BLAC_CITKO
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 03-AUG-2022, entry version 84.
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; Proteobacteria; 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}.
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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; -; 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; 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