ID   PENA_BURM1              Reviewed;         313 AA.
AC   Q02940;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=penA;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 17616 / 249;
RX   PubMed=8494361; DOI=10.1128/aac.37.4.667;
RA   Proenca R., Niu W.W., Cacalano G., Prince A.;
RT   "The Pseudomonas cepacia 249 chromosomal penicillinase is a member of the
RT   AmpC family of chromosomal beta-lactamases.";
RL   Antimicrob. Agents Chemother. 37:667-674(1993).
RN   [2]
RP   COMMENT ON SEQUENCE.
RX   PubMed=7514860; DOI=10.1128/aac.38.2.407;
RA   Joris B., Galleni M., Frere J.M., Labia R.;
RT   "Analysis of the penA gene of Pseudomonas cepacia 249.";
RL   Antimicrob. Agents Chemother. 38:407-408(1994).
CC   -!- FUNCTION: Upon expression in E.coli enables the latter to utilize
CC       penicillin as a carbon source. {ECO:0000305|PubMed:8494361}.
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:PRU10102};
CC   -!- INDUCTION: By penicillin G, impenem and AmpR.
CC       {ECO:0000269|PubMed:8494361}.
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This protein could be artifactual, it seems to contain pieces
CC       of several different proteins. {ECO:0000305|PubMed:7514860}.
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DR   EMBL; L02928; AAA25927.1; -; Genomic_DNA.
DR   PIR; A48903; A48903.
DR   AlphaFoldDB; Q02940; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..15
FT   CHAIN           16..313
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016967"
FT   ACT_SITE        190
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
SQ   SEQUENCE   313 AA;  34328 MW;  BF2A67C670A644F2 CRC64;
     MQRIGVTDYT ILGTVKGAEL ELVRFTHPFM GFDVPAILGD HVTRMPVPVP FTPRLPRPGR
     LCDRSEIRPG KPLTRLARTA LICRALIRRW MARTSYSDSV NCHTQPISAI FDYKDLRFEP
     PSNRISPAGQ TSVDRLLQLS QGQAVEGQSA VARLTGEKKN HPGAQYANRL SPRIANNHPA
     TQQTLFELGS GAKERNAINV SYLTALGTPG FTLMLPARML CGIVSDNNFT QKQLCPSPAR
     CTRGPAEPAK RGPWLEPGLV IRKDGLRTGK LLSSLRGLCL TVLRFQPTVP CFCRLALSSS
     VAISSTGLVN FSR