TORR_ECOLI
ID TORR_ECOLI Reviewed; 230 AA.
AC P38684; P77344;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=TorCAD operon transcriptional regulatory protein TorR;
GN Name=torR; OrderedLocusNames=b0995, JW0980;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8083154; DOI=10.1128/jb.176.18.5601-5606.1994;
RA Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.;
RT "The torR gene of Escherichia coli encodes a response regulator protein
RT involved in the expression of the trimethylamine N-oxide reductase genes.";
RL J. Bacteriol. 176:5601-5606(1994).
RN [2]
RP ERRATUM OF PUBMED:8083154.
RX PubMed=7798146; DOI=10.1128/jb.177.1.275-275.1995;
RA Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.;
RL J. Bacteriol. 177:275-275(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [5]
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 [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8596446; DOI=10.1111/j.1365-2958.1995.mmi_17050971.x;
RA Simon G., Jourlin C., Ansaldi M., Pascal M.-C., Chippaux M., Mejean V.;
RT "Binding of the TorR regulator to cis-acting direct repeats activates tor
RT operon expression.";
RL Mol. Microbiol. 17:971-980(1995).
RN [7]
RP MUTAGENESIS OF ASP-53.
RX PubMed=9135110; DOI=10.1006/jmbi.1997.0919;
RA Jourlin C., Ansaldi M., Mejean V.;
RT "Transphosphorylation of the TorR response regulator requires the three
RT phosphorylation sites of the TorS unorthodox sensor in Escherichia coli.";
RL J. Mol. Biol. 267:770-777(1997).
RN [8]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10648521; DOI=10.1128/jb.182.4.961-966.2000;
RA Ansaldi M., Simon G., Lepelletier M., Mejean V.;
RT "The TorR high-affinity binding site plays a key role in both torR
RT autoregulation and torCAD operon expression in Escherichia coli.";
RL J. Bacteriol. 182:961-966(2000).
RN [9]
RP INTERACTION WITH TORI.
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).
CC -!- FUNCTION: Member of the two-component regulatory system TorS/TorR
CC involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO).
CC Phosphorylated TorR activates the transcription of the torCAD operon by
CC binding to four decameric boxes located in the torCAD promoter. Box1, 2
CC and 4 contain the DNA sequence 5'-CTGTTCATAT-3' and box3 contains the
CC DNA sequence 5'-CCGTTCATCC-3'. Phosphorylated as well as
CC unphosphorylated TorR negatively regulates its own expression by
CC binding to box1 and 2.
CC -!- SUBUNIT: Interacts with TorI. TorI binds to the effector domain of
CC TorR. This interaction, which does not interfere with TorR DNA binding
CC activity, probably prevents the recruitment of RNA polymerase to the
CC torCAD promoter. {ECO:0000269|PubMed:15197250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated and dephosphorylated by TorS.
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DR EMBL; X94231; CAA63922.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74080.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36137.1; -; Genomic_DNA.
DR PIR; A64841; A64841.
DR RefSeq; NP_415515.1; NC_000913.3.
DR RefSeq; WP_001120125.1; NZ_SSZK01000002.1.
DR PDB; 1ZGZ; X-ray; 1.80 A; A/B/C/D=1-122.
DR PDBsum; 1ZGZ; -.
DR AlphaFoldDB; P38684; -.
DR SMR; P38684; -.
DR BioGRID; 4261488; 9.
DR BioGRID; 850542; 1.
DR DIP; DIP-11016N; -.
DR IntAct; P38684; 4.
DR STRING; 511145.b0995; -.
DR iPTMnet; P38684; -.
DR jPOST; P38684; -.
DR PaxDb; P38684; -.
DR PRIDE; P38684; -.
DR EnsemblBacteria; AAC74080; AAC74080; b0995.
DR EnsemblBacteria; BAA36137; BAA36137; BAA36137.
DR GeneID; 946182; -.
DR KEGG; ecj:JW0980; -.
DR KEGG; eco:b0995; -.
DR PATRIC; fig|1411691.4.peg.1276; -.
DR EchoBASE; EB2499; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_6; -.
DR InParanoid; P38684; -.
DR OMA; EMGSDDY; -.
DR PhylomeDB; P38684; -.
DR BioCyc; EcoCyc:TORR-MON; -.
DR EvolutionaryTrace; P38684; -.
DR PRO; PR:P38684; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..230
FT /note="TorCAD operon transcriptional regulatory protein
FT TorR"
FT /id="PRO_0000081255"
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 132..227
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000305"
FT MUTAGEN 53
FT /note="D->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:9135110"
FT CONFLICT 134
FT /note="C -> L (in Ref. 1; CAA63922)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1ZGZ"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:1ZGZ"
SQ SEQUENCE 230 AA; 26233 MW; D1936404503FBA09 CRC64;
MPHHIVIVED EPVTQARLQS YFTQEGYTVS VTASGAGLRE IMQNQSVDLI LLDINLPDEN
GLMLTRALRE RSTVGIILVT GRSDRIDRIV GLEMGADDYV TKPLELRELV VRVKNLLWRI
DLARQAQPHT QDNCYRFAGY CLNVSRHTLE RDGEPIKLTR AEYEMLVAFV TNPGEILSRE
RLLRMLSARR VENPDLRTVD VLIRRLRHKL SADLLVTQHG EGYFLAADVC
