ID   BLP1_PSEAI              Reviewed;         288 AA.
AC   Q03170;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Beta-lactamase PSE-1;
DE            EC=3.5.2.6;
DE   AltName: Full=Beta-lactamase CARB-2;
DE   AltName: Full=Carbenicillinase 2;
DE   Flags: Precursor;
GN   Name=pse1 {ECO:0000303|PubMed:1804019}; Synonyms=carB2;
OS   Pseudomonas aeruginosa.
OG   Plasmid RPL11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=RPL11; TRANSPOSON=Tn1403;
RX   PubMed=1804019; DOI=10.1128/aac.35.11.2428;
RA   Huovinen P., Jacoby G.A.;
RT   "Sequence of the PSE-1 beta-lactamase gene.";
RL   Antimicrob. Agents Chemother. 35:2428-2430(1991).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND
RP   INDUCTION.
RC   PLASMID=RPL11;
RX   PubMed=410783; DOI=10.1128/jb.132.1.341-345.1977;
RA   Matthew M., Sykes R.B.;
RT   "Properties of the beta-lactamase specified by the Pseudomonas plasmid
RT   RPL11.";
RL   J. Bacteriol. 132:341-345(1977).
CC   -!- FUNCTION: Hydrolyzes penicillin, ampicillin and carbenicillin but not
CC       other antibiotics including oxacillin, methicillin and cloxacillin.
CC       {ECO:0000269|PubMed:410783}.
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   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate but not by
CC       cloxacillin. {ECO:0000269|PubMed:410783}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:410783}.
CC   -!- INDUCTION: Constitutive (at protein level).
CC       {ECO:0000269|PubMed:410783}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25740.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z18955; CAA79480.1; -; Genomic_DNA.
DR   EMBL; M69058; AAA25741.1; -; Genomic_DNA.
DR   EMBL; M69058; AAA25740.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001931474.1; NZ_RXTA01000067.1.
DR   AlphaFoldDB; Q03170; -.
DR   BMRB; Q03170; -.
DR   SMR; Q03170; -.
DR   GeneID; 72423020; -.
DR   KEGG; ag:AAA25741; -.
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; Disulfide bond; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..288
FT                   /note="Beta-lactamase PSE-1"
FT                   /id="PRO_0000017046"
FT   ACT_SITE        65
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         229..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..118
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  31348 MW;  BA618F058720F4C8 CRC64;
     MKFLLAFSLL IPSVVFASSS KFQQVEQDVK AIEVSLSARI GVSVLDTQNG EYWDYNGNQR
     FPLTSTFKTI ACAKLLYDAE QGKVNPNSTV EIKKADLVTY SPVIEKQVGQ AITLDDACFA
     TMTTSDNTAA NIILSAVGGP KGVTDFLRQI GDKETRLDRI EPDLNEGKLG DLRDTTTPKA
     IASTLNKFLF GSALSEMNQK KLESWMVNNQ VTGNLLRSVL PAGWNIADRS GAGGFGARSI
     TAVVWSEHQA PIIVSIYLAQ TQASMAERND AIVKIGHSIF DVYTSQSR
//