Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

HTH-type transcriptional activator RhaR

Gene

rhaR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Activates expression of the rhaSR operon in response to L-rhamnose.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi195 – 21420H-T-H motifBy similarityAdd
BLAST
DNA bindingi244 – 26724H-T-H motifBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Rhamnose metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00222.
ECOL316407:JW3877-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional activator RhaR
Alternative name(s):
L-rhamnose operon transcriptional activator RhaR
Gene namesi
Name:rhaR
Synonyms:rhaC1
Ordered Locus Names:b3906, JW3877
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10842. rhaR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282HTH-type transcriptional activator RhaRPRO_0000194551Add
BLAST

Proteomic databases

PaxDbiP09378.

Expressioni

Inductioni

Autoregulated. Binding of the cAMP receptor protein (CRP) is required for full expression.1 Publication

Interactioni

Subunit structurei

Binds DNA as a dimer.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei246 – 2461Interaction with sigma-70

Protein-protein interaction databases

BioGridi4263058. 8 interactions.
DIPiDIP-10693N.
IntActiP09378. 9 interactions.
STRINGi511145.b3906.

Structurei

3D structure databases

ProteinModelPortaliP09378.
SMRiP09378. Positions 191-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108BRW. Bacteria.
ENOG410XYX0. LUCA.
HOGENOMiHOG000290513.
InParanoidiP09378.
KOiK02854.
OMAiFALDEFC.
OrthoDBiEOG6Z3KH4.
PhylomeDBiP09378.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
2.60.120.280. 1 hit.
HAMAPiMF_01533. HTH_type_RhaR.
InterProiIPR003313. AraC-bd.
IPR009057. Homeodomain-like.
IPR018060. HTH_AraC.
IPR018062. HTH_AraC-typ_CS.
IPR011051. RmlC_Cupin.
IPR023699. Tscrpt_act_RhaR.
IPR020449. Tscrpt_reg_HTH_AraC-type.
[Graphical view]
PfamiPF02311. AraC_binding. 1 hit.
PF12833. HTH_18. 1 hit.
[Graphical view]
PRINTSiPR00032. HTHARAC.
SMARTiSM00342. HTH_ARAC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF51182. SSF51182. 1 hit.
PROSITEiPS00041. HTH_ARAC_FAMILY_1. 1 hit.
PS01124. HTH_ARAC_FAMILY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHQLKLLKD DFFASDQQAV AVADRYPQDV FAEHTHDFCE LVIVWRGNGL
60 70 80 90 100
HVLNDRPYRI TRGDLFYIHA DDKHSYASVN DLVLQNIIYC PERLKLNLDW
110 120 130 140 150
QGAIPGFNAS AGQPHWRLGS MGMAQARQVI GQLEHESSQH VPFANEMAEL
160 170 180 190 200
LFGQLVMLLN RHRYTSDSLP PTSSETLLDK LITRLAASLK SPFALDKFCD
210 220 230 240 250
EASCSERVLR QQFRQQTGMT INQYLRQVRV CHAQYLLQHS RLLISDISTE
260 270 280
CGFEDSNYFS VVFTRETGMT PSQWRHLNSQ KD
Length:282
Mass (Da):32,373
Last modified:July 24, 2007 - v2
Checksum:i5563D7B0773CEC9D
GO

Sequence cautioni

The sequence AAA24530.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence AAB03039.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE77403.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA29453.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06058 Genomic DNA. Translation: CAA29453.1. Different initiation.
L19201 Genomic DNA. Translation: AAB03039.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76888.2.
AP009048 Genomic DNA. Translation: BAE77403.1. Different initiation.
X60699 Genomic DNA. Translation: CAA43110.1.
M85158 Genomic DNA. Translation: AAA24530.1. Sequence problems.
PIRiS40850.
RefSeqiNP_418342.2. NC_000913.3.
WP_001336056.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76888; AAC76888; b3906.
BAE77403; BAE77403; BAE77403.
GeneIDi948396.
KEGGiecj:JW3877.
eco:b3906.
PATRICi32123323. VBIEscCol129921_4022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06058 Genomic DNA. Translation: CAA29453.1. Different initiation.
L19201 Genomic DNA. Translation: AAB03039.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76888.2.
AP009048 Genomic DNA. Translation: BAE77403.1. Different initiation.
X60699 Genomic DNA. Translation: CAA43110.1.
M85158 Genomic DNA. Translation: AAA24530.1. Sequence problems.
PIRiS40850.
RefSeqiNP_418342.2. NC_000913.3.
WP_001336056.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP09378.
SMRiP09378. Positions 191-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263058. 8 interactions.
DIPiDIP-10693N.
IntActiP09378. 9 interactions.
STRINGi511145.b3906.

Proteomic databases

PaxDbiP09378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76888; AAC76888; b3906.
BAE77403; BAE77403; BAE77403.
GeneIDi948396.
KEGGiecj:JW3877.
eco:b3906.
PATRICi32123323. VBIEscCol129921_4022.

Organism-specific databases

EchoBASEiEB0835.
EcoGeneiEG10842. rhaR.

Phylogenomic databases

eggNOGiENOG4108BRW. Bacteria.
ENOG410XYX0. LUCA.
HOGENOMiHOG000290513.
InParanoidiP09378.
KOiK02854.
OMAiFALDEFC.
OrthoDBiEOG6Z3KH4.
PhylomeDBiP09378.

Enzyme and pathway databases

BioCyciEcoCyc:PD00222.
ECOL316407:JW3877-MONOMER.

Miscellaneous databases

PROiP09378.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
2.60.120.280. 1 hit.
HAMAPiMF_01533. HTH_type_RhaR.
InterProiIPR003313. AraC-bd.
IPR009057. Homeodomain-like.
IPR018060. HTH_AraC.
IPR018062. HTH_AraC-typ_CS.
IPR011051. RmlC_Cupin.
IPR023699. Tscrpt_act_RhaR.
IPR020449. Tscrpt_reg_HTH_AraC-type.
[Graphical view]
PfamiPF02311. AraC_binding. 1 hit.
PF12833. HTH_18. 1 hit.
[Graphical view]
PRINTSiPR00032. HTHARAC.
SMARTiSM00342. HTH_ARAC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF51182. SSF51182. 1 hit.
PROSITEiPS00041. HTH_ARAC_FAMILY_1. 1 hit.
PS01124. HTH_ARAC_FAMILY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Positive regulation of the Escherichia coli L-rhamnose operon is mediated by the products of tandemly repeated regulatory genes."
    Tobin J.F., Schleif R.F.
    J. Mol. Biol. 196:789-799(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli."
    Garcia C., Baldoma L., Badia J., Aguilar J.
    J. Gen. Microbiol. 138:1109-1116(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-282.
    Strain: K12.
  6. "Mapping, cloning, expression, and sequencing of the rhaT gene, which encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium and Escherichia coli."
    Tate C.G., Muiry J.A.R., Henderson P.J.F.
    J. Biol. Chem. 267:6923-6932(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 266-282.
    Strain: K12.
  7. "A regulatory cascade in the induction of rhaBAD."
    Egan S.M., Schleif R.F.
    J. Mol. Biol. 234:87-98(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: ECL116.
  8. "Transcriptional regulation of the Escherichia coli rhaT gene."
    Via P., Badia J., Baldoma L., Obradors N., Aguilar J.
    Microbiology 142:1833-1840(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Interdependence of activation at rhaSR by cyclic AMP receptor protein, the RNA polymerase alpha subunit C-terminal domain, and rhaR."
    Holcroft C.C., Egan S.M.
    J. Bacteriol. 182:6774-6782(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY CRP.
  10. "Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR."
    Wickstrum J.R., Egan S.M.
    J. Bacteriol. 186:6277-6285(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIGMA-70.

Entry informationi

Entry nameiRHAR_ECOLI
AccessioniPrimary (citable) accession number: P09378
Secondary accession number(s): Q2M8K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 24, 2007
Last modified: January 20, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Its activity is regulated by L-rhamnose. When this sugar becomes available to the cell, basal-level RhaR binds L-rhamnose and becomes activated.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.