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Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase type II) (Carbapenem-hydrolyzing beta-lactamase BlaB-1) (CHbetaL-1) (Class B carbapenemase BlaB-1) (Metallo-beta-lactamase type II)

 BLAB1_ELIME             Reviewed;         249 AA.
O08498;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 91.
RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
EC=3.5.2.6 {ECO:0000269|PubMed:9576862};
AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
AltName: Full=Beta-lactamase type II {ECO:0000303|PubMed:10858348};
AltName: Full=Carbapenem-hydrolyzing beta-lactamase BlaB-1 {ECO:0000303|PubMed:9576862};
Short=CHbetaL-1 {ECO:0000303|PubMed:10858348};
AltName: Full=Class B carbapenemase BlaB-1 {ECO:0000303|PubMed:10858348};
AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:10858348};
Flags: Precursor;
Name=blaB1; Synonyms=blaB {ECO:0000303|PubMed:9576862};
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Elizabethkingia.
NCBI_TaxID=238;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBUNIT, AND SUBSTRATE SPECIFICITY.
STRAIN=ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585;
PubMed=9576862; DOI=10.1042/bj3320145;
Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S.,
Perilli M., Galleni M., Frere J.-M., Amicosante G.;
"Characterization and sequence of the Chryseobacterium
(Flavobacterium) meningosepticum carbapenemase: a new molecular class
B beta-lactamase showing a broad substrate profile.";
Biochem. J. 332:145-152(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PINT;
PubMed=10858348; DOI=10.1128/AAC.44.7.1878-1886.2000;
Bellais S., Aubert D., Naas T., Nordmann P.;
"Molecular and biochemical heterogeneity of class B carbapenem-
hydrolyzing beta-lactamases in Chryseobacterium meningosepticum.";
Antimicrob. Agents Chemother. 44:1878-1886(2000).
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-222 IN COMPLEX WITH
SUBSTRATE ANALOG AND ZINC IONS, COFACTOR, AND SUBUNIT.
PubMed=12684522; DOI=10.1074/jbc.M301062200;
Garcia-Saez I., Hopkins J., Papamicael C., Franceschini N.,
Amicosante G., Rossolini G.M., Galleni M., Frere J.M., Dideberg O.;
"The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-
lactamase in complex with the inhibitor, D-captopril.";
J. Biol. Chem. 278:23868-23873(2003).
-!- FUNCTION: Confers resistance to the different beta-lactams
antibiotics (penicillin, cephalosporin and carbapenem) via the
hydrolysis of the beta-lactam ring. {ECO:0000269|PubMed:9576862}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000269|PubMed:9576862}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12684522};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:12684522};
-!- ENZYME REGULATION: Inhibited by chelating agents such as EDTA, 1-
10 phenanthroline and pyridine-2,6-dicarboxylic acid.
{ECO:0000269|PubMed:9576862}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=24 uM for cefoxitin {ECO:0000269|PubMed:9576862};
KM=29 uM for cephaloridine {ECO:0000269|PubMed:9576862};
KM=32 uM for penicillin G {ECO:0000269|PubMed:9576862};
KM=43 uM for 6-beta-iodopenicillanate
{ECO:0000269|PubMed:9576862};
KM=66 uM for nitrocefin {ECO:0000269|PubMed:9576862};
KM=180 uM for cefotaxime {ECO:0000269|PubMed:9576862};
KM=370 uM for imipenem {ECO:0000269|PubMed:9576862};
Note=Kcat is 350 sec(-1) for lactamase activity with imipenem as
substrate. Kcat is 300 sec(-1) for lactamase activity with 6-
beta-iodopenicillanate as substrate. Kcat is 280 sec(-1) for
lactamase activity with penicillin G as substrate. Kcat is 39
sec(-1) for lactamase activity with cefotaxime as substrate.
Kcat is 17 sec(-1) for lactamase activity with nitrocefin as
substrate. Kcat is 14 sec(-1) for lactamase activity with
cephaloridine as substrate. Kcat is 6 sec(-1) for lactamase
activity with cefoxitin as substrate.
{ECO:0000269|PubMed:9576862};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12684522,
ECO:0000269|PubMed:9576862}.
-!- 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; X96858; CAA65601.1; -; Genomic_DNA.
EMBL; AF189298; AAF89154.1; -; Genomic_DNA.
RefSeq; WP_029729112.1; NG_048691.1.
PDB; 1M2X; X-ray; 1.50 A; A/B/C/D=27-249.
PDBsum; 1M2X; -.
ProteinModelPortal; O08498; -.
SMR; O08498; -.
ChEMBL; CHEMBL1667692; -.
DrugBank; DB02032; 1-(3-Mercapto-2-Methyl-Propionyl)-Pyrrolidine-2-Carboxylic Acid.
BioCyc; MetaCyc:MONOMER-13428; -.
EvolutionaryTrace; O08498; -.
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 22 {ECO:0000269|PubMed:9576862}.
CHAIN 23 249 Metallo-beta-lactamase type 2.
/FTId=PRO_0000016949.
METAL 98 98 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:12684522}.
METAL 100 100 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:12684522}.
METAL 102 102 Zinc 2. {ECO:0000269|PubMed:12684522}.
METAL 161 161 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:12684522}.
METAL 180 180 Zinc 2. {ECO:0000269|PubMed:12684522}.
METAL 222 222 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:12684522}.
BINDING 183 183 Substrate. {ECO:0000269|PubMed:12684522}.
STRAND 28 34 {ECO:0000244|PDB:1M2X}.
STRAND 37 46 {ECO:0000244|PDB:1M2X}.
STRAND 49 60 {ECO:0000244|PDB:1M2X}.
STRAND 63 68 {ECO:0000244|PDB:1M2X}.
HELIX 73 75 {ECO:0000244|PDB:1M2X}.
HELIX 76 87 {ECO:0000244|PDB:1M2X}.
STRAND 91 95 {ECO:0000244|PDB:1M2X}.
STRAND 97 100 {ECO:0000244|PDB:1M2X}.
TURN 101 103 {ECO:0000244|PDB:1M2X}.
HELIX 107 112 {ECO:0000244|PDB:1M2X}.
STRAND 116 120 {ECO:0000244|PDB:1M2X}.
HELIX 121 129 {ECO:0000244|PDB:1M2X}.
STRAND 136 141 {ECO:0000244|PDB:1M2X}.
STRAND 143 147 {ECO:0000244|PDB:1M2X}.
STRAND 150 155 {ECO:0000244|PDB:1M2X}.
STRAND 159 164 {ECO:0000244|PDB:1M2X}.
STRAND 167 170 {ECO:0000244|PDB:1M2X}.
TURN 171 174 {ECO:0000244|PDB:1M2X}.
STRAND 175 179 {ECO:0000244|PDB:1M2X}.
HELIX 198 211 {ECO:0000244|PDB:1M2X}.
TURN 212 214 {ECO:0000244|PDB:1M2X}.
STRAND 216 223 {ECO:0000244|PDB:1M2X}.
HELIX 230 243 {ECO:0000244|PDB:1M2X}.
SEQUENCE 249 AA; 28144 MW; 0F042B5126E338F6 CRC64;
MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK YAANAVYLVT
DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH DDRAGGLEYF GKIGAKTYST
KMTDSILAKE NKPRAQYTFD NNKSFKVGKS EFQVYYPGKG HTADNVVVWF PKEKVLVGGC
IIKSADSKDL GYIGEAYVND WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE
YQQKQKASN


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