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P0AEV1

- RSSB_ECOLI

UniProt

P0AEV1 - RSSB_ECOLI

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Protein
Regulator of RpoS
Gene
rssB, hnr, sprE, ychL, b1235, JW1223
Organism
Escherichia coli (strain K12)
Status
Reviewed - - 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 Publications

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. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
  2. protein bindingInferred from physical interactioni PubMed 10339606PubMed 16600914PubMed 18383615 Source: EcoCyc
  3. sigma factor antagonist activityInferred from direct assayi PubMed 10672187 Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. positive regulation of proteolysisInferred from direct assayi PubMed 11238382 Source: EcoCyc
  2. protein destabilizationInferred from mutant phenotypei PubMed 8635466PubMed 8637901 Source: EcoCyc
  3. regulation of RNA biosynthetic processInferred from direct assayi PubMed 10672187 Source: GOC
  4. response to stressInferred from electronic annotationi Source: UniProtKB-KW
  1. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
  2. sigma factor antagonist activityInferred from direct assayi PubMed 10672187 Source: EcoCyc
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 RpoS
Gene namesi
Name:rssB
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 identifier
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 identifier
Chaini1 – 337337Regulator of RpoSUniRule annotation
PRO_0000081388

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei58 – 5814-aspartylphosphateUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP0AEV1.

Expressioni

Inductioni

Expression is induced during stationary phase by RpoS.4 Publications

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 Publications

Protein-protein interaction databases

IntActiP0AEV1. 4 interactions.
STRINGi511145.b1235.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EODX-ray1.75A1-130[»]
ProteinModelPortaliP0AEV1.
SMRiP0AEV1. Positions 3-282.

Miscellaneous databases

EvolutionaryTraceiP0AEV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Domaini9 – 123115Response regulatory

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.

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000119811.
KOiK02485.
OMAiATSEPIH.
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]FASTA

« Hide

MTQPLVGKQI LIVEDEQVFR SLLDSWFSSL GATTVLAADG VDALELLGGF    50
TPDLMICDIA MPRMNGLKLL EHIRNRGDQT PVLVISATEN MADIAKALRL 100
GVEDVLLKPV KDLNRLREMV FACLYPSMFN SRVEEEERLF RDWDAMVDNP 150
AAAAKLLQEL QPPVQQVISH CRVNYRQLVA ADKPGLVLDI AALSENDLAF 200
YCLDVTRAGH NGVLAALLLR ALFNGLLQEQ LAHQNQRLPE LGALLKQVNH 250
LLRQANLPGQ FPLLVGYYHR ELKNLILVSA GLNATLNTGE HQVQISNGVP 300
LGTLGNAYLN QLSQRCDAWQ CQIWGTGGRL RLMLSAE 337
Length:337
Mass (Da):37,302
Last modified:December 20, 2005 - v1
Checksum:iAB962EF94BC7B470
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A36871.
RefSeqi NP_415751.1. NC_000913.3.
YP_489503.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EOD X-ray 1.75 A 1-130 [» ]
ProteinModelPortali P0AEV1.
SMRi P0AEV1. Positions 3-282.
ModBasei Search...

Protein-protein interaction databases

IntActi P0AEV1. 4 interactions.
STRINGi 511145.b1235.

Proteomic databases

PRIDEi P0AEV1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74317 ; AAC74317 ; b1235 .
BAA36103 ; BAA36103 ; BAA36103 .
GeneIDi 12932932.
945855.
KEGGi ecj:Y75_p1208.
eco:b1235.
PATRICi 32117726. VBIEscCol129921_1283.

Organism-specific databases

EchoBASEi EB2042.
EcoGenei EG12121. rssB.

Phylogenomic databases

eggNOGi COG0784.
HOGENOMi HOG000119811.
KOi K02485.
OMAi ATSEPIH.
OrthoDBi EOG69GZGV.
PhylomeDBi P0AEV1.

Enzyme and pathway databases

BioCyci EcoCyc:EG12121-MONOMER.
ECOL316407:JW1223-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AEV1.
PROi P0AEV1.

Gene expression databases

Genevestigatori P0AEV1.

Family and domain databases

HAMAPi MF_00958. RssB.
InterProi IPR011006. CheY-like_superfamily.
IPR028616. RssB.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view ]
Pfami PF00072. Response_reg. 1 hit.
[Graphical view ]
SMARTi SM00448. REC. 1 hit.
[Graphical view ]
SUPFAMi SSF52172. SSF52172. 1 hit.
PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  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. "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
    Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.
    , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
    DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    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 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: June 11, 2014
This is version 74 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

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