BLAB4_ELIME
ID BLAB4_ELIME Reviewed; 249 AA.
AC Q9XBN7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Metallo-beta-lactamase type 2 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:O08498};
DE AltName: Full=B2 metallo-beta-lactamase {ECO:0000250|UniProtKB:O08498};
DE AltName: Full=Beta-lactamase type II {ECO:0000250|UniProtKB:O08498};
DE AltName: Full=Carbapenem-hydrolyzing beta-lactamase BlaB-4 {ECO:0000250|UniProtKB:O08498};
DE Short=CHbetaL-4 {ECO:0000250|UniProtKB:O08498};
DE AltName: Full=Class B carbapenemase BlaB-4 {ECO:0000250|UniProtKB:O08498};
DE AltName: Full=Metallo lactamase BlaB-3 {ECO:0000303|PubMed:10817691};
DE AltName: Full=Metallo-beta-lactamase type II {ECO:0000250|UniProtKB:O08498};
DE Flags: Precursor;
GN Name=blaB4;
GN Synonyms=blaB {ECO:0000250|UniProtKB:O08498},
GN blaB3 {ECO:0000303|PubMed:10817691};
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13253 / DSM 2800 / CCUG 214 / CIP 60.57 / LMG 12279 / NBRC
RC 12535 / NCTC 100 / 1416;
RX PubMed=10817691; DOI=10.1128/aac.44.6.1448-1452.2000;
RA Woodford N., Palepou M.-F.I., Babini G.S., Holmes B., Livermore D.M.;
RT "Carbapenemases of chryseobacterium (Flavobacterium) meningosepticum:
RT distribution of blaB and characterization of a novel metallo-beta-lactamase
RT gene, blaB3, in the type strain, NCTC 10016.";
RL Antimicrob. Agents Chemother. 44:1448-1452(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13253 / DSM 2800 / CCUG 214 / CIP 60.57 / LMG 12279 / NBRC
RC 12535 / NCTC 100 / 1416;
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).
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:0000250|UniProtKB:O08498}.
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:O08498};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O08498};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O08498};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O08498}.
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; AF162284; AAD43582.1; -; Genomic_DNA.
DR RefSeq; WP_063857827.1; NG_048698.1.
DR AlphaFoldDB; Q9XBN7; -.
DR SMR; Q9XBN7; -.
DR STRING; 1216967.L100_02762; -.
DR KEGG; ag:AAD43582; -.
DR eggNOG; COG0491; Bacteria.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Antibiotic resistance; Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:O08498, ECO:0000255,
FT ECO:0000305|PubMed:10817691"
FT CHAIN 23..249
FT /note="Metallo-beta-lactamase type 2"
FT /id="PRO_0000016952"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O08498"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O08498"
SQ SEQUENCE 249 AA; 28225 MW; F5327FD6516153B5 CRC64;
MMKKMKWALV LALGLTGLNA FGQETPEVKI EKLKDNLYVY TTYNTFNGTK YAANAVYLVT
SKGVVVIDSP WGEEKFKNFT DEIYKRHGKK VIMNIATHSH DDRAGGLEYF KSLGAKTYST
KMTDSILAKD NKPRAQYTFD NNKSFKVGKD EFQVYYPGKG HTADHVVVWF PKDKVLVGGC
IIKSGDSKDL GFLGEAYVND WTQSVHNIQK KFPNVQYVVA GHDDWKDQTA IQHTLDLISE
YQQKQKASN
