ID   BLAB5_ELIME             Reviewed;         249 AA.
AC   Q9KJA9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 75.
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-5 {ECO:0000250|UniProtKB:O08498};
DE            Short=CHbetaL-5 {ECO:0000250|UniProtKB:O08498};
DE   AltName: Full=Class B carbapenemase BlaB-5 {ECO:0000250|UniProtKB:O08498};
DE   AltName: Full=Metallo-beta-lactamase type II {ECO:0000250|UniProtKB:O08498};
DE   Flags: Precursor;
GN   Name=blaB5; Synonyms=blaB {ECO:0000250|UniProtKB:O08498};
OS   Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 11306 / CIP 79.5;
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; AF189303; AAF89159.1; -; Genomic_DNA.
DR   RefSeq; WP_063857828.1; NG_048699.1.
DR   AlphaFoldDB; Q9KJA9; -.
DR   SMR; Q9KJA9; -.
DR   KEGG; ag:AAF89159; -.
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   CDD; cd16316; BlaB-like_MBL-B1; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001018; Beta-lactamase_class-B_CS.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR42951:SF20; BETA LACTAMASE; 1.
DR   PANTHER; PTHR42951; METALLO-BETA-LACTAMASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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   CHAIN           23..249
FT                   /note="Metallo-beta-lactamase type 2"
FT                   /id="PRO_0000016953"
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;  28161 MW;  252BA20FCEF1A837 CRC64;
     MLKRLKGLLV LALGFTGLQV FGQQNPDIKI EKLKDNLYVY TTYNTFKGTK YAANAVYMVT
     DKGVVVIDSP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH DDRAGGLEYF GKLGAKTYST
     KMTDSILAKE NKPRAKYTFD NNKSFKVGNT EFQVYYPGKG HTADNVVVWF PKDKVLVGGC
     IVKSGDSKDL GYIGEAYVND WTQSIHNIQQ KFPDVQYVVA GHDDWKDQTS IQHTLDLISD
     YQQKQKASN
//