ID   BLAC_STRGR              Reviewed;          13 AA.
AC   P81173;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   12-AUG-2020, entry version 46.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   Flags: Fragment;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 23345 / DSM 40236 / JCM 4644 / NBRC 12875 / NCIMB 13023 / NRRL
RC   B-2682 / VKM Ac-800 / IMRU 3463;
RX   PubMed=9720038; DOI=10.1099/00221287-144-8-2169;
RA   Deak E., Szabo I., Kalmanczhelyi A., Gal Z., Barabas G., Panyige A.;
RT   "Membrane-bound and extracellular beta-lactamase production with
RT   developmental regulation in Streptomyces griseus NRRL B-2682.";
RL   Microbiology 144:2169-2177(1998).
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. Membrane.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Membrane;
KW   Secreted.
FT   CHAIN           1..>13
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000195442"
FT   NON_TER         13
SQ   SEQUENCE   13 AA;  1236 MW;  14C5129118D54760 CRC64;
     AAAPDIPIAN VNA