BLO1_KLEOX
ID BLO1_KLEOX Reviewed; 291 AA.
AC P22391; Q9S6S0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Beta-lactamase OXY-1;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=bla;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E23004;
RX PubMed=2653216; DOI=10.1128/aac.33.1.63;
RA Arakawa Y., Ohta M., Kido N., Mori M., Ito H., Komatsu T., Fujii Y.,
RA Kato N.;
RT "Chromosomal beta-lactamase of Klebsiella oxytoca, a new class A enzyme
RT that hydrolyzes broad-spectrum beta-lactam antibiotics.";
RL Antimicrob. Agents Chemother. 33:63-70(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SL781, and SL7811;
RX PubMed=8132152; DOI=10.1111/j.1574-6968.1994.tb06671.x;
RA Fournier B., Arlet G., Lagrange P.H., Philippon A.;
RT "Klebsiella oxytoca: resistance to aztreonam by overproduction of the
RT chromosomally encoded beta-lactamase.";
RL FEMS Microbiol. Lett. 116:31-36(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KH66;
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).
CC -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active
CC against cephalosporins.
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 KH66 OXY-1 is known as OXY-1a.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; M27459; AAA25084.1; -; Genomic_DNA.
DR EMBL; Z30177; CAA82916.1; -; Genomic_DNA.
DR EMBL; Z30178; CAA82917.1; -; Genomic_DNA.
DR EMBL; Y17715; CAB42615.1; -; Genomic_DNA.
DR PIR; S42075; S42075.
DR RefSeq; WP_014228247.1; NZ_PQKQ01000002.1.
DR RefSeq; WP_063864546.1; NG_049845.1.
DR PDB; 3BYD; X-ray; 1.93 A; A=25-291.
DR PDBsum; 3BYD; -.
DR AlphaFoldDB; P22391; -.
DR SMR; P22391; -.
DR STRING; 571.MC52_15470; -.
DR KEGG; ag:AAA25084; -.
DR KEGG; ag:CAB42615; -.
DR eggNOG; COG2367; Bacteria.
DR EvolutionaryTrace; P22391; -.
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; -; 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; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Hydrolase; Signal.
FT SIGNAL 1..24
FT CHAIN 25..291
FT /note="Beta-lactamase OXY-1"
FT /id="PRO_0000016997"
FT ACT_SITE 73
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 262
FT /note="L -> P (in strain: KH66)"
FT VARIANT 278
FT /note="E -> K (in strain: KH66)"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:3BYD"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3BYD"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3BYD"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:3BYD"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3BYD"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:3BYD"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:3BYD"
SQ SEQUENCE 291 AA; 31044 MW; 9908F5AA97EDDC8A CRC64;
MLKSSWRKTA LMAAAAVPLL LASGSLWASA DAIQQKLADL EKRSGGRLGV ALINTADDSQ
TLYRGDERFA MCSTGKVMAA AAVLKQSESN PEVVNKRLEI KKSDLVVWSP ITEKHLQSGM
TLAELSAAAL QYSDNTAMNK MISYLGGPEK VTAFAQSIGD VTFRLDRTEP ALNSAIPGDK
RDTTTPLAMA ESLRKLTLGN ALGEQQRAQL VTWLKGNTTG GQSIRAGLPA SWAVGDKTGA
GDYGTTNDIA VIWPENHAPL VLVTYFTQPQ QDAKSRKEVL AAAAKIVTEG L
