BLC1_ECOLX
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 03-AUG-2022, entry version 122.
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; Proteobacteria; 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}.
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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 AlphaFoldDB; P28585; -.
DR SMR; P28585; -.
DR BindingDB; P28585; -.
DR GeneID; 39692553; -.
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; -; 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 Antibiotic resistance; Direct protein sequencing; Hydrolase; Plasmid;
KW 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"
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
