ID   BLA1_ENTCL              Reviewed;         286 AA.
AC   P18251;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Beta-lactamase Ohio-1;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
OS   Enterobacter cloacae.
OG   Plasmid pDS075.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Enterobacter;
OC   Enterobacter cloacae complex.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2121093; DOI=10.1128/aac.34.8.1570;
RA   Shlaes D.M., Currie-Mccumber C., Hull A., Behlau I., Kron M.;
RT   "OHIO-1 beta-lactamase is part of the SHV-1 family.";
RL   Antimicrob. Agents Chemother. 34:1570-1576(1990).
RN   [2]
RP   AMINO ACID NUMBERING SCHEME.
RX   PubMed=2039479; DOI=10.1042/bj2760269;
RA   Ambler R.P., Coulson A.F., Frere J.M., Ghuysen J.M., Joris B., Forsman M.,
RA   Levesque R.C., Tiraby G., Waley S.G.;
RT   "A standard numbering scheme for the class A beta-lactamases.";
RL   Biochem. J. 276:269-270(1991).
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   -!- MISCELLANEOUS: The class A beta-lactamase family has a specific amino-
CC       acid numbering system, sometimes called Ambler or ABL numbering and
CC       often misspelt as Amber. A multiple sequence alignment was used to
CC       derive a consensus sequence and then the consensus was numbered taking
CC       into account insertions and deletions. This allows use of identical
CC       numbers, e.g. for active site residues, despite differences in protein
CC       length. UniProt always uses natural numbering of residues, hence there
CC       appear to be differences in numbering between this entry and some
CC       papers. {ECO:0000305|PubMed:2039479}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M33655; AAA72078.1; -; Unassigned_DNA.
DR   PIR; A44958; A44958.
DR   AlphaFoldDB; P18251; -.
DR   SMR; P18251; -.
DR   DrugBank; DB01606; Tazobactam.
DR   CARD; ARO:3006956; OHIO-1; ARO:0001004; antibiotic inactivation.
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:InterPro.
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   NCBIfam; NF033103; bla_class_A; 1.
DR   NCBIfam; NF012143; SHV_LEN_OKP; 1.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE-TYPE TRANSPEPTIDASE FOLD 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; Disulfide bond; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..286
FT                   /note="Beta-lactamase Ohio-1"
FT                   /id="PRO_0000016996"
FT   ACT_SITE        66
FT                   /note="Nucleophile; acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..119
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31354 MW;  9FE16709361AF9C5 CRC64;
     MRYFRLCIIS LLATLPLRVH AGPQPLEQIK LSESQLSGSV GMIEMDLARP GTLTAWRADE
     RFPMMSTFKV VLCGAGLARV DAGDEQLERK IHYRRQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLPAVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTAR
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGRLIRSV LPAGWFIADK TGAGERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIAGAL IEHWQR
//