ID BLAC_CITKO Reviewed; 294 AA. AC P22390; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 27-MAR-2024, entry version 88. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Penicillinase; DE Flags: Precursor; OS Citrobacter koseri (Citrobacter diversus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=545; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ULA-27; RX PubMed=1778425; DOI=10.1016/0378-1097(91)90448-j; RA Perilli M., Franceschini N., Segatore B., Amicosante G., Oratore A., RA Duez C., Joris B., Frere J.-M.; RT "Cloning and nucleotide sequencing of the gene encoding the beta-lactamase RT from Citrobacter diversus."; RL FEMS Microbiol. Lett. 67:79-84(1991). RN [2] RP PROTEIN SEQUENCE OF 28-83. RC STRAIN=ULA-27; RX PubMed=2039443; DOI=10.1042/bj2750629; RA Franceschini N., Amicosante G., Perilli M., Maccarrone M., Oratore A., RA van Beeumen J., Frere J.-M.; RT "Proteolytic interconversion and N-terminal sequences of the Citrobacter RT diversus major beta-lactamases."; RL Biochem. J. 275:629-633(1991). RN [3] RP PROTEIN SEQUENCE OF 72-79. RX PubMed=2848500; DOI=10.1042/bj2540891; RA Amicosante G., Oratore A., Joris B., Galleni M., Frere J.-M., RA van Beeumen J.; RT "Chromosome-encoded beta-lactamases of Citrobacter diversus. Interaction RT with beta-iodopenicillanate and labelling of the active site."; RL Biochem. J. 254:891-893(1988). 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; X62610; CAA44485.1; -; Genomic_DNA. DR PIR; S19006; S19006. DR AlphaFoldDB; P22390; -. DR SMR; P22390; -. DR SABIO-RK; P22390; -. 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; Direct protein sequencing; Hydrolase; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:2039443" FT CHAIN 28..294 FT /note="Beta-lactamase" FT /id="PRO_0000016977" FT ACT_SITE 76 FT /note="Acyl-ester intermediate" FT ACT_SITE 174 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 240..242 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CONFLICT 28 FT /note="R -> G (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="R -> S (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 80..83 FT /note="TMVA -> AMAT (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 294 AA; 31862 MW; BF075822858C54BB CRC64; MFKKRGRQTV LIAAVLAFFT ASSPLLARTQ GEPTQVQQKL AALEKQSGGR LGVALINTAD RSQILYRGDE RFAMCSTSKT MVAAAVLKQS ETQHDILQQK MVIKKADLTN WNPVTEKYVD KEMTLAELSA ATLQYSDNTA MNKLLEHLGG TSNVTAFARS IGDTTFRLDR KEPELNTAIP GDERDTTCPL AMAKSLHKLT LGDALAGAQR AQLVEWLKGN TTGGQSIRAG LPEGWVVGDK TGAGDYGTTN DIAVIWPEDR APLILVTYFT QPQQDAKGRK DILAAAAKIV TEGL //