BLAB1_ELIME
ID BLAB1_ELIME Reviewed; 249 AA.
AC O08498;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000269|PubMed:9576862};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000305};
DE AltName: Full=Beta-lactamase type II {ECO:0000303|PubMed:10858348};
DE AltName: Full=Carbapenem-hydrolyzing beta-lactamase BlaB-1 {ECO:0000303|PubMed:9576862};
DE Short=CHbetaL-1 {ECO:0000303|PubMed:10858348};
DE AltName: Full=Class B carbapenemase BlaB-1 {ECO:0000303|PubMed:10858348};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000303|PubMed:10858348};
DE Flags: Precursor;
GN Name=blaB1; Synonyms=blaB {ECO:0000303|PubMed:9576862};
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585;
RX PubMed=9576862; DOI=10.1042/bj3320145;
RA Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S., Perilli M.,
RA Galleni M., Frere J.-M., Amicosante G.;
RT "Characterization and sequence of the Chryseobacterium (Flavobacterium)
RT meningosepticum carbapenemase: a new molecular class B beta-lactamase
RT showing a broad substrate profile.";
RL Biochem. J. 332:145-152(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PINT;
RX PubMed=10858348; DOI=10.1128/aac.44.7.1878-1886.2000;
RA Bellais S., Aubert D., Naas T., Nordmann P.;
RT "Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing
RT beta-lactamases in Chryseobacterium meningosepticum.";
RL Antimicrob. Agents Chemother. 44:1878-1886(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-222 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=12684522; DOI=10.1074/jbc.m301062200;
RA Garcia-Saez I., Hopkins J., Papamicael C., Franceschini N., Amicosante G.,
RA Rossolini G.M., Galleni M., Frere J.M., Dideberg O.;
RT "The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-
RT lactamase in complex with the inhibitor, D-captopril.";
RL J. Biol. Chem. 278:23868-23873(2003).
CC -!- FUNCTION: Confers resistance to the different beta-lactams antibiotics
CC (penicillin, cephalosporin and carbapenem) via the hydrolysis of the
CC beta-lactam ring. {ECO:0000269|PubMed:9576862}.
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:0000269|PubMed:9576862};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12684522};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12684522};
CC -!- ACTIVITY REGULATION: Inhibited by chelating agents such as EDTA, 1-10
CC phenanthroline and pyridine-2,6-dicarboxylic acid.
CC {ECO:0000269|PubMed:9576862}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for cefoxitin {ECO:0000269|PubMed:9576862};
CC KM=29 uM for cephaloridine {ECO:0000269|PubMed:9576862};
CC KM=32 uM for penicillin G {ECO:0000269|PubMed:9576862};
CC KM=43 uM for 6-beta-iodopenicillanate {ECO:0000269|PubMed:9576862};
CC KM=66 uM for nitrocefin {ECO:0000269|PubMed:9576862};
CC KM=180 uM for cefotaxime {ECO:0000269|PubMed:9576862};
CC KM=370 uM for imipenem {ECO:0000269|PubMed:9576862};
CC Note=kcat is 350 sec(-1) for lactamase activity with imipenem as
CC substrate. kcat is 300 sec(-1) for lactamase activity with 6-beta-
CC iodopenicillanate as substrate. kcat is 280 sec(-1) for lactamase
CC activity with penicillin G as substrate. kcat is 39 sec(-1) for
CC lactamase activity with cefotaxime as substrate. kcat is 17 sec(-1)
CC for lactamase activity with nitrocefin as substrate. kcat is 14 sec(-
CC 1) for lactamase activity with cephaloridine as substrate. kcat is 6
CC sec(-1) for lactamase activity with cefoxitin as substrate.
CC {ECO:0000269|PubMed:9576862};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12684522,
CC ECO:0000269|PubMed:9576862}.
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; X96858; CAA65601.1; -; Genomic_DNA.
DR EMBL; AF189298; AAF89154.1; -; Genomic_DNA.
DR RefSeq; WP_029729112.1; NG_048691.1.
DR PDB; 1M2X; X-ray; 1.50 A; A/B/C/D=27-249.
DR PDBsum; 1M2X; -.
DR AlphaFoldDB; O08498; -.
DR SMR; O08498; -.
DR ChEMBL; CHEMBL1667692; -.
DR DrugBank; DB02032; Epicaptopril.
DR KEGG; ag:CAA65601; -.
DR BioCyc; MetaCyc:MON-13428; -.
DR EvolutionaryTrace; O08498; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0017001; P:antibiotic catabolic process; IDA: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; Direct protein sequencing; Hydrolase;
KW Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:9576862"
FT CHAIN 23..249
FT /note="Metallo-beta-lactamase type 2"
FT /id="PRO_0000016949"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12684522"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12684522"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1M2X"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1M2X"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:1M2X"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1M2X"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:1M2X"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:1M2X"
SQ 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
