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 27-MAR-2024, entry version 86. 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; Pseudomonadota; 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}. 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; 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; 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 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 //