BLO2_SALTM
ID BLO2_SALTM Reviewed; 275 AA.
AC P0A1V8; P05191; Q57015;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Beta-lactamase OXA-2;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=bla; Synonyms=oxa2;
OS Salmonella typhimurium.
OG Plasmid IncN R46, and Plasmid pBP11.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Type 1A; PLASMID=IncN R46;
RX PubMed=3876949; DOI=10.1016/0014-5793(85)80989-3;
RA Dale J.W., Godwin D., Mossakowska D., Stephenson P., Wall S.;
RT "Sequence of the OXA2 beta-lactamase: comparison with other penicillin-
RT reactive enzymes.";
RL FEBS Lett. 191:39-44(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncN R46;
RX PubMed=2538329; DOI=10.1111/j.1432-1033.1989.tb14649.x;
RA Mossakowska D., Ali N.A., Dale J.W.;
RT "Oxacillin-hydrolysing beta-lactamases. A comparative analysis at
RT nucleotide and amino acid sequence levels.";
RL Eur. J. Biochem. 180:309-318(1989).
RN [3]
RP PROTEIN SEQUENCE OF 22-32.
RC PLASMID=IncN R46;
RX PubMed=6335398; DOI=10.1042/bj2241009;
RA Holland S., Dale J.W.;
RT "Improved purification and characterization of the OXA-2 beta-lactamase.";
RL Biochem. J. 224:1009-1013(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pBP11;
RX PubMed=2689593; DOI=10.1099/00221287-135-4-761;
RA Nuecken E.J., Henschke R.B., Schmidt F.R.J.;
RT "Nucleotide sequence of an OXA-2 beta-lactamase gene from the R-plasmid
RT R1767 derived plasmid pBP11 and comparison to closely related resistance
RT determinants found in R46 and Tn2603.";
RL J. Gen. Microbiol. 135:761-765(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 22-275, AND CARBOXYLATION AT
RP LYS-75.
RX PubMed=8240304; DOI=10.1042/bj2950871;
RA Ledent P., Frere J.M.;
RT "Substrate-induced inactivation of the OXA2 beta-lactamase.";
RL Biochem. J. 295:871-878(1993).
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 -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M25261; AAA98357.1; -; Genomic_DNA.
DR EMBL; X03037; CAA26839.1; -; Genomic_DNA.
DR EMBL; X07260; CAA30246.1; -; Genomic_DNA.
DR PIR; A91350; PNEBT.
DR RefSeq; NP_511223.1; NC_003292.1.
DR RefSeq; NP_511225.1; NC_003292.1.
DR RefSeq; WP_001007673.1; NG_049496.1.
DR PDB; 1K38; X-ray; 1.50 A; A/B=22-275.
DR PDBsum; 1K38; -.
DR AlphaFoldDB; P0A1V8; -.
DR SMR; P0A1V8; -.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR GeneID; 67369352; -.
DR KEGG; ag:CAA30246; -.
DR EvolutionaryTrace; P0A1V8; -.
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.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:6335398"
FT CHAIN 22..275
FT /note="Beta-lactamase OXA-2"
FT /id="PRO_0000017026"
FT ACT_SITE 72
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT BINDING 210..212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:8240304"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1K38"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1K38"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 205..226
FT /evidence="ECO:0007829|PDB:1K38"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:1K38"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:1K38"
SQ SEQUENCE 275 AA; 31686 MW; D3678DFCB78DE8B6 CRC64;
MAIRIFAILF SIFSLATFAH AQEGTLERSD WRKFFSEFQA KGTIVVADER QADRAMLVFD
PVRSKKRYSP ASTFKIPHTL FALDAGAVRD EFQIFRWDGV NRGFAGHNQD QDLRSAMRNS
TVWVYELFAK EIGDDKARRY LKKIDYGNAD PSTSNGDYWI EGSLAISAQE QIAFLRKLYR
NELPFRVEHQ RLVKDLMIVE AGRNWILRAK TGWEGRMGWW VGWVEWPTGS VFFALNIDTP
NRMDDLFKRE AIVRAILRSI EALPPNPAVN SDAAR
