ID   BLA1_BACCE              Reviewed;         306 AA.
AC   P10424;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=penPC;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 44-63.
RC   STRAIN=ATCC 13061 / DSM 6127 / NCIMB 8967 / NCTC 9946 / NRRL B-3537 / 5/B;
RX   PubMed=2991192; DOI=10.1128/jb.163.2.487-492.1985;
RA   Wang W., Mezes P.S.F., Yang Y.Q., Blacher R.W., Lampen J.O.;
RT   "Cloning and sequencing of the beta-lactamase I gene of Bacillus cereus 5/B
RT   and its expression in Bacillus subtilis.";
RL   J. Bacteriol. 163:487-492(1985).
CC   -!- FUNCTION: Acts preferentially on 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   -!- SUBCELLULAR LOCATION: Secreted.
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; M12607; AAA22668.1; -; Genomic_DNA.
DR   PIR; A23097; PNBS5B.
DR   AlphaFoldDB; P10424; -.
DR   SMR; P10424; -.
DR   STRING; 1396.DJ87_2341; -.
DR   DrugCentral; P10424; -.
DR   eggNOG; COG2367; Bacteria.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000269|PubMed:2991192"
FT   CHAIN           44..306
FT                   /note="Beta-lactamase 1"
FT                   /id="PRO_0000016971"
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;  33596 MW;  AD0FE16E435A4D12 CRC64;
     MKNKKMLKIG MCVGILGLSI TSLVTFTGGA LQVEAKEKTG QVKHKNQATH KEFSQLEKKF
     DARLGVYAID TGTNQTIAYR PNERFAFAST YKALAAGVLL QQNSTKKLDE VITYTKEDLV
     DYSPVTEKHV DTGMTLGEIA EAAVRYSDNT AGNILFHKIG GPKGYEKALR KMGDRVTMSD
     RFETELNEAI PGDIRDTSTA KAIARNLKDF TVGNALPHQK RNILTEWMKG NATGDKLIRA
     GVPTDWVDAD KSGAGSYGTR NDIAIVWPPN RSPIIIAILS SKDEKEATYD NQLIKEAAEV
     VIDAIK