ID   BLC2_SALTM              Reviewed;         291 AA.
AC   P74841;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Beta-lactamase CTX-M-2;
DE            EC=3.5.2.6;
DE   AltName: Full=Cefotaximase 2;
DE   Flags: Precursor;
GN   Name=bla;
OS   Salmonella typhimurium.
OG   Plasmid pMVP-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CAS-5;
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).
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; X92507; CAA63263.1; -; Genomic_DNA.
DR   RefSeq; WP_025368620.1; NZ_LVFM01000032.1.
DR   AlphaFoldDB; P74841; -.
DR   SMR; P74841; -.
DR   KEGG; ag:CAA63263; -.
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   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-2"
FT                   /id="PRO_0000016990"
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;  31378 MW;  82277CD9CD41E7C0 CRC64;
     MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ
     ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI KKSDLVNYNP IAEKHVNGTM
     TLAELGAAAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNTAIPGDP
     RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS
     GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAESRRDIL AAAAKIVTHG F