ID   BLC4_SALTM              Reviewed;         291 AA.
AC   O33807;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Beta-lactamase CTX-M-4;
DE            EC=3.5.2.6;
DE   AltName: Full=Cefotaximase 4;
DE   Flags: Precursor;
GN   Name=bla;
OS   Salmonella typhimurium.
OG   Plasmid pMSL.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-240.
RX   PubMed=9593162; DOI=10.1128/aac.42.5.1259;
RA   Gazouli M., Tzelepi E., Sidorenko S.V., Tzouvelekis L.S.;
RT   "Sequence of the gene encoding a plasmid-mediated cefotaxime-hydrolyzing
RT   class A beta-lactamase (CTX-M-4): involvement of serine 237 in
RT   cephalosporin hydrolysis.";
RL   Antimicrob. Agents Chemother. 42:1259-1262(1998).
RN   [2]
RP   MUTAGENESIS OF ARG-277.
RX   PubMed=9868772; DOI=10.1111/j.1574-6968.1998.tb13331.x;
RA   Gazouli M., Legakis N.J., Tzouvelekis L.S.;
RT   "Effect of substitution of Asn for Arg-276 in the cefotaxime-hydrolyzing
RT   class A beta-lactamase CTX-M-4.";
RL   FEMS Microbiol. Lett. 169:289-293(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; Y14156; CAA74573.1; -; Genomic_DNA.
DR   RefSeq; WP_032489025.1; NG_048990.1.
DR   AlphaFoldDB; O33807; -.
DR   SMR; O33807; -.
DR   KEGG; ag:CAA74573; -.
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; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..291
FT                   /note="Beta-lactamase CTX-M-4"
FT                   /id="PRO_0000016991"
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   MUTAGEN         240
FT                   /note="S->A: Causes minor alterations in the interaction of
FT                   with beta-lactams, reduces slightly the relative hydrolytic
FT                   activity against cefotaxime and the susceptibility to
FT                   inhibition by clavulanate."
FT                   /evidence="ECO:0000269|PubMed:9593162"
FT   MUTAGEN         277
FT                   /note="R->N: Confers lower levels of resistance to
FT                   cefotaxime, ceftriaxone and aztreonam while the levels of
FT                   resistance to penicillins and penicillin-inhibitor
FT                   combinations are similar. Slightly less susceptible to
FT                   inhibition by clavulanate and tazobactam. Cause a 3-fold
FT                   reduction in the relative rate of hydrolysis of
FT                   cefotaxime."
FT                   /evidence="ECO:0000269|PubMed:9868772"
SQ   SEQUENCE   291 AA;  31255 MW;  2E22E251008DF7C6 CRC64;
     MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV AQINTADNSQ
     ILYVADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI RASDLVNYNP IAEKHVNGTM
     TLAELGAGAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNSAIPGDP
     RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGMPK SWGVGDKTGS
     GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAESRRDIL AAAAKIVTHG F