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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.UniRule annotation6 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

  • sigma factor antagonist activity Source: EcoCyc

GO - Biological processi

  • phosphorelay signal transduction system Source: InterPro
  • positive regulation of proteolysis Source: EcoCyc
  • protein destabilization Source: EcoCyc
  • regulation of gene expression Source: UniProtKB-HAMAP
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12121. rssB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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)DescriptionActionsGraphical viewLength
Mutagenesisi58D → P, Q or R: Lack of phosphorylation. Cannot bind RpoS. 3 Publications1
Mutagenesisi67L → A: Lack of phosphorylation. 1 Publication1
Mutagenesisi109P → S: Resistant to IraP but not to IraD. Increases stabilization by IraM. Decreases phosphorylation. 1 Publication1
Mutagenesisi143W → R: Resistant to both IraP and IraD. Increases stabilization by IraM. 1 Publication1
Mutagenesisi214L → H: Resistant to IraP and IraD. 1 Publication1
Mutagenesisi216A → T: Resistant to IraP, IraD and IraM. 1 Publication1
Mutagenesisi218L → V: Resistant to IraP, IraD and IraM. 1 Publication1
Mutagenesisi255A → V: Resistant to IraM. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000813881 – 337Regulator of RpoSAdd BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei584-aspartylphosphateUniRule annotation1 Publication1

Post-translational modificationi

Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS.UniRule annotation4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AEV1.
PRIDEiP0AEV1.

Expressioni

Inductioni

Expression is induced during stationary phase by RpoS.1 Publication

Interactioni

Subunit structurei

Binds to RpoS with a stoichiometry of 1:1. Interacts with the anti-adapter proteins IraP, IraD and IraM.UniRule annotation6 Publications

Protein-protein interaction databases

IntActiP0AEV1. 4 interactors.
STRINGi511145.b1235.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Beta strandi9 – 13Combined sources5
Helixi17 – 29Combined sources13
Beta strandi33 – 38Combined sources6
Helixi40 – 47Combined sources8
Beta strandi53 – 57Combined sources5
Helixi67 – 75Combined sources9
Beta strandi82 – 86Combined sources5
Helixi91 – 100Combined sources10
Beta strandi103 – 108Combined sources6
Helixi115 – 124Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AEV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 123Response regulatoryPROSITE-ProRule annotationAdd BLAST115

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.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105I93. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000119811.
InParanoidiP0AEV1.
KOiK02485.
OMAiEERLFQD.
PhylomeDBiP0AEV1.

Family and domain databases

HAMAPiMF_00958. RssB. 1 hit.
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.
WP_000193447.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74317; AAC74317; b1235.
BAA36103; BAA36103; BAA36103.
GeneIDi945855.
KEGGiecj:JW1223.
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.
WP_000193447.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

IntActiP0AEV1. 4 interactors.
STRINGi511145.b1235.

Proteomic databases

PaxDbiP0AEV1.
PRIDEiP0AEV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74317; AAC74317; b1235.
BAA36103; BAA36103; BAA36103.
GeneIDi945855.
KEGGiecj:JW1223.
eco:b1235.
PATRICi32117726. VBIEscCol129921_1283.

Organism-specific databases

EchoBASEiEB2042.
EcoGeneiEG12121. rssB.

Phylogenomic databases

eggNOGiENOG4105I93. Bacteria.
COG0784. LUCA.
HOGENOMiHOG000119811.
InParanoidiP0AEV1.
KOiK02485.
OMAiEERLFQD.
PhylomeDBiP0AEV1.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AEV1.
PROiP0AEV1.

Family and domain databases

HAMAPiMF_00958. RssB. 1 hit.
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...

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: November 2, 2016
This is version 88 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

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.