ID   BLAC_STRBA              Reviewed;         313 AA.
AC   P35391;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
OS   Streptomyces badius.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40139;
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M34178; AAA26707.1; -; Genomic_DNA.
DR   PIR; A45822; A45822.
DR   AlphaFoldDB; P35391; -.
DR   SMR; P35391; -.
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   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.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..313
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017014"
FT   REGION          28..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT   BINDING         256..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            96
FT                   /note="Increases nucleophilicity of active site Ser"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKD3"
SQ   SEQUENCE   313 AA;  33720 MW;  9C71C07DDC0EBF57 CRC64;
     MHHPRVRTAV AGLVAVLSLV PLAACGQSDS TAPPSSAKPA TSASASLPRP KPYTGDFKKL
     EREFDARLGV YAIDTGTGRE VTHNDRARFA YHSTFKALQA AVVLSTYSLD GLDKRVTYTR
     EDLVAHSPVT EKHVDTGMTL KELCDASVRY SDNTAANLLF DPRAAGPKGL DASLEKLGDD
     ITRMDREEPE LSRWVPGEKR DTSTPRALAE DLRAFVLGKA LRAPERAQLT TWLRTNTTGD
     AVIRAGVPEN WVVGDKTGTG SYYGARNDIA VVWPPDSAPI VIAILSHRGT KDAEPDDELI
     AEAASVVVDS LSS