TORI_ECOLI
ID TORI_ECOLI Reviewed; 66 AA.
AC Q2EES9; Q2MAK2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Response regulator inhibitor for tor operon;
DE Short=Tor inhibitor;
GN Name=torI; OrderedLocusNames=b4501, JW5387;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION IN TOR OPERON REGULATION, AND INTERACTION WITH TORR.
RX PubMed=15197250; DOI=10.1073/pnas.0401927101;
RA Ansaldi M., Theraulaz L., Mejean V.;
RT "TorI, a response regulator inhibitor of phage origin in Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9423-9428(2004).
RN [4]
RP STRUCTURE BY NMR, FUNCTION AS AN EXCISIONASE, AND MUTAGENESIS OF TYR-28 AND
RP ARG-45.
RX PubMed=16079126; DOI=10.1074/jbc.m507409200;
RA Elantak L., Ansaldi M., Guerlesquin F., Mejean V., Morelli X.;
RT "Structural and genetic analyses reveal a key role in prophage excision for
RT the TorI response regulator inhibitor.";
RL J. Biol. Chem. 280:36802-36808(2005).
CC -!- FUNCTION: Transcription inhibitory protein for the torCAD operon. Also
CC acts as an excisionase and plays an essential role in the defective
CC prophage CPS53 excision. {ECO:0000269|PubMed:15197250,
CC ECO:0000269|PubMed:16079126}.
CC -!- SUBUNIT: Interacts with TorR. Binds to the effector domain of TorR.
CC This interaction, which does not interfere with TorR DNA binding
CC activity, probably prevents the recruitment of RNA polymerase to the
CC torCAD promoter. Binds to DNA. {ECO:0000269|PubMed:15197250}.
CC -!- INTERACTION:
CC Q2EES9; P76502: sixA; NbExp=3; IntAct=EBI-9154838, EBI-548621;
CC -!- SIMILARITY: Belongs to the phage AlpA excisionase family.
CC {ECO:0000305}.
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DR EMBL; U00096; ABD18695.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76704.1; -; Genomic_DNA.
DR RefSeq; WP_001163428.1; NZ_SSUV01000027.1.
DR RefSeq; YP_588463.1; NC_000913.3.
DR PDB; 1Z4H; NMR; -; A=1-66.
DR PDBsum; 1Z4H; -.
DR AlphaFoldDB; Q2EES9; -.
DR BMRB; Q2EES9; -.
DR SMR; Q2EES9; -.
DR BioGRID; 4260552; 15.
DR BioGRID; 853375; 1.
DR IntAct; Q2EES9; 1.
DR STRING; 511145.b4501; -.
DR PaxDb; Q2EES9; -.
DR PRIDE; Q2EES9; -.
DR EnsemblBacteria; ABD18695; ABD18695; b4501.
DR EnsemblBacteria; BAE76704; BAE76704; BAE76704.
DR GeneID; 1450232; -.
DR GeneID; 60669294; -.
DR KEGG; ecj:JW5387; -.
DR KEGG; eco:b4501; -.
DR PATRIC; fig|1411691.4.peg.4366; -.
DR eggNOG; COG3311; Bacteria.
DR HOGENOM; CLU_140176_22_2_6; -.
DR OMA; CAFKSKL; -.
DR BioCyc; EcoCyc:MON0-1641; -.
DR EvolutionaryTrace; Q2EES9; -.
DR PRO; PR:Q2EES9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0044349; P:DNA excision; IMP:EcoCyc.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
PE 1: Evidence at protein level;
KW 3D-structure; DNA recombination; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..66
FT /note="Response regulator inhibitor for tor operon"
FT /id="PRO_0000252144"
FT MUTAGEN 28
FT /note="Y->F,S: Loss of all excisionase activity."
FT /evidence="ECO:0000269|PubMed:16079126"
FT MUTAGEN 45
FT /note="R->K,Q: Retains approximately 10% excisionase
FT activity."
FT /evidence="ECO:0000269|PubMed:16079126"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1Z4H"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:1Z4H"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1Z4H"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1Z4H"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1Z4H"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:1Z4H"
SQ SEQUENCE 66 AA; 7678 MW; 587B519EF433DC5B CRC64;
MQHELQPDSL VDLKFIMADT GFGKTFIYDR IKSGDLPKAK VIHGRARWLY RDHCEFKNKL
LSRANG
