ID   BLAC_PROMI              Reviewed;         298 AA.
AC   P30897;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Carbenicillinase;
DE   Flags: Precursor;
GN   Name=blaP;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-37.
RC   STRAIN=GN79;
RX   PubMed=1840585; DOI=10.1128/jb.173.21.7038-7041.1991;
RA   Sakurai Y., Tsukamoto K., Sawai T.;
RT   "Nucleotide sequence and characterization of a carbenicillin-hydrolyzing
RT   penicillinase gene from Proteus mirabilis.";
RL   J. Bacteriol. 173:7038-7041(1991).
CC   -!- FUNCTION: Hydrolyzes carbenicillin.
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; D13209; BAA02496.1; -; Genomic_DNA.
DR   PIR; A41381; A41381.
DR   AlphaFoldDB; P30897; -.
DR   SMR; P30897; -.
DR   BindingDB; P30897; -.
DR   ChEMBL; CHEMBL5744; -.
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; Disulfide bond;
KW   Hydrolase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..298
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017007"
FT   ACT_SITE        72
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..126
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  32765 MW;  A3710003B728BD5F CRC64;
     MNVRQHKASF FSVVITFLCL TLSLNANATD SVLEAVTNAE TELGARIGLA AHDLETGKRW
     EHKSNERFPL SSTFKTLACA NVLQRVDLGK ERIDRVVRFS ESNLVTYSPV TEKHVGKKGM
     SLAELCQATL STSDNSAANF ILQAIGGPKA LTKFLRSIGD DTTRLDRWEP ELNEAVPGDK
     RDTTTPIAMV TTLEKLLIDE TLSIKSRQQL ESWLKGNEVG DALFRKGVPS DWIVADRTGA
     GGYGSRAITA VMWPPNRKPI VAALYITETD ASFEERNAVI AKIGEQIAKT VLMENSRN