ID   BLAC_KITAU              Reviewed;         311 AA.
AC   P10509;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, 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   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Reynes J.-P., Drocourt D., Tiraby G.;
RL   Submitted (NOV-1988) to the EMBL/GenBank/DDBJ databases.
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; X13597; CAA31933.1; -; Genomic_DNA.
DR   PIR; S02714; S02714.
DR   AlphaFoldDB; P10509; -.
DR   SMR; P10509; -.
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; Signal.
FT   SIGNAL          1..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           35..311
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017013"
FT   ACT_SITE        87
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         255..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  32486 MW;  6FC8F4E5CD4C1DFA CRC64;
     MRLTQAPPSR RTLMTLGAGA TMAALLPAGG AAYASTSTAK APAAEGISGR LRALEKQYAA
     RLGVFALDTG TGAGRSYRAG ERFPMCSVFK ALAAAAVLRD VDARREFLTK RIHYTEKFVK
     DAGYIPVTGK PENIAGGMTG AELCAAAVSE SDNGAGNLLL RELDGPTGIT RFCRSLGDTT
     TRLDRWEPAL NSAEPDRVTD TTSPGAIGRT FGRLIVGSAL RAGDRKRLTG WLVANTTNRP
     TFRAGLPDDW VLADKTGGGE QYGVANDVGV VQPPGRAPLV LSVLSTKFDP KGPTDNPLVA
     KAAALVAGEL T