ID   BLC4_PSEAI              Reviewed;         288 AA.
AC   Q51355;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Beta-lactamase CARB-4;
DE            EC=3.5.2.6;
DE   AltName: Full=Carbenicillinase 4;
DE   Flags: Precursor;
GN   Name=carB4;
OS   Pseudomonas aeruginosa.
OG   Plasmid pUD12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P83372; TRANSPOSON=Tn1413;
RX   PubMed=9687391; DOI=10.1128/aac.42.8.1966;
RA   Sanschagrin F., Bejaoui N., Levesque R.C.;
RT   "Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing beta-lactamases.";
RL   Antimicrob. Agents Chemother. 42:1966-1972(1998).
CC   -!- FUNCTION: Hydrolyzes carbenicillin. Methicillin and oxacillin are
CC       weakly hydrolyzed.
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 clavulanic acid and sulbactam.
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; U14749; AAC09012.1; -; Genomic_DNA.
DR   RefSeq; WP_032489168.1; NG_048742.1.
DR   AlphaFoldDB; Q51355; -.
DR   SMR; Q51355; -.
DR   KEGG; ag:AAC09012; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid; Signal;
KW   Transposable element.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..288
FT                   /note="Beta-lactamase CARB-4"
FT                   /id="PRO_0000017044"
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:0000255"
SQ   SEQUENCE   288 AA;  31490 MW;  19C068832675FD5E CRC64;
     MKLLLVFSLL IPSMVFANSS KFQQVEQDAK VIEASLSAHI GISVLDTQTG EYWDYNGNQR
     FPLTSTFKTI ACAKLLYDAE QGEINPKSTI EIKKADLVTY SPVIEKQVGQ AITLDDACFA
     TMTTSDNAAA NIILNALGGP ESVTDFLRQI GDKETRLDRI EPELNEGKLG DLRDTTTPNA
     IVNTLNELLF GSTLSQDGQK KLEYWMVNNQ VTGNLLRSVL PEGWNIADRS GAGGFGARSI
     TAVVWSEAQS PIIVSIYLAQ TEASIADRND AIVKIGRSIF EVYSSQSR