ID   BLA1_BACMY              Reviewed;         306 AA.
AC   P28018;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Beta-lactamase 1;
DE            EC=3.5.2.6;
DE   AltName: Full=Beta-lactamase I;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=blaCI;
OS   Bacillus mycoides.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NI10R;
RA   Groenstad A., Kristensen T., Hornes E., Kolstoe A.-B.;
RT   "The beta-lactamase I gene From Bacillus mycoides.";
RL   Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
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; X62244; CAA44161.1; -; Genomic_DNA.
DR   PIR; S17339; S17339.
DR   AlphaFoldDB; P28018; -.
DR   SMR; P28018; -.
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..43
FT                   /evidence="ECO:0000250"
FT   CHAIN           44..306
FT                   /note="Beta-lactamase 1"
FT                   /id="PRO_0000016972"
FT   ACT_SITE        89
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         251..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  33383 MW;  849BB01FD499E3BB CRC64;
     MKNKRMLKIG MCVGILGLSV TSLEAFTGGA LQVEAKEKTG QVKHKNQATH KEFSQLEKKF
     DARLGVYAID TGTNQTISYR HNERFAFAST YKALAAGVLL QQNSIDTLNE VIKFTKEDLV
     DYSPVTEKHV DTGMKLGEIA EAAVRSSDNT AGNILFHKIG GPKGYEKALR QIGDRVTMSD
     RFETELNEAI PGDIRDTSTA KAIASNLKAF TVGNALPAEK RKILTEWMKG NATGDKLIRA
     GVPTDWIVGD KSGAGSYGTR NDIAIVWPPN RAPIIIAILS SKDEKEATYD NQLIAEAPEV
     IVKSLK