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P0AEV1 (RSSB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of RpoS
Gene names
Name:rssB
Synonyms:hnr, sprE, ychL
Ordered Locus Names:b1235, JW1223
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.11 Ref.12 Ref.15 Ref.16

Enzyme regulation

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. Ref.13 Ref.14 Ref.17

Subunit structure

Binds to RpoS with a stoichiometry of 1:1. Interacts with the anti-adapter proteins IraP, IraD and IraM. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

Induction

Expression is induced during stationary phase by RpoS. Ref.10 Ref.13 Ref.14 Ref.17

Domain

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. Ref.12 Ref.17

Post-translational modification

Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS. Ref.8 Ref.9 Ref.12 Ref.17

Disruption phenotype

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. Ref.6 Ref.15

Sequence similarities

Belongs to the RssB family.

Contains 1 response regulatory domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Regulator of RpoS HAMAP-Rule MF_00958
PRO_0000081388

Regions

Domain9 – 123115Response regulatory

Amino acid modifications

Modified residue5814-aspartylphosphate HAMAP-Rule MF_00958

Experimental info

Mutagenesis581D → P, Q or R: Lack of phosphorylation. Cannot bind RpoS. Ref.8 Ref.12 Ref.17
Mutagenesis671L → A: Lack of phosphorylation. Ref.17
Mutagenesis1091P → S: Resistant to IraP but not to IraD. Increases stabilization by IraM. Decreases phosphorylation. Ref.17
Mutagenesis1431W → R: Resistant to both IraP and IraD. Increases stabilization by IraM. Ref.17
Mutagenesis2141L → H: Resistant to IraP and IraD. Ref.17
Mutagenesis2161A → T: Resistant to IraP, IraD and IraM. Ref.17
Mutagenesis2181L → V: Resistant to IraP, IraD and IraM. Ref.17
Mutagenesis2551A → V: Resistant to IraM. Ref.17

Secondary structure

....................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEV1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: AB962EF94BC7B470

FASTA33737,302
        10         20         30         40         50         60 
MTQPLVGKQI LIVEDEQVFR SLLDSWFSSL GATTVLAADG VDALELLGGF TPDLMICDIA 

        70         80         90        100        110        120 
MPRMNGLKLL EHIRNRGDQT PVLVISATEN MADIAKALRL GVEDVLLKPV KDLNRLREMV 

       130        140        150        160        170        180 
FACLYPSMFN SRVEEEERLF RDWDAMVDNP AAAAKLLQEL QPPVQQVISH CRVNYRQLVA 

       190        200        210        220        230        240 
ADKPGLVLDI AALSENDLAF YCLDVTRAGH NGVLAALLLR ALFNGLLQEQ LAHQNQRLPE 

       250        260        270        280        290        300 
LGALLKQVNH LLRQANLPGQ FPLLVGYYHR ELKNLILVSA GLNATLNTGE HQVQISNGVP 

       310        320        330 
LGTLGNAYLN QLSQRCDAWQ CQIWGTGGRL RLMLSAE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66003 Genomic DNA. Translation: CAA46802.1.
M64675 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74317.1.
AP009048 Genomic DNA. Translation: BAA36103.1.
PIRA36871.
RefSeqNP_415751.1. NC_000913.3.
YP_489503.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EODX-ray1.75A1-130[»]
ProteinModelPortalP0AEV1.
SMRP0AEV1. Positions 3-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AEV1. 4 interactions.
STRING511145.b1235.

Proteomic databases

PRIDEP0AEV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74317; AAC74317; b1235.
BAA36103; BAA36103; BAA36103.
GeneID12932932.
945855.
KEGGecj:Y75_p1208.
eco:b1235.
PATRIC32117726. VBIEscCol129921_1283.

Organism-specific databases

EchoBASEEB2042.
EcoGeneEG12121. rssB.

Phylogenomic databases

eggNOGCOG0784.
HOGENOMHOG000119811.
KOK02485.
OMAATSEPIH.
OrthoDBEOG69GZGV.
PhylomeDBP0AEV1.

Enzyme and pathway databases

BioCycEcoCyc:EG12121-MONOMER.
ECOL316407:JW1223-MONOMER.

Gene expression databases

GenevestigatorP0AEV1.

Family and domain databases

HAMAPMF_00958. RssB.
InterProIPR011006. CheY-like_superfamily.
IPR028616. RssB.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52172. SSF52172. 1 hit.
PROSITEPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEV1.
PROP0AEV1.

Entry information

Entry nameRSSB_ECOLI
AccessionPrimary (citable) accession number: P0AEV1
Secondary accession number(s): P37055
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene