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Protein

Regulator of RpoS

Gene

rssB

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

Functioni

Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. In stationary phase, could also act as an anti-sigma factor and reduce the ability of RpoS to activate gene expression. Is also involved in the regulation of the mRNA polyadenylation pathway during stationary phase, probably by maintaining the association of PcnB with the degradosome.6 PublicationsUniRule annotation

Enzyme regulationi

Under certain stress conditions, activity is inhibited by the anti-adapter proteins IraP, IraD and IraM. IraP is involved in response to phosphate stavation, IraD in response to DNA damage and IraM in response to magnesium starvation. IraD and IraM interact with inactive RssB, blocking its ability to interact with RpoS. IraP may mimic RpoS in its interaction with RssB and directly competing with RpoS for binding to RssB.3 Publications

GO - Molecular functioni

  1. sigma factor antagonist activity Source: EcoCyc

GO - Biological processi

  1. phosphorelay signal transduction system Source: InterPro
  2. positive regulation of proteolysis Source: EcoCyc
  3. protein destabilization Source: EcoCyc
  4. regulation of nucleic acid-templated transcription Source: GOC
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:EG12121-MONOMER.
ECOL316407:JW1223-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of RpoSUniRule annotation
Gene namesi
Name:rssBUniRule annotation
Synonyms:hnr, sprE, ychL
Ordered Locus Names:b1235, JW1223
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12121. rssB.

Pathology & Biotechi

Disruption phenotypei

Mutants exhibit nearly constitutively high levels of RpoS and are impaired in the post-transcriptional growth phase-related and osmotic regulation of RpoS. In exponentially growing cells, mutants exhibit significantly reduced levels of polyadenylation and increased stability of specific mRNAs.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581D → P, Q or R: Lack of phosphorylation. Cannot bind RpoS. 3 Publications
Mutagenesisi67 – 671L → A: Lack of phosphorylation. 1 Publication
Mutagenesisi109 – 1091P → S: Resistant to IraP but not to IraD. Increases stabilization by IraM. Decreases phosphorylation. 1 Publication
Mutagenesisi143 – 1431W → R: Resistant to both IraP and IraD. Increases stabilization by IraM. 1 Publication
Mutagenesisi214 – 2141L → H: Resistant to IraP and IraD. 1 Publication
Mutagenesisi216 – 2161A → T: Resistant to IraP, IraD and IraM. 1 Publication
Mutagenesisi218 – 2181L → V: Resistant to IraP, IraD and IraM. 1 Publication
Mutagenesisi255 – 2551A → V: Resistant to IraM. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Regulator of RpoSPRO_0000081388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 5814-aspartylphosphate1 PublicationUniRule annotation

Post-translational modificationi

Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS.4 PublicationsUniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP0AEV1.

Expressioni

Inductioni

Expression is induced during stationary phase by RpoS.1 Publication

Gene expression databases

GenevestigatoriP0AEV1.

Interactioni

Subunit structurei

Binds to RpoS with a stoichiometry of 1:1. Interacts with the anti-adapter proteins IraP, IraD and IraM.6 PublicationsUniRule annotation

Protein-protein interaction databases

IntActiP0AEV1. 4 interactions.
STRINGi511145.b1235.

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi9 – 135Combined sources
Helixi17 – 2913Combined sources
Beta strandi33 – 386Combined sources
Helixi40 – 478Combined sources
Beta strandi53 – 575Combined sources
Helixi67 – 759Combined sources
Beta strandi82 – 865Combined sources
Helixi91 – 10010Combined sources
Beta strandi103 – 1086Combined sources
Helixi115 – 12410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EODX-ray1.75A1-130[»]
ProteinModelPortaliP0AEV1.
SMRiP0AEV1. Positions 3-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 123115Response regulatoryUniRule annotationAdd
BLAST

Domaini

Contains an N-terminal receiver domain and a C-terminal output domain that are both required for binding to RpoS. IraP and IraD interact with the N-terminal domain. IraM interacts with the C-terminal domain and, more weakly, the N-terminal domain.2 Publications

Sequence similaritiesi

Belongs to the RssB family.UniRule annotation
Contains 1 response regulatory domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000119811.
InParanoidiP0AEV1.
KOiK02485.
OMAiEERLFQD.
OrthoDBiEOG69GZGV.
PhylomeDBiP0AEV1.

Family and domain databases

HAMAPiMF_00958. RssB.
InterProiIPR011006. CheY-like_superfamily.
IPR028616. RssB.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTQPLVGKQI LIVEDEQVFR SLLDSWFSSL GATTVLAADG VDALELLGGF
60 70 80 90 100
TPDLMICDIA MPRMNGLKLL EHIRNRGDQT PVLVISATEN MADIAKALRL
110 120 130 140 150
GVEDVLLKPV KDLNRLREMV FACLYPSMFN SRVEEEERLF RDWDAMVDNP
160 170 180 190 200
AAAAKLLQEL QPPVQQVISH CRVNYRQLVA ADKPGLVLDI AALSENDLAF
210 220 230 240 250
YCLDVTRAGH NGVLAALLLR ALFNGLLQEQ LAHQNQRLPE LGALLKQVNH
260 270 280 290 300
LLRQANLPGQ FPLLVGYYHR ELKNLILVSA GLNATLNTGE HQVQISNGVP
310 320 330
LGTLGNAYLN QLSQRCDAWQ CQIWGTGGRL RLMLSAE
Length:337
Mass (Da):37,302
Last modified:December 20, 2005 - v1
Checksum:iAB962EF94BC7B470
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66003 Genomic DNA. Translation: CAA46802.1.
M64675 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74317.1.
AP009048 Genomic DNA. Translation: BAA36103.1.
PIRiA36871.
RefSeqiNP_415751.1. NC_000913.3.
YP_489503.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74317; AAC74317; b1235.
BAA36103; BAA36103; BAA36103.
GeneIDi12932932.
945855.
KEGGiecj:Y75_p1208.
eco:b1235.
PATRICi32117726. VBIEscCol129921_1283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66003 Genomic DNA. Translation: CAA46802.1.
M64675 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74317.1.
AP009048 Genomic DNA. Translation: BAA36103.1.
PIRiA36871.
RefSeqiNP_415751.1. NC_000913.3.
YP_489503.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EODX-ray1.75A1-130[»]
ProteinModelPortaliP0AEV1.
SMRiP0AEV1. Positions 3-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0AEV1. 4 interactions.
STRINGi511145.b1235.

Proteomic databases

PRIDEiP0AEV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74317; AAC74317; b1235.
BAA36103; BAA36103; BAA36103.
GeneIDi12932932.
945855.
KEGGiecj:Y75_p1208.
eco:b1235.
PATRICi32117726. VBIEscCol129921_1283.

Organism-specific databases

EchoBASEiEB2042.
EcoGeneiEG12121. rssB.

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000119811.
InParanoidiP0AEV1.
KOiK02485.
OMAiEERLFQD.
OrthoDBiEOG69GZGV.
PhylomeDBiP0AEV1.

Enzyme and pathway databases

BioCyciEcoCyc:EG12121-MONOMER.
ECOL316407:JW1223-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEV1.
PROiP0AEV1.

Gene expression databases

GenevestigatoriP0AEV1.

Family and domain databases

HAMAPiMF_00958. RssB.
InterProiIPR011006. CheY-like_superfamily.
IPR028616. RssB.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Contreras A.
    Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Organization and functions of genes in the upstream region of tyrT of Escherichia coli: phenotypes of mutants with partial deletion of a new gene (tgs)."
    Boesl M., Kersten H.
    J. Bacteriol. 176:221-231(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli."
    Muffler A., Fischer D., Altuvia S., Storz G., Hengge-Aronis R.
    EMBO J. 15:1333-1339(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, GENE NAME.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  7. "The response regulator SprE controls the stability of RpoS."
    Pratt L.A., Silhavy T.J.
    Proc. Natl. Acad. Sci. U.S.A. 93:2488-2492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  8. "Regulation of RssB-dependent proteolysis in Escherichia coli: a role for acetyl phosphate in a response regulator-controlled process."
    Bouche S., Klauck E., Fischer D., Lucassen M., Jung K., Hengge-Aronis R.
    Mol. Microbiol. 27:787-795(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT ASP-58, MUTAGENESIS OF ASP-58.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  9. "Regulation of RpoS proteolysis in Escherichia coli: the response regulator RssB is a recognition factor that interacts with the turnover element in RpoS."
    Becker G., Klauck E., Hengge-Aronis R.
    Proc. Natl. Acad. Sci. U.S.A. 96:6439-6444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPOS, PHOSPHORYLATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  10. "SprE levels are growth phase regulated in a sigma(S)-dependent manner at the level of translation."
    Gibson K.E., Silhavy T.J.
    J. Bacteriol. 182:4117-4120(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  11. "The response regulator RssB, a recognition factor for sigmaS proteolysis in Escherichia coli, can act like an anti-sigmaS factor."
    Becker G., Klauck E., Hengge-Aronis R.
    Mol. Microbiol. 35:657-666(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH RPOS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "Role of the response regulator RssB in sigma recognition and initiation of sigma proteolysis in Escherichia coli."
    Klauck E., Lingnau M., Hengge-Aronis R.
    Mol. Microbiol. 40:1381-1390(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPOS, DOMAIN, PHOSPHORYLATION, MUTAGENESIS OF ASP-58.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  13. "Modulating RssB activity: IraP, a novel regulator of sigma(S) stability in Escherichia coli."
    Bougdour A., Wickner S., Gottesman S.
    Genes Dev. 20:884-897(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH IRAP.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors."
    Bougdour A., Cunning C., Baptiste P.J., Elliott T., Gottesman S.
    Mol. Microbiol. 68:298-313(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH IRAD AND IRAM.
    Strain: K12 / MG1655 / ATCC 47076.
  15. "The response regulator SprE (RssB) modulates polyadenylation and mRNA stability in Escherichia coli."
    Carabetta V.J., Mohanty B.K., Kushner S.R., Silhavy T.J.
    J. Bacteriol. 191:6812-6821(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POLYADENYLATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  16. "The response regulator SprE (RssB) is required for maintaining poly(A) polymerase I-degradosome association during stationary phase."
    Carabetta V.J., Silhavy T.J., Cristea I.M.
    J. Bacteriol. 192:3713-3721(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN POLYADENYLATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  17. "Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein."
    Battesti A., Hoskins J.R., Tong S., Milanesio P., Mann J.M., Kravats A., Tsegaye Y.M., Bougdour A., Wickner S., Gottesman S.
    Genes Dev. 27:2722-2735(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH IRAP; IRAD AND IRAM, DOMAIN, PHOSPHORYLATION, MUTAGENESIS OF ASP-58; LEU-67; PRO-109; TRP-143; LEU-214; ALA-216; LEU-218 AND ALA-255.
  18. "The structure of RssB, a ClpX adaptor protein that regulates sigma S."
    Levchenko I., Grant R.A., Sauer R.T., Baker T.A.
    Submitted (SEP-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-130.

Entry informationi

Entry nameiRSSB_ECOLI
AccessioniPrimary (citable) accession number: P0AEV1
Secondary accession number(s): P37055
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.