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   27-MAR-2024, entry version 87.
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; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; 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   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; 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; 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
//