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Protein

RsbT co-antagonist protein RsbRA

Gene

rsbRA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro.
One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.
Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.

Enzyme and pathway databases

BioCyciBSUB:BSU04670-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RsbT co-antagonist protein RsbRA
Alternative name(s):
Stressosome protein RsbRA
Gene namesi
Name:rsbRA
Synonyms:rsbR, ycxR
Ordered Locus Names:BSU04670
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene have a decreased response to salt stress, indicating that RsbRA is a positive regulator of sigma-B activity. Its activity is dependent on RsbRB.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711T → A: No phosphorylation; when associated with A-205. No stress response. In absence of the other RsbR paralogs greatly reduced stress response. 1 Publication
Mutagenesisi171 – 1711T → D: Decrease in induction of sigma-B activity in response to a salt stress. In absence of the other RsbR paralogs no change in stress response. 1 Publication
Mutagenesisi205 – 2051T → A: No phosphorylation; when associated with A-171. In absence of the other RsbR paralogs unable to function as a co-antagonist when RsbRB. 1 Publication
Mutagenesisi205 – 2051T → D: Decrease in induction of sigma-B activity in response to a salt stress. In absence of the other RsbR paralogs no change in stress response when RsbRB. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274RsbT co-antagonist protein RsbRAPRO_0000097470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711Phosphothreonine2 Publications
Modified residuei205 – 2051Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by RsbT. This threonine phosphorylation abrogates the ability of RsbRA to stimulate RsbT in vitro.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP42409.

PTM databases

iPTMnetiP42409.

Interactioni

Subunit structurei

Interacts with RsbRB and RsbS in the stressosome. The stressosome probably also contains RsbRC and RsbRD.1 Publication

Protein-protein interaction databases

DIPiDIP-375N.
IntActiP42409. 2 interactions.
STRINGi224308.Bsubs1_010100002643.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Helixi15 – 3016Combined sources
Helixi39 – 5416Combined sources
Turni60 – 634Combined sources
Helixi64 – 7613Combined sources
Helixi81 – 10020Combined sources
Helixi109 – 13527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BNLX-ray2.00A/B/C/D/E/F1-136[»]
ProteinModelPortaliP42409.
SMRiP42409. Positions 3-136, 152-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42409.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini150 – 265116STASPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 STAS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107MMM. Bacteria.
COG1366. LUCA.
HOGENOMiHOG000269596.
InParanoidiP42409.
KOiK17763.
OMAiLQKGIQT.
PhylomeDBiP42409.

Family and domain databases

Gene3Di3.30.750.24. 1 hit.
InterProiIPR014792. RsbRA_N.
IPR002645. STAS_dom.
[Graphical view]
PfamiPF08678. Rsbr_N. 1 hit.
PF01740. STAS. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 1 hit.
PROSITEiPS50801. STAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSNQTVYQF IAENQNELLQ LWTDTLKELS EQESYQLTDQ VYENISKEYI
60 70 80 90 100
DILLLSVKDE NAAESQISEL ALRAVQIGLS MKFLATALAE FWKRLYTKMN
110 120 130 140 150
DKRLPDQEST ELIWQIDRFF SPINTEIFNQ YSISWEKTVS LQKIALQELS
160 170 180 190 200
APLIPVFENI TVMPLVGTID TERAKRIMEN LLNGVVKHRS QVVLIDITGV
210 220 230 240 250
PVVDTMVAHH IIQASEAVRL VGAKCLLAGI RPEIAQTIVN LGIDLSQVIT
260 270
KNTLQKGIQT ALEMTDRKIV SLGE
Length:274
Mass (Da):31,050
Last modified:November 1, 1995 - v1
Checksum:i4E14615EA6FC0493
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85080.1.
AB001488 Genomic DNA. Translation: BAA19304.1.
AL009126 Genomic DNA. Translation: CAB12274.1.
PIRiE69701.
RefSeqiNP_388348.1. NC_000964.3.
WP_009966610.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12274; CAB12274; BSU04670.
GeneIDi938176.
KEGGibsu:BSU04670.
PATRICi18972518. VBIBacSub10457_0487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85080.1.
AB001488 Genomic DNA. Translation: BAA19304.1.
AL009126 Genomic DNA. Translation: CAB12274.1.
PIRiE69701.
RefSeqiNP_388348.1. NC_000964.3.
WP_009966610.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BNLX-ray2.00A/B/C/D/E/F1-136[»]
ProteinModelPortaliP42409.
SMRiP42409. Positions 3-136, 152-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-375N.
IntActiP42409. 2 interactions.
STRINGi224308.Bsubs1_010100002643.

PTM databases

iPTMnetiP42409.

Proteomic databases

PaxDbiP42409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12274; CAB12274; BSU04670.
GeneIDi938176.
KEGGibsu:BSU04670.
PATRICi18972518. VBIBacSub10457_0487.

Phylogenomic databases

eggNOGiENOG4107MMM. Bacteria.
COG1366. LUCA.
HOGENOMiHOG000269596.
InParanoidiP42409.
KOiK17763.
OMAiLQKGIQT.
PhylomeDBiP42409.

Enzyme and pathway databases

BioCyciBSUB:BSU04670-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP42409.

Family and domain databases

Gene3Di3.30.750.24. 1 hit.
InterProiIPR014792. RsbRA_N.
IPR002645. STAS_dom.
[Graphical view]
PfamiPF08678. Rsbr_N. 1 hit.
PF01740. STAS. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 1 hit.
PROSITEiPS50801. STAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSBRA_BACSU
AccessioniPrimary (citable) accession number: P42409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 115 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.