BLO1_ECOLX
ID BLO1_ECOLX Reviewed; 276 AA.
AC P13661;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-lactamase OXA-1;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=bla; Synonyms=oxa1;
OS Escherichia coli.
OG Plasmid RGN238.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn2603;
RX PubMed=2823258; DOI=10.1073/pnas.84.21.7378;
RA Ouellette M., Bissonnette L., Roy P.H.;
RT "Precise insertion of antibiotic resistance determinants into Tn21-like
RT transposons: nucleotide sequence of the OXA-1 beta-lactamase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7378-7382(1987).
RN [2]
RP SEQUENCE REVISION TO 131.
RA Ouellette M., Roy P.H.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 26-276, PROTEIN SEQUENCE OF
RP N-TERMINUS, CARBOXYLATION AT LYS-74, AND SUBUNIT.
RX PubMed=12493831; DOI=10.1110/ps.0224303;
RA Sun T., Nukaga M., Mayama K., Braswell E.H., Knox J.R.;
RT "Comparison of beta-lactamases of classes A and D: 1.5-A crystallographic
RT structure of the class D OXA-1 oxacillinase.";
RL Protein Sci. 12:82-91(2003).
CC -!- FUNCTION: This is an oxacillin-hydrolyzing beta-lactamase.
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:PRU10103};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12493831}.
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; J02967; AAA91586.2; -; Genomic_DNA.
DR PIR; A39880; A39880.
DR RefSeq; NP_957554.1; NC_005327.1.
DR RefSeq; WP_001334766.1; NZ_WUUG01000022.1.
DR RefSeq; YP_006953880.1; NC_019089.1.
DR RefSeq; YP_008574821.1; NC_022374.1.
DR PDB; 1M6K; X-ray; 1.50 A; A/B=26-276.
DR PDB; 3ISG; X-ray; 1.40 A; A/B=26-276.
DR PDB; 4MLL; X-ray; 1.37 A; A/B/C/D=26-276.
DR PDBsum; 1M6K; -.
DR PDBsum; 3ISG; -.
DR PDBsum; 4MLL; -.
DR AlphaFoldDB; P13661; -.
DR SMR; P13661; -.
DR BindingDB; P13661; -.
DR ChEMBL; CHEMBL4951; -.
DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR DrugCentral; P13661; -.
DR KEGG; ag:AAA91586; -.
DR BRENDA; 3.5.2.6; 2026.
DR SABIO-RK; P13661; -.
DR EvolutionaryTrace; P13661; -.
DR PRO; PR:P13661; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0008658; F:penicillin 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 Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW Plasmid; Signal; Transposable element.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12493831"
FT CHAIN 26..276
FT /note="Beta-lactamase OXA-1"
FT /id="PRO_0000017024"
FT ACT_SITE 71
FT /note="Acyl-ester intermediate"
FT BINDING 238..240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:12493831"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:4MLL"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:4MLL"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 227..236
FT /evidence="ECO:0007829|PDB:4MLL"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:4MLL"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:4MLL"
SQ SEQUENCE 276 AA; 30880 MW; 5ADF7626422BA124 CRC64;
MKNTIHINFA IFLIIANIIY SSASASTDIS TVASPLFEGT EGCFLLYDAS TNAEIAQFNK
AKCATQMAPD STFKIALSLM AFDAEIIDQK TIFKWDKTPK GMEIWNSNHT PKTWMQFSVV
WVSQEITQKI GLNKIKNYLK DFDYGNQDFS GDKERNNGLT EAWLESSLKI SPEEQIQFLR
KIINHNLPVK NSAIENTIEN MYLQDLDNST KLYGKTGAGF TANRTLQNGW FEGFIISKSG
HKYVFVSALT GNLGSNLTSS IKAKKNAITI LNTLNL
