BLP1_PSEAI
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 03-AUG-2022, entry version 95.
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; Proteobacteria; 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 PRIDE; Q03170; -.
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; -; 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; 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
