ID   BLAC_BACTU              Reviewed;         309 AA.
AC   Q45726;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla;
OS   Bacillus thuringiensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bt13;
RX   PubMed=7789815; DOI=10.1016/0378-1119(95)00089-o;
RA   Zhang M.-Y., Loevgren A.;
RT   "Cloning and sequencing of a beta-lactamase-encoding gene from the insect
RT   pathogen Bacillus thuringiensis.";
RL   Gene 158:83-86(1995).
CC   -!- FUNCTION: This protein is a beta-lactamase with a substrate specificity
CC       for penicillins.
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; X83424; CAA58448.1; -; Genomic_DNA.
DR   PIR; JC4117; JC4117.
DR   AlphaFoldDB; Q45726; -.
DR   SMR; Q45726; -.
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; Hydrolase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..309
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016976"
FT   ACT_SITE        92
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  33699 MW;  9C10BE11213237C1 CRC64;
     MMILKNKRML KIGICVGILG LSITSLEAFT GGALQVEAKQ KTGQVKHKNQ ATHKEFSQLE
     KKFDARVGVY AIDTGTNQTI SYRSNERFAF ASTYKALAAG VLLQQNSIDT LNEVITFTKE
     DLVDYSPVTE KHVDTGMKLG EIAEAAVRSS DNTAGNILFN KIGGPKGYEK ALRKMGDRVT
     MSDRFETELN EAIPGDIRDT STAKRIATNL KAFTVGNALP AEKRKILTEW MKGNATGDKL
     IRAGVPTDWV VGDKSGAGSY GTRNDIAIVW PPNRAPIIIA ILSSKDEKEA SYDNQLIAEA
     TEVIVKALK