ID   BLAC_STRCE              Reviewed;         311 AA.
AC   Q06650;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla;
OS   Streptomyces cellulosae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KCC S0127;
RX   PubMed=7916705; DOI=10.1016/0378-1119(93)90769-y;
RA   Ogawara H.;
RT   "Sequence of a gene encoding beta-lactamase from Streptomyces cellulosae.";
RL   Gene 124:111-114(1993).
CC   -!- FUNCTION: Hydrolyzes benzylpenicillin and cloxacillin (at 10% of the
CC       rate of benzylpenicillin).
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; D12653; BAA02176.1; -; Genomic_DNA.
DR   PIR; JN0520; JN0520.
DR   AlphaFoldDB; Q06650; -.
DR   SMR; Q06650; -.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; NADP; Signal.
FT   SIGNAL          1..36
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           37..311
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017015"
FT   ACT_SITE        86
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         252..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  33137 MW;  F3578EBEEA92A3FB CRC64;
     MRKPTSSLTR RSVLGAGLGL GGALALGSTT ASAASAGTTP SENPAAVRRL RALEREHQAR
     IGVFALNLAT GASLLHRAHE LFPMCSVFKT LAAAAVLRDL DHDGSQLARV IRYTEADVTK
     SGHAPVTKDH IDTGMTIRDL CDATIRYSDN CAANLLLREL GGPTAVTRFC RSLGDPVTRL
     DRWEPELNSG EPDRRTDTTS PYAIARTYQR LVLGNALNRP DRALLTDWLL RNTTTLTTFR
     TGLPKGWTVA DKSGGGDTYG TRNEAAIAWT PDGAPVLLTA LTHKPSLPTA PGDTPLIIKL
     ATVLSEAVAP A