ID   BLAC_BACAM              Reviewed;         306 AA.
AC   Q44674;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=penP;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   van Dijl J.M., de Jong A., Nauta A., Venema G., Bron S.;
RT   "Identification of penicillinase-encoding genes of Bacillus
RT   amyloliquefaciens and Bacillus subtilis.";
RL   Submitted (AUG-1994) 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; Z35653; CAA84712.1; -; Genomic_DNA.
DR   PIR; S47330; S47330.
DR   AlphaFoldDB; Q44674; -.
DR   SMR; Q44674; -.
DR   STRING; 692420.BAMF_1288; -.
DR   eggNOG; COG2367; Bacteria.
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..34
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..306
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016969"
FT   ACT_SITE        89
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         251..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  33409 MW;  BEC57A283995E415 CRC64;
     MNVKRKATLK FGICIGLLCV SFTGFNSLFG STHAEAKSIE NTKMTSCITN QKFVQLEKKF
     DARLGVYAID TGSNKTIAYR PNERFAYAST YKVLAAAAVL KQKPIEKLND VIRYTKEDLV
     TYSPITEKHL DTGMSLKEIS EAAIRYSDNT AGNILLQQLG GPKGFEKSLK QIGDHVTKAD
     RFETDLNSAI PGDIRDTSTA KALATDLKAF TLGNTLTTDK RTILTDWMRG NATGDELIRA
     GAPAGWEVGD KSGAGSYGTR NDIAIVWPPD RAPIVLAILT KRFTKDAEYD NALIAEAAKV
     ALDDLK
//