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Protein

RsbT co-antagonist protein RsbRA

Gene

rsbRA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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.

GO - Molecular functioni

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)DescriptionActionsGraphical viewLength
Mutagenesisi171T → A: No phosphorylation; when associated with A-205. No stress response. In absence of the other RsbR paralogs greatly reduced stress response. 1 Publication1
Mutagenesisi171T → 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 Publication1
Mutagenesisi205T → 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 Publication1
Mutagenesisi205T → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000974701 – 274RsbT co-antagonist protein RsbRAAdd BLAST274

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei171Phosphothreonine2 Publications1
Modified residuei205Phosphothreonine1 Publication1

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
PRIDEiP42409

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 interactors
STRINGi224308.Bsubs1_010100002643

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 13Combined sources9
Helixi15 – 30Combined sources16
Helixi39 – 54Combined sources16
Turni60 – 63Combined sources4
Helixi64 – 76Combined sources13
Helixi81 – 100Combined sources20
Helixi109 – 135Combined sources27

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42409

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 265STASPROSITE-ProRule annotationAdd BLAST116

Phylogenomic databases

eggNOGiENOG4107MMM Bacteria
COG1366 LUCA
HOGENOMiHOG000269596
InParanoidiP42409
KOiK17763
OMAiNQYSISW
PhylomeDBiP42409

Family and domain databases

CDDicd01067 Globin_like, 1 hit
Gene3Di1.10.490.10, 1 hit
3.30.750.24, 1 hit
InterProiView protein in InterPro
IPR012292 Globin/Proto
IPR014792 RsbRA_N
IPR002645 STAS_dom
IPR036513 STAS_dom_sf
PfamiView protein in Pfam
PF08678 Rsbr_N, 1 hit
PF01740 STAS, 1 hit
SUPFAMiSSF52091 SSF52091, 1 hit
PROSITEiView protein in PROSITE
PS50801 STAS, 1 hit

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, NZ_JNCM01000031.1

Genome annotation databases

EnsemblBacteriaiCAB12274; CAB12274; BSU04670
GeneIDi938176
KEGGibsu:BSU04670
PATRICifig|224308.43.peg.487

Similar proteinsi

Entry informationi

Entry nameiRSBRA_BACSU
AccessioniPrimary (citable) accession number: P42409
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health