BLAI_BACLI
ID BLAI_BACLI Reviewed; 128 AA.
AC P06555; P12286;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Penicillinase repressor;
DE AltName: Full=Beta-lactamase repressor protein;
DE AltName: Full=Regulatory protein BlaI;
GN Name=blaI; Synonyms=penI;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3096969; DOI=10.1128/jb.168.3.1128-1132.1986;
RA Himeno T., Imanaka T., Aiba S.;
RT "Nucleotide sequence of the penicillinase repressor gene penI of Bacillus
RT licheniformis and regulation of penP and penI by the repressor.";
RL J. Bacteriol. 168:1128-1132(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3305074; DOI=10.1016/0014-5793(87)80375-7;
RA Nicholls N.J., Lampen J.O.;
RT "Repressor gene, blaI, for Bacillus licheniformis 749 beta-lactamase.";
RL FEBS Lett. 221:179-183(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3260234; DOI=10.1128/jb.170.7.3206-3212.1988;
RA Wittman V., Wong H.C.;
RT "Regulation of the penicillinase genes of Bacillus licheniformis:
RT interaction of the pen repressor with its operators.";
RL J. Bacteriol. 170:3206-3212(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-128.
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3040663; DOI=10.1128/jb.169.9.3873-3878.1987;
RA Kobayashi T., Zhu Y.F., Nicholls N.J., Lampen J.O.;
RT "A second regulatory gene, blaR1, encoding a potential penicillin-binding
RT protein required for induction of beta-lactamase in Bacillus
RT licheniformis.";
RL J. Bacteriol. 169:3873-3878(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=3498148; DOI=10.1093/nar/15.15.6049;
RA Grossman M.J., Lampen J.O.;
RT "Purification and DNA binding properties of the blaI gene product,
RT repressor for the beta-lactamase gene, blaP, of Bacillus licheniformis.";
RL Nucleic Acids Res. 15:6049-6062(1987).
RN [6]
RP STRUCTURE BY NMR OF 1-82, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH DNA.
RX PubMed=14568532; DOI=10.1016/j.jmb.2003.09.005;
RA Melckebeke H.V., Vreuls C., Gans P., Filee P., Llabres G., Joris B.,
RA Simorre J.-P.;
RT "Solution structural study of BlaI: implications for the repression of
RT genes involved in beta-lactam antibiotic resistance.";
RL J. Mol. Biol. 333:711-720(2003).
RN [7]
RP STRUCTURE BY NMR OF 1-82, SUBUNIT, AND INTERACTION WITH DNA.
RX PubMed=17576674; DOI=10.1093/nar/gkm448;
RA Boudet J., Duval V., Van Melckebeke H., Blackledge M., Amoroso A.,
RA Joris B., Simorre J.-P.;
RT "Conformational and thermodynamic changes of the repressor/DNA operator
RT complex upon monomerization shed new light on regulation mechanisms of
RT bacterial resistance against beta-lactam antibiotics.";
RL Nucleic Acids Res. 35:4384-4395(2007).
CC -!- FUNCTION: Transcriptional repressor that constitutively blocks
CC expression of beta-lactamase. Regulates genes involved in antibiotic
CC resistance. Binds DNA as a dimer.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17576674}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Upon exposure to beta-lactams, proteolytic cleavage at a single
CC site may impair dimerization and abolish repressor activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BlaI transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; M14734; AAA22648.1; -; Genomic_DNA.
DR EMBL; M21337; AAA22650.1; -; Genomic_DNA.
DR EMBL; X05798; CAA29242.1; -; Genomic_DNA.
DR EMBL; M17368; AAA22272.1; -; Genomic_DNA.
DR PIR; B28183; B28183.
DR PIR; S00093; RGBSBI.
DR PDB; 1P6R; NMR; -; A=1-82.
DR PDB; 2P7C; NMR; -; B=1-82.
DR PDBsum; 1P6R; -.
DR PDBsum; 2P7C; -.
DR AlphaFoldDB; P06555; -.
DR BMRB; P06555; -.
DR SMR; P06555; -.
DR PATRIC; fig|1402.64.peg.4007; -.
DR EvolutionaryTrace; P06555; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005650; BlaI_family.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34134; PTHR34134; 1.
DR Pfam; PF03965; Penicillinase_R; 1.
DR PIRSF; PIRSF019455; CopR_AtkY; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..128
FT /note="Penicillinase repressor"
FT /id="PRO_0000062792"
FT DNA_BIND 6..70
FT /note="H-T-H motif"
FT REGION 73..128
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT SITE 100..101
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="S -> P (in Ref. 3; AAA22650)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..98
FT /note="MV -> IL (in Ref. 3; AAA22650)"
FT /evidence="ECO:0000305"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1P6R"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1P6R"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:1P6R"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1P6R"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1P6R"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1P6R"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1P6R"
SQ SEQUENCE 128 AA; 15034 MW; BC8305AF72E7CB8B CRC64;
MKKIPQISDA ELEVMKVIWK HSSINTNEVI KELSKTSTWS PKTIQTMLLR LIKKGALNHH
KEGRVFVYTP NIDESDYIEV KSHSFLNRFY NGTLNSMVLN FLENDQLSGE EINELYQILE
EHKNRKKE
