ID   BLT2_ECOLX              Reviewed;         289 AA.
AC   O69395;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Beta-lactamase Toho-2;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla;
OS   Escherichia coli.
OG   Plasmid IncFII pMTY036.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TUM1083;
RX   PubMed=9593147; DOI=10.1128/aac.42.5.1181;
RA   Ma L., Ishii Y., Ishiguro M., Matsuzawa H., Yamaguchi K.;
RT   "Cloning and sequencing of the gene encoding Toho-2, a class A beta-
RT   lactamase preferentially inhibited by tazobactam.";
RL   Antimicrob. Agents Chemother. 42:1181-1186(1998).
CC   -!- FUNCTION: Hydrolyzes beta-lactam antibiotics such as penicillin G,
CC       carbenicillin, cephaloridine, cefoxitin, cefotaxime, ceftazidime, and
CC       aztreonam. Has especially increased relative hydrolysis rates for
CC       cephalothin, cephaloridine, cefotaxime and ceftizoxime.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- ACTIVITY REGULATION: Inhibited 16-fold better by the beta-lactamase
CC       inhibitor tazobactam than by clavulanic acid.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; D89862; BAA28282.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69395; -.
DR   SMR; O69395; -.
DR   KEGG; ag:BAA28282; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..289
FT                   /note="Beta-lactamase Toho-2"
FT                   /id="PRO_0000016995"
FT   ACT_SITE        73
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         235..237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  30745 MW;  A75723E1793060A6 CRC64;
     MVTKRVQRMM SAAAACIPLL LGSPTLYAQT SAVQQKLAAL EKSSGGRLGV ALIDTADNTQ
     VLYRGDERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
     TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTEP TLNTAIPGDP
     RDTTTARAGA DVASLRWVMR WAKPSGAVGD VAQRQYDRAA GIRAGLPTSW TVGDKTGSGD
     YGTTNDIAVI WPQGRAPLVL VTYFTQPQQN AESRRDVLAS AARIIAEGL
//