ID   BLAC_BACCE              Reviewed;         306 AA.
AC   P00809; P70876;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=blaY;
OS   Bacillus cereus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=569/H / NCTC 9945;
RX   PubMed=6308567; DOI=10.1093/nar/11.14.4997;
RA   Sloma A., Gross M.;
RT   "Molecular cloning and nucleotide sequence of the type I beta-lactamase
RT   gene from Bacillus cereus.";
RL   Nucleic Acids Res. 11:4997-5004(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=569/H/9;
RX   PubMed=3124817; DOI=10.1042/bj2480657;
RA   Madgwick P.J., Waley S.G.;
RT   "Beta-lactamase I from Bacillus cereus. Structure and site-directed
RT   mutagenesis.";
RL   Biochem. J. 248:657-662(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-75.
RC   STRAIN=569/H / NCTC 9945;
RX   PubMed=6413253; DOI=10.1016/0014-5793(83)81006-0;
RA   Mezes P.S.F., Yang Y.Q., Hussain M., Lampen J.O.;
RT   "Bacillus cereus 569/H beta-lactamase I: cloning in Escherichia coli and
RT   signal sequence determination.";
RL   FEBS Lett. 161:195-200(1983).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA29819.1; Type=Erroneous initiation; Evidence={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; X01990; CAA26021.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X01602; CAA25753.1; -; Genomic_DNA.
DR   EMBL; X06599; CAA29819.1; ALT_INIT; Genomic_DNA.
DR   PIR; A01004; PNBSU.
DR   RefSeq; WP_063842248.1; NG_047482.1.
DR   AlphaFoldDB; P00809; -.
DR   SMR; P00809; -.
DR   BindingDB; P00809; -.
DR   ChEMBL; CHEMBL5732; -.
DR   DrugCentral; P00809; -.
DR   SABIO-RK; P00809; -.
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; DD-peptidase/beta-lactamase superfamily; 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; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..306
FT                   /note="Beta-lactamase 1"
FT                   /id="PRO_0000016970"
FT   ACT_SITE        91
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         253..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        273
FT                   /note="S -> R (in Ref. 2; CAA29819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278..280
FT                   /note="VLI -> IAIL (in Ref. 2; CAA29819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291..292
FT                   /note="ND -> DN (in Ref. 2; CAA29819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305..306
FT                   /note="GS -> ALR (in Ref. 2; CAA29819)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  33322 MW;  F00F4DB9DB6D41AA CRC64;
     MILKNKRMLK IGICVGILGL SITSLEAFTG ESLQVEAKEK TGQVKHKNQA THKEFSQLEK
     KFDARLGVYA IDTGTNQTIS YRPNERFAFA STYKALAAGV LLQQNSIDSL NEVITYTKED
     LVDYSPVTEK HVDTGMKLGE IAEAAVRSSD NTAGNILFNK IGGPKGYEKA LRHMGDRITM
     SNRFETELNE AIPGDIRDTS TAKAIATNLK AFTVGNALPA EKRKILTEWM KGNATGDKLI
     RAGIPTDWVV GDKSGAGSYG TRNDIAVVWP PNSAPIIVLI SSKDEKEAIY NDQLIAEATK
     VIVKGS
//