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Protein

Serine/threonine-protein kinase RsbT

Gene

rsbT

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity of the RsbU phosphatase may be stimulated by a long-lived interaction with RsbT and the serine kinase function of RsbT is not required to directly modify RsbU. Also phosphorylates RsbR thanks to its threonine kinase activity, preventing it to phosphorylate RsbT.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU04690-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RsbT (EC:2.7.11.1)
Alternative name(s):
Anti-sigma-B factor RsbT
Switch protein/serine kinase
Gene namesi
Name:rsbT
Synonyms:ycxT
Ordered Locus Names:BSU04690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781D → N: Loss of kinase activity towards RsbS. Loss of the ability to activate sigma-B in response to salt and ethanol stress while retaining the ability to respond to energy stress. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133Serine/threonine-protein kinase RsbTPRO_0000097472Add
BLAST

Proteomic databases

PaxDbiP42411.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rsbSP424102EBI-5247957,EBI-5247936
ybdMO314353EBI-5247957,EBI-5255200

Protein-protein interaction databases

DIPiDIP-402N.
IntActiP42411. 7 interactions.
STRINGi224308.Bsubs1_010100002653.

Structurei

3D structure databases

ProteinModelPortaliP42411.
SMRiP42411. Positions 34-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105QD0. Bacteria.
COG2172. LUCA.
HOGENOMiHOG000269930.
InParanoidiP42411.
KOiK17752.
OMAiRNTLVHG.
PhylomeDBiP42411.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
[Graphical view]
PfamiPF13581. HATPase_c_2. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.

Sequencei

Sequence statusi: Complete.

P42411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDQSCVRIM TEWDIVAARQ LGRNVAKELG FGTVDQARIT TAISELARNI
60 70 80 90 100
YLYAGKGQIG IEQVADRGKK GLKIIAEDQG PGIPDIRKVM EDGFSTSGGL
110 120 130
GAGLPGVKRL MDEFSLNSVA GEGTEIQAIK WLR
Length:133
Mass (Da):14,349
Last modified:November 1, 1995 - v1
Checksum:iB9B5CF507F747F7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85082.1.
AB001488 Genomic DNA. Translation: BAA19306.1.
AL009126 Genomic DNA. Translation: CAB12276.1.
X81652 Genomic DNA. No translation available.
PIRiG69701.
RefSeqiNP_388350.1. NC_000964.3.
WP_003246640.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12276; CAB12276; BSU04690.
GeneIDi938168.
KEGGibsu:BSU04690.
PATRICi18972522. VBIBacSub10457_0489.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85082.1.
AB001488 Genomic DNA. Translation: BAA19306.1.
AL009126 Genomic DNA. Translation: CAB12276.1.
X81652 Genomic DNA. No translation available.
PIRiG69701.
RefSeqiNP_388350.1. NC_000964.3.
WP_003246640.1. NZ_JNCM01000031.1.

3D structure databases

ProteinModelPortaliP42411.
SMRiP42411. Positions 34-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-402N.
IntActiP42411. 7 interactions.
STRINGi224308.Bsubs1_010100002653.

Proteomic databases

PaxDbiP42411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12276; CAB12276; BSU04690.
GeneIDi938168.
KEGGibsu:BSU04690.
PATRICi18972522. VBIBacSub10457_0489.

Phylogenomic databases

eggNOGiENOG4105QD0. Bacteria.
COG2172. LUCA.
HOGENOMiHOG000269930.
InParanoidiP42411.
KOiK17752.
OMAiRNTLVHG.
PhylomeDBiP42411.

Enzyme and pathway databases

BioCyciBSUB:BSU04690-MONOMER.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
[Graphical view]
PfamiPF13581. HATPase_c_2. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRSBT_BACSU
AccessioniPrimary (citable) accession number: P42411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 104 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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.