BLAC_BACAM
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 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=penP;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; 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; -; 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..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