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Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (BLA-IMP) (IMP-1) (Beta-lactamase type II) (Metallo-beta-lactamase type II)

 BLAB_SERMA              Reviewed;         246 AA.
P52699;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 93.
RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
EC=3.5.2.6 {ECO:0000269|PubMed:8141584};
AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
AltName: Full=BLA-IMP {ECO:0000303|PubMed:8141584};
Short=IMP-1 {ECO:0000303|PubMed:8141584};
AltName: Full=Beta-lactamase type II {ECO:0000303|PubMed:8141584};
AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:8141584};
Flags: Precursor;
Serratia marcescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Yersiniaceae; Serratia.
NCBI_TaxID=615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-42,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, AND SUBSTRATE SPECIFICITY.
STRAIN=AK9373 / TN9106;
PubMed=8141584; DOI=10.1128/AAC.38.1.71;
Osano E., Arakawa Y., Wacharotayankun R., Ohta M., Horii T., Ito H.,
Yoshimura F., Kato N.;
"Molecular characterization of an enterobacterial metallo beta-
lactamase found in a clinical isolate of Serratia marcescens that
shows imipenem resistance.";
Antimicrob. Agents Chemother. 38:71-78(1994).
[2]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 19-246 IN COMPLEX WITH
SUBSTRATE ANALOG 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. {ECO:0000269|PubMed:8141584}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000269|PubMed:8141584}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:26482303};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:26482303};
-!- ENZYME REGULATION: Inhibited by captopril stereoisomers, Hg(2+),
Fe(2+), Cu(2+) and by chelating agents such as EDTA
(PubMed:8141584, PubMed:26482303). This enzyme is not susceptible
to inactivation by the beta-lactamase-blocking agents clavulanic
acid or cloxacillin (PubMed:8141584).
{ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:8141584}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.74 uM for meropenem {ECO:0000269|PubMed:8141584};
KM=1.24 uM for ceftazidime {ECO:0000269|PubMed:8141584};
KM=2.07 uM for ceftizoxime and panipenem
{ECO:0000269|PubMed:8141584};
KM=2.13 uM for cefoperazone {ECO:0000269|PubMed:8141584};
KM=2.15 uM for ampicillin {ECO:0000269|PubMed:8141584};
KM=3.97 uM for aztreonam {ECO:0000269|PubMed:8141584};
KM=7.33 uM for imipenem {ECO:0000269|PubMed:8141584};
KM=7.55 uM for moxalactam {ECO:0000269|PubMed:8141584};
KM=7.74 uM for cephaloridine {ECO:0000269|PubMed:8141584};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P25910}.
-!- 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; S71932; AAB30289.1; -; Genomic_DNA.
EMBL; D50438; BAA08930.1; -; Genomic_DNA.
RefSeq; WP_003159548.1; NG_049172.1.
PDB; 1DD6; X-ray; 2.00 A; A/B=19-246.
PDB; 1VGN; X-ray; 2.63 A; A/B=19-246.
PDB; 1WUO; X-ray; 2.01 A; A/B/C/D=19-246.
PDB; 1WUP; X-ray; 3.00 A; A/B/C/D=19-246.
PDB; 2DOO; X-ray; 2.43 A; A/B=19-246.
PDB; 4C1F; X-ray; 2.01 A; A/B=19-246.
PDB; 4C1G; X-ray; 1.71 A; A/B=19-246.
PDB; 5EV6; X-ray; 1.98 A; A/B/C/D=19-246.
PDB; 5EV8; X-ray; 2.30 A; A/B/C/D=19-246.
PDB; 5EWA; X-ray; 2.30 A; A/B/C/D=19-246.
PDB; 5HH4; X-ray; 2.00 A; A/B/C/D=19-246.
PDBsum; 1DD6; -.
PDBsum; 1VGN; -.
PDBsum; 1WUO; -.
PDBsum; 1WUP; -.
PDBsum; 2DOO; -.
PDBsum; 4C1F; -.
PDBsum; 4C1G; -.
PDBsum; 5EV6; -.
PDBsum; 5EV8; -.
PDBsum; 5EWA; -.
PDBsum; 5HH4; -.
ProteinModelPortal; P52699; -.
SMR; P52699; -.
DrugBank; DB04749; 2-(3-OXO-PROPYLSULFANYLCARBONYL)-ETHANETHIOLATE.
DrugBank; DB02706; Mercaptocarboxylate Inhibitor.
DrugBank; DB07526; N-[4-({[5-(DIMETHYLAMINO)-1-NAPHTHYL]SULFONYL}AMINO)BUTYL]-3-SULFANYLPROPANAMIDE.
KEGG; ag:AAB30289; -.
KO; K18782; -.
BRENDA; 3.5.2.6; 5690.
EvolutionaryTrace; P52699; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; IDA: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; 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;
3D-structure; Antibiotic resistance; Direct protein sequencing;
Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
SIGNAL 1 18 {ECO:0000269|PubMed:8141584}.
CHAIN 19 246 Metallo-beta-lactamase type 2.
/FTId=PRO_0000016946.
METAL 95 95 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:26482303}.
METAL 97 97 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:26482303}.
METAL 99 99 Zinc 2. {ECO:0000269|PubMed:26482303}.
METAL 157 157 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:26482303}.
METAL 176 176 Zinc 2. {ECO:0000269|PubMed:26482303}.
METAL 215 215 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:26482303}.
BINDING 179 179 Substrate. {ECO:0000269|PubMed:26482303}.
BINDING 185 185 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P25910}.
STRAND 26 31 {ECO:0000244|PDB:4C1G}.
STRAND 34 43 {ECO:0000244|PDB:4C1G}.
TURN 44 46 {ECO:0000244|PDB:4C1G}.
STRAND 47 58 {ECO:0000244|PDB:4C1G}.
STRAND 61 66 {ECO:0000244|PDB:4C1G}.
HELIX 71 83 {ECO:0000244|PDB:4C1G}.
STRAND 87 92 {ECO:0000244|PDB:4C1G}.
STRAND 94 97 {ECO:0000244|PDB:4C1G}.
HELIX 98 101 {ECO:0000244|PDB:4C1G}.
HELIX 104 109 {ECO:0000244|PDB:4C1G}.
STRAND 114 117 {ECO:0000244|PDB:4C1G}.
HELIX 118 126 {ECO:0000244|PDB:4C1G}.
STRAND 133 136 {ECO:0000244|PDB:4C1G}.
STRAND 138 144 {ECO:0000244|PDB:4C1G}.
TURN 145 147 {ECO:0000244|PDB:4C1G}.
STRAND 148 151 {ECO:0000244|PDB:4C1G}.
STRAND 155 158 {ECO:0000244|PDB:4C1G}.
STRAND 163 166 {ECO:0000244|PDB:4C1G}.
TURN 167 170 {ECO:0000244|PDB:4C1G}.
STRAND 171 175 {ECO:0000244|PDB:4C1G}.
TURN 191 193 {ECO:0000244|PDB:4C1G}.
HELIX 194 205 {ECO:0000244|PDB:4C1G}.
STRAND 209 216 {ECO:0000244|PDB:4C1G}.
HELIX 222 238 {ECO:0000244|PDB:4C1G}.
SEQUENCE 246 AA; 27120 MW; 9B2599E8F1B22D36 CRC64;
MSKLSVFFIF LFCSIATAAE SLPDLKIEKL DEGVYVHTSF EEVNGWGVVP KHGLVVLVNA
EAYLIDTPFT AKDTEKLVTW FVERGYKIKG SISSHFHSDS TGGIEWLNSR SIPTYASELT
NELLKKDGKV QATNSFSGVN YWLVKNKIEV FYPGPGHTPD NVVVWLPERK ILFGGCFIKP
YGLGNLGDAN IEAWPKSAKL LKSKYGKAKL VVPSHSEVGD ASLLKLTLEQ AVKGLNESKK
PSKPSN


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