ID   BLC6_SALTM              Reviewed;         291 AA.
AC   O65976;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Beta-lactamase CTX-M-6;
DE            EC=3.5.2.6;
DE   AltName: Full=Cefotaximase 6;
DE   Flags: Precursor;
GN   Name=bla;
OS   Salmonella typhimurium.
OG   Plasmid pAS31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AS31;
RX   PubMed=9742701; DOI=10.1111/j.1574-6968.1998.tb13159.x;
RA   Gazouli M., Tzelepi E., Markogiannakis A., Legakis N.J., Tzouvelekis L.S.;
RT   "Two novel plasmid-mediated cefotaxime-hydrolyzing beta-lactamases (CTX-M-5
RT   and CTX-M-6) from Salmonella typhimurium.";
RL   FEMS Microbiol. Lett. 165:289-293(1998).
CC   -!- FUNCTION: Has cefotaxime-hydrolyzing activity.
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; AJ005045; CAA06312.1; -; Genomic_DNA.
DR   RefSeq; WP_032489171.1; NG_049021.1.
DR   AlphaFoldDB; O65976; -.
DR   SMR; O65976; -.
DR   KEGG; ag:CAA06312; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..291
FT                   /note="Beta-lactamase CTX-M-6"
FT                   /id="PRO_0000016993"
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;  31207 MW;  DC95E4FE77531053 CRC64;
     MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ
     ILYVADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI RASDLVNYNP IAEKHVNGTM
     TLAQLGAGAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNSAIPGDP
     RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWGVGDKTGS
     GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAESRRDVL AAAAKIVTHG F
//