ID   BLA2_STRCI              Reviewed;         314 AA.
AC   P14560;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Beta-lactamase 2;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=blaU;
OS   Streptomyces cacaoi.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 3082 / DSM 40057 / JCM 4352 / KCC S-0352 / NBRC 12748 / NCIMB
RC   9626 / IMRU 3082;
RX   PubMed=2559297; DOI=10.1111/j.1365-2958.1989.tb00125.x;
RA   Forsman M., Lindgren L., Haeggstroem B., Jaurin B.;
RT   "Transcriptional induction of Streptomyces cacaoi beta-lactamase by a beta-
RT   lactam compound.";
RL   Mol. Microbiol. 3:1425-1432(1989).
RN   [2]
RP   COMPARISON OF BLAU AND BLAL.
RX   PubMed=1468613; DOI=10.1016/0378-1097(92)90295-y;
RA   Magdalena J., Forsman M., Lenzini M.V., Brans A., Dusart J.;
RT   "Two different beta-lactamase genes are present in Streptomyces cacaoi.";
RL   FEMS Microbiol. Lett. 78:101-105(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15708; CAA33739.1; -; Genomic_DNA.
DR   PIR; S06967; S06967.
DR   AlphaFoldDB; P14560; -.
DR   SMR; P14560; -.
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   CHAIN           27..314
FT                   /note="Beta-lactamase 2"
FT                   /id="PRO_0000017017"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        96
FT                   /note="Acyl-ester intermediate"
FT   BINDING         258..260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34023 MW;  F895674E3B22ACD3 CRC64;
     MLHTRIRRAT LGAVAALSLV PVMACGQESS ADAAEPAGSA PSSSAAAHKP GEVEPYAAEL
     KALEDEFDVR LGVYAVDTGS GREVAYRDGE RFPYNSTFKA LECGAVLDKH TDREMDRVVK
     YSEDDLVDNS PVTEKHVEDG MTLTALCDAA VRYSDNTAAN LLFETVGGPK GLDKTLEGLG
     DHVTRMERVE PFLSRWEPGS KRDTSTPRAF AKDLRAYVLG DVLAEGDRKQ LTTWLRNNTT
     GDGLIRAGVR QGWVVGDKTG TGSYYGARND MAVVWRPDGR PLVLNVMVHG HTKDAELDSE
     LIARATEVVA DRLG