ID   BLO2_KLEOX              Reviewed;         290 AA.
AC   P23954; P71418;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=Beta-lactamase OXY-2;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla;
OS   Klebsiella oxytoca.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SL911;
RX   PubMed=8834898; DOI=10.1128/aac.40.2.460;
RA   Fournier B., Lagrange P.H., Philippon A.;
RT   "Beta-lactamase gene promoters of 71 clinical strains of Klebsiella
RT   oxytoca.";
RL   Antimicrob. Agents Chemother. 40:460-463(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SB23;
RX   PubMed=8878568; DOI=10.1128/aac.40.9.1988;
RA   Kimura K., Arakawa Y., Ohsuka S., Ito H., Suzuki K., Kurokawa H., Kato N.,
RA   Ohta M.;
RT   "Molecular aspects of high-level resistance to sulbactam-cefoperazone in
RT   Klebsiella oxytoca clinical isolates.";
RL   Antimicrob. Agents Chemother. 40:1988-1994(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KH11;
RX   PubMed=10223957; DOI=10.1128/aac.43.5.1294;
RA   Wu S.W., Dornbusch K., Kronvall G.;
RT   "Genetic characterization of resistance to extended-spectrum beta-lactams
RT   in Klebsiella oxytoca isolates recovered from patients with septicemia at
RT   hospitals in the Stockholm area.";
RL   Antimicrob. Agents Chemother. 43:1294-1297(1999).
RN   [4]
RP   PROTEIN SEQUENCE OF 28-290.
RC   STRAIN=D488;
RX   PubMed=1909282; DOI=10.1016/0378-1097(91)90301-p;
RA   Reynaud A., Peduzzi J., Barthelemy M., Labia R.;
RT   "Cefotaxime-hydrolysing activity of the beta-lactamase of Klebsiella
RT   oxytoca D488 could be related to a threonine residue at position 140.";
RL   FEMS Microbiol. Lett. 65:185-192(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 28-290.
RC   STRAIN=HB60;
RX   PubMed=9462429; DOI=10.1093/jac/40.6.789;
RA   Farzaneh S., Peduzzi J., Sofer L., Reynaud A., Barthelemy M., Labia R.;
RT   "Characterization and amino acid sequence of the OXY-2 group beta-lactamase
RT   of pI 5.7 isolated from aztreonam-resistant Klebsiella oxytoca strain
RT   HB60.";
RL   J. Antimicrob. Chemother. 40:789-795(1997).
RN   [6]
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   -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active
CC       against all third-generation cephalosporins but ceftazidime.
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: In strain KH11 OXY-2 is known as OXY-2a.
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; Z49084; CAA88908.1; -; Genomic_DNA.
DR   EMBL; D84548; BAA12695.1; -; Genomic_DNA.
DR   EMBL; Y17714; CAB42614.1; -; Genomic_DNA.
DR   RefSeq; WP_017146441.1; NG_049856.1.
DR   AlphaFoldDB; P23954; -.
DR   SMR; P23954; -.
DR   CARD; ARO:3002402; OXY-2-7; ARO:0001004; antibiotic inactivation.
DR   OrthoDB; 9784149at2; -.
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   InterPro; IPR058162; OXY-1/2.
DR   NCBIfam; NF033103; bla_class_A; 1.
DR   NCBIfam; NF000271; blaOXY; 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   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:1909282,
FT                   ECO:0000269|PubMed:9462429"
FT   CHAIN           28..290
FT                   /note="Beta-lactamase OXY-2"
FT                   /id="PRO_0000016998"
FT   ACT_SITE        72
FT                   /note="Nucleophile; acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        75
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   BINDING         236..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         15
FT                   /note="Missing (in strain: KH11 and SB23)"
FT   VARIANT         199
FT                   /note="D -> N (in strain: D488 and HB60)"
FT   VARIANT         225
FT                   /note="A -> V (in strain: D488)"
FT   VARIANT         255
FT                   /note="D -> N (in strain: D488)"
SQ   SEQUENCE   290 AA;  31136 MW;  134C4BC24E9999E7 CRC64;
     MIKSSWRKIA MLAAAVPLLL ASGALWASTD AIHQKLTDLE KRSGGRLGVA LINTADNSQI
     LYRGDERFAM CSTSKVMAAA AVLKQSESNK EVVNKRLEIN AADLVVWSPI TEKHLQSGMT
     LAELSAATLQ YSDNTAMNLI IGYLGGPEKV TAFARSIGDA TFRLDRTEPT LNTAIPGDER
     DTSTPLAMAE SLRKLTLGDA LGEQQRAQLV TWLKGNTTGG QSIRAGLPES WVVGDKTGAG
     DYGTTNDIAV IWPEDHAPLV LVTYFTQPQQ DAKNRKEVLA AAAKIVTEGL
//