BLAC_AMYLA
ID BLAC_AMYLA Reviewed; 302 AA.
AC Q06316;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=bla;
OS Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=1913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LC411;
RX PubMed=8440253; DOI=10.1002/j.1460-2075.1993.tb05696.x;
RA Coque J.J.R., Liras P., Martin J.F.;
RT "Genes for a beta-lactamase, a penicillin-binding protein and a
RT transmembrane protein are clustered with the cephamycin biosynthetic genes
RT in Nocardia lactamdurans.";
RL EMBO J. 12:631-639(1993).
CC -!- FUNCTION: Active on penicillins but not on cephalosporins.
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}.
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DR EMBL; Z13971; CAA78373.1; -; Genomic_DNA.
DR PIR; S36188; S36188.
DR AlphaFoldDB; Q06316; -.
DR SMR; Q06316; -.
DR PRIDE; Q06316; -.
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 3: Inferred from homology;
KW Antibiotic resistance; Hydrolase; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..302
FT /note="Beta-lactamase"
FT /id="PRO_0000017006"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Increases nucleophilicity of active site Ser"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
SQ SEQUENCE 302 AA; 32084 MW; B7D6550AAE88B4F4 CRC64;
MADRRRVHAW ARARPAAPEP APPTPSAAAP SVAPGPAATP PDPAVEQEFT RLQTQYDARL
GLYAVDTGSG ESVAFRADER FAFASTFKAL AAAAVLDSTT PQQLDQVVRY SKDELLENSP
ITKDHVATGM TLRELCDAAV RFSDNTAGNL LLKHVGGPQG LDAALTAVGD EVTSADRWEP
ELNSAVPGDV RDTSTPRALA HDLRQFVLGD ALAEDDRALL TDWLRRNTTG GTVIRAGVPA
DWVVGDKTGS GYYGGRNDIA VLWPPNRAPI VMAVMTSREE PRAKRADALL ADAARVAVTA
LG