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

Transcriptional regulatory protein RcsB

Gene

rcsB

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

Functioni

Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.UniRule annotation7 Publications

Enzyme regulationi

Activity is modulated by phosphorylation and interaction with other transcriptional regulators. Probably up-regulated by YmgA/AriR, and possibly down-regulated by YcgZ, all 3 are connector proteins providing additional signal input into the signaling system.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi168 – 18720H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • phosphorelay signal transduction system Source: UniProtKB-HAMAP
  • positive regulation of cell projection organization Source: CACAO
  • positive regulation of transcription, DNA-templated Source: EcoCyc
  • response to antibiotic Source: CACAO
  • single-species biofilm formation on inanimate substrate Source: CACAO
  • transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Capsule biogenesis/degradation, Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein RcsBUniRule annotation
Alternative name(s):
Capsular synthesis regulator component B
Gene namesi
Name:rcsBUniRule annotation
Ordered Locus Names:b2217, JW2205
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10821. rcsB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561D → E: Increases heterodimer formation with RcsA. Does not affect heterodimer formation with BglJ. 1 Publication
Mutagenesisi56 – 561D → N: Decreases heterodimer formation with RcsA. Does not affect heterodimer formation with BglJ. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Transcriptional regulatory protein RcsBPRO_0000081209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 5614-aspartylphosphateUniRule annotation

Post-translational modificationi

Phosphorylated and activated by RcsD.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0DMC7.

Expressioni

Inductioni

Expression is dependent on the alternate sigma factor, RpoN (PubMed:2404948). Repressed by hydroxyurea.2 Publications

Interactioni

Subunit structurei

Interacts with RcsD and RcsA. Homodimer. Can form an heterodimer with the coactivator RcsA, which binds to the RcsAB boxes to promote transcription of RcsA-dependent genes. Can also form a heterodimer with GadE to bind to the GAD box, and with BglJ to bind to the bgl promoter.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
bglJP394042EBI-369670,EBI-551429

Protein-protein interaction databases

BioGridi4260879. 3 interactions.
IntActiP0DMC7. 40 interactions.
STRINGi511145.b2217.

Structurei

3D structure databases

ProteinModelPortaliP0DMC7.
SMRiP0DMC7. Positions 1-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 124120Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini144 – 20966HTH luxR-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RcsB family.UniRule annotation
Contains 1 HTH luxR-type DNA-binding domain.UniRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41068CG. Bacteria.
COG2197. LUCA.
KOiK07687.
OMAiIEWVNIV.
PhylomeDBiP0DMC7.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00981. RcsB.
InterProiIPR011006. CheY-like_superfamily.
IPR030864. RcsB.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0DMC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNMNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINNLPKLDA
60 70 80 90 100
HVLITDLSMP GDKYGDGITL IKYIKRHFPS LSIIVLTMNN NPAILSAVLD
110 120 130 140 150
LDIEGIVLKQ GAPTDLPKAL AALQKGKKFT PESVSRLLEK ISAGGYGDKR
160 170 180 190 200
LSPKESEVLR LFAEGFLVTE IAKKLNRSIK TISSQKKSAM MKLGVENDIA
210
LLNYLSSVTL SPADKD
Length:216
Mass (Da):23,671
Last modified:February 19, 2014 - v1
Checksum:iA78D1BD3004E0680
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28242 Genomic DNA. Translation: AAA24504.1.
U00096 Genomic DNA. Translation: AAC75277.1.
AP009048 Genomic DNA. Translation: BAA16000.1.
S37760 Genomic DNA. Translation: AAB22290.1.
PIRiJV0068. BVECCB.
RefSeqiNP_416721.1. NC_000913.3.
WP_001061917.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75277; AAC75277; b2217.
BAA16000; BAA16000; BAA16000.
GeneIDi947441.
KEGGiecj:JW2205.
eco:b2217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28242 Genomic DNA. Translation: AAA24504.1.
U00096 Genomic DNA. Translation: AAC75277.1.
AP009048 Genomic DNA. Translation: BAA16000.1.
S37760 Genomic DNA. Translation: AAB22290.1.
PIRiJV0068. BVECCB.
RefSeqiNP_416721.1. NC_000913.3.
WP_001061917.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0DMC7.
SMRiP0DMC7. Positions 1-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260879. 3 interactions.
IntActiP0DMC7. 40 interactions.
STRINGi511145.b2217.

Proteomic databases

PaxDbiP0DMC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75277; AAC75277; b2217.
BAA16000; BAA16000; BAA16000.
GeneIDi947441.
KEGGiecj:JW2205.
eco:b2217.

Organism-specific databases

EchoBASEiEB0814.
EcoGeneiEG10821. rcsB.

Phylogenomic databases

eggNOGiENOG41068CG. Bacteria.
COG2197. LUCA.
KOiK07687.
OMAiIEWVNIV.
PhylomeDBiP0DMC7.

Miscellaneous databases

PROiP0DMC7.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00981. RcsB.
InterProiIPR011006. CheY-like_superfamily.
IPR030864. RcsB.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RcsB and RcsC: a two-component regulator of capsule synthesis in Escherichia coli."
    Stout V., Gottesman S.
    J. Bacteriol. 172:659-669(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "The rcsB gene, a positive regulator of colanic acid biosynthesis in Escherichia coli, is also an activator of ftsZ expression."
    Gervais F.G., Phoenix P., Drapeau G.R.
    J. Bacteriol. 174:3964-3971(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-9, FUNCTION IN COLANIC ACID SYNTHESIS AND CELL DIVISION.
    Strain: K12.
  6. "RcsA, an unstable positive regulator of capsular polysaccharide synthesis."
    Stout V., Torres-Cabassa A., Maurizi M.R., Gutnick D., Gottesman S.
    J. Bacteriol. 173:1738-1747(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RCSA.
  7. "The RcsAB box. Characterization of a new operator essential for the regulation of exopolysaccharide biosynthesis in enteric bacteria."
    Wehland M., Bernhard F.
    J. Biol. Chem. 275:7013-7020(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RCSA, BINDING TO RCSAB BOX.
  8. "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli."
    Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.
    Biosci. Biotechnol. Biochem. 65:2364-2367(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORELAY.
  9. "Regulation of osmC gene expression by the two-component system rcsB-rcsC in Escherichia coli."
    Davalos-Garcia M., Conter A., Toesca I., Gutierrez C., Cam K.
    J. Bacteriol. 183:5870-5876(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  10. "A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC->YojN->RcsB signalling pathway implicated in capsular synthesis and swarming behaviour."
    Takeda S.-H., Fujisawa Y., Matsubara M., Aiba H., Mizuno T.
    Mol. Microbiol. 40:440-450(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, PHOSPHORELAY.
  11. "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli."
    Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T., Mizuno T.
    J. Bacteriol. 185:5735-5746(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORELAY.
    Strain: K12 / ST001.
  12. "Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains."
    Rogov V.V., Bernhard F., Loehr F., Doetsch V.
    J. Mol. Biol. 343:1035-1048(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RCSD.
  13. "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli."
    Tschowri N., Busse S., Hengge R.
    Genes Dev. 23:522-534(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
    Strain: K12 / MC4100.
  14. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYDROXYUREA.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. "BglJ-RcsB heterodimers relieve repression of the Escherichia coli bgl operon by H-NS."
    Venkatesh G.R., Kembou Koungni F.C., Paukner A., Stratmann T., Blissenbach B., Schnetz K.
    J. Bacteriol. 192:6456-6464(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BGL DEREPRESSION, ENZYME REGULATION, INTERACTION WITH RCSA AND BGLJ, MUTAGENESIS OF ASP-56.
    Strain: CSH50.
  16. "Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE."
    Castanie-Cornet M.P., Cam K., Bastiat B., Cros A., Bordes P., Gutierrez C.
    Nucleic Acids Res. 38:3546-3554(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GADE, BINDING TO THE GAD BOX.

Entry informationi

Entry nameiRCSB_ECOLI
AccessioniPrimary (citable) accession number: P0DMC7
Secondary accession number(s): P14374, P69407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 19, 2014
Last modified: July 6, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There is a close linkage between the Rcs and PhoQ/P signaling systems, and both signaling systems respond to certain external divalent cations (zinc and magnesium).1 Publication

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.