:0000269|PubMed:9761898}.
METAL 118 118 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303,
ECO:0000269|PubMed:7588620,
ECO:0000269|PubMed:9761898}.
METAL 120 120 Zinc 2. {ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303}.
METAL 179 179 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303,
ECO:0000269|PubMed:7588620,
ECO:0000269|PubMed:9761898}.
METAL 198 198 Zinc 2. {ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303}.
METAL 240 240 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:20677753,
ECO:0000269|PubMed:24059435,
ECO:0000269|PubMed:26482303}.
BINDING 201 201 Substrate. {ECO:0000269|PubMed:26482303}.
BINDING 210 210 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:26482303,
ECO:0000269|PubMed:9761898}.
STRAND 38 40 {ECO:0000244|PDB:4C1H}.
STRAND 42 52 {ECO:0000244|PDB:4C1H}.
STRAND 55 64 {ECO:0000244|PDB:4C1H}.
STRAND 67 78 {ECO:0000244|PDB:4C1H}.
STRAND 81 85 {ECO:0000244|PDB:4C1H}.
HELIX 91 105 {ECO:0000244|PDB:4C1H}.
STRAND 109 113 {ECO:0000244|PDB:4C1H}.
STRAND 116 118 {ECO:0000244|PDB:4C1H}.
HELIX 119 122 {ECO:0000244|PDB:4C1H}.
HELIX 125 131 {ECO:0000244|PDB:4C1H}.
STRAND 134 136 {ECO:0000244|PDB:4C1H}.
HELIX 139 147 {ECO:0000244|PDB:4C1H}.
STRAND 159 165 {ECO:0000244|PDB:4C1H}.
STRAND 168 173 {ECO:0000244|PDB:4C1H}.
STRAND 177 182 {ECO:0000244|PDB:4C1H}.
STRAND 185 187 {ECO:0000244|PDB:4C1H}.
TURN 189 191 {ECO:0000244|PDB:4C1H}.
STRAND 194 197 {ECO:0000244|PDB:4C1H}.
STRAND 212 214 {ECO:0000244|PDB:2M5C}.
TURN 216 218 {ECO:0000244|PDB:4C1H}.
HELIX 219 229 {ECO:0000244|PDB:4C1H}.
STRAND 236 241 {ECO:0000244|PDB:4C1H}.
HELIX 247 255 {ECO:0000244|PDB:4C1H}.
SEQUENCE 257 AA; 28092 MW; 268EBFB7DDA45431 CRC64;
MKKNTLLKVG LCVGLLGTIQ FVSTISSVQA SQKVEKTVIK NETGTISISQ LNKNVWVHTE
LGSFNGEAVP SNGLVLNTSK GLVLVDSSWD DKLTKELIEM VEKKFQKRVT DVIITHAHAD
RIGGIKTLKE RGIKAHSTAL TAELAKKNGY EEPLGDLQTV TNLKFGNMKV ETFYPGKGHT
EDNIVVWLPQ YNILVGGCLV KSTSAKDLGN VADAYVNEWS TSIENVLKRY RNINAVVPGH
GEVGDKGLLL HTLDLLK


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