ID BLC1_ECOLX Reviewed; 291 AA. AC P28585; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 27-MAR-2024, entry version 128. DE RecName: Full=Beta-lactamase CTX-M-1; DE EC=3.5.2.6; DE AltName: Full=Beta-lactamase MEN-1; DE AltName: Full=Cefotaximase 1; DE Flags: Precursor; GN Name=bla; Synonyms=men1; OS Escherichia coli. OG Plasmid pMVP-3. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=GRI-1; RX PubMed=8834913; DOI=10.1128/aac.40.2.509; RA Bauernfeind A., Stemplinger I., Jungwirth R., Casellas J.M.; RT "Sequences of beta-lactamase genes encoding CTX-M-1 (MEN-1) and CTX-M-2 and RT relationship of their amino acid sequences with those of other beta- RT lactamases."; RL Antimicrob. Agents Chemother. 40:509-513(1996). RN [2] RP PROTEIN SEQUENCE OF 29-291. RC STRAIN=MEN; RX PubMed=1633193; DOI=10.1016/0167-4838(92)90121-s; RA Barthelemy M., Peduzzi J., Bernard H., Tancrede C., Labia R.; RT "Close amino acid sequence relationship between the new plasmid-mediated RT extended-spectrum beta-lactamase MEN-1 and chromosomally encoded enzymes of RT Klebsiella oxytoca."; RL Biochim. Biophys. Acta 1122:15-22(1992). CC -!- FUNCTION: Broad spectrum beta-lactamase which confers resistance to CC penicillins, as well as first, second and third-generation CC 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 -!- SIMILARITY: Belongs to the class-A 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; X92506; CAA63262.1; -; Genomic_DNA. DR PIR; S23929; S23929. DR RefSeq; WP_013188473.1; NZ_WVVL01000035.1. DR RefSeq; YP_006954479.1; NC_019098.1. DR RefSeq; YP_008995260.1; NC_023277.2. DR RefSeq; YP_008997418.1; NC_023289.2. DR RefSeq; YP_008998816.1; NC_023329.1. DR RefSeq; YP_009061062.1; NC_024974.1. DR RefSeq; YP_009061420.1; NC_024978.1. DR RefSeq; YP_009061643.1; NC_024979.1. DR RefSeq; YP_009061676.1; NC_024980.1. DR RefSeq; YP_009068156.1; NC_025138.1. DR RefSeq; YP_009068457.1; NC_025140.1. DR RefSeq; YP_009068512.1; NC_025141.1. DR RefSeq; YP_009068695.1; NC_025142.1. DR RefSeq; YP_009068890.1; NC_025143.1. DR RefSeq; YP_009069013.1; NC_025144.1. DR RefSeq; YP_009070899.1; NC_025176.1. DR RefSeq; YP_009328600.1; NC_032100.1. DR PDB; 7U48; X-ray; 1.67 A; A/B/C=1-291. DR PDB; 7U49; X-ray; 1.72 A; A/B/C=1-291. DR PDB; 7U4B; X-ray; 1.92 A; A/B/C=1-290. DR PDB; 7U57; X-ray; 2.37 A; A/B/C=1-291. DR PDBsum; 7U48; -. DR PDBsum; 7U49; -. DR PDBsum; 7U4B; -. DR PDBsum; 7U57; -. DR AlphaFoldDB; P28585; -. DR SMR; P28585; -. DR BindingDB; P28585; -. DR GeneID; 79719115; -. DR KEGG; ag:CAA63262; -. DR BRENDA; 3.5.2.6; 2026. 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; 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 PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-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 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase; KW Plasmid; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000269|PubMed:1633193" FT CHAIN 29..291 FT /note="Beta-lactamase CTX-M-1" FT /id="PRO_0000016989" 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 HELIX 32..44 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:7U48" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 75..87 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:7U4B" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 122..132 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 135..145 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 148..157 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 186..197 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 204..215 FT /evidence="ECO:0007829|PDB:7U48" FT TURN 221..223 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:7U48" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 245..253 FT /evidence="ECO:0007829|PDB:7U48" FT STRAND 260..267 FT /evidence="ECO:0007829|PDB:7U48" FT HELIX 277..288 FT /evidence="ECO:0007829|PDB:7U48" SQ SEQUENCE 291 AA; 31246 MW; D82501CF8AE55FC5 CRC64; MVKKSLRQFT LMATATVTLL LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ ILYRADERFA MCSTSKVMAV AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVDGTM SLAELSAAAL QYSDNVAMNK LISHVGGPAS VTAFARQLGD ETFRLDRTEP TLNTAIPGDP RDTTSPRAMA QTLRNLTLGK ALGDSQRAQL VTWMKGNTTG AASIQAGLPA SWVVGDKTGS GDYGTTNDIA VIWPKDRAPL ILVTYFTQPQ PKAESRRDVL ASAAKIVTNG L //