ID   BLAC_STRLA              Reviewed;         305 AA.
AC   P35393;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
OS   Streptomyces lavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8664 / DSM 40213 / JCM 4055 / KCC S-0055 / NBRC 12789 /
RC   NCIMB 9840;
RX   PubMed=2391494; DOI=10.1099/00221287-136-3-589;
RA   Forsman M., Haeggstroem B., Lindgren L., Jaurin B.;
RT   "Molecular analysis of beta-lactamases from four species of Streptomyces:
RT   comparison of amino acid sequences with those of other beta-lactamases.";
RL   J. Gen. Microbiol. 136:589-598(1990).
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; M34180; AAA26708.1; -; Genomic_DNA.
DR   PIR; C45822; C45822.
DR   AlphaFoldDB; P35393; -.
DR   SMR; P35393; -.
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   InterPro; IPR006311; TAT_signal.
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.
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..305
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017019"
FT   ACT_SITE        82
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         250..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  32354 MW;  7F29DA5436650647 CRC64;
     MGTTGARPSR RAVLTAAAGA AVAGIPLGGS TAFAAPRGNP DVLRQLRALE QEHSARLGVY
     ARDTATGRTV LHRAEERFPM CSVFKTLAVA AVLRDLDRDG EFLATRLFYT EQEVKDSGFG
     PVTGLPENLA AGMTVERLCA AAICQSDNAA ANLLLRELGG PEAVTRFCRS VGDRTTRLDR
     WEPELNSAEP GRLTDTTTPR AIGATYGELV LGDALAPRDR ERLTGWLLAN TTSTERFRKG
     LPADWTLGDK TGGGAYGTNN DAGVTWPPHR PPVVMVVLTT HDRPDAVADN PLVAKTAALL
     ASALG
//