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-MAY-2023, entry version 78. 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; Pseudomonadota; 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; DD-peptidase/beta-lactamase superfamily; 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; beta-lactamase/transpeptidase-like; 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 //