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Protein

Phosphoserine phosphatase RsbU

Gene

rsbU

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

Functioni

Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.1 Publication

Catalytic activityi

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.

Enzyme regulationi

Stimulated by a long-lived interaction with RsbT.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciBSUB:BSU04700-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine phosphatase RsbU (EC:3.1.3.3)
Alternative name(s):
Sigma factor SigB regulation protein RsbU
Gene namesi
Name:rsbU
Ordered Locus Names:BSU04700
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU04700. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Phosphoserine phosphatase RsbUPRO_0000057790Add
BLAST

Proteomic databases

PaxDbiP40399.

Interactioni

Protein-protein interaction databases

DIPiDIP-410N.
STRINGi224308.Bsubs1_010100002658.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2120Combined sources
Helixi24 – 3916Combined sources
Helixi44 – 5815Combined sources
Helixi64 – 8320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W53X-ray1.60A1-84[»]
2J6YX-ray1.85A/B/C/D/E1-111[»]
2J6ZX-ray1.95A1-111[»]
2J70X-ray1.95A1-111[»]
ProteinModelPortaliP40399.
SMRiP40399. Positions 1-84, 107-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40399.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini123 – 333211PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2208.
HOGENOMiHOG000269934.
InParanoidiP40399.
KOiK07315.
OMAiFQLRDDF.
OrthoDBiEOG6ZH2CT.
PhylomeDBiP40399.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR017944. KaiA/RbsU_helical_domain.
IPR001932. PPM-type_phosphatase_dom.
IPR014787. PSer_Pase_RsbU_N.
[Graphical view]
PfamiPF08673. RsbU_N. 1 hit.
PF07228. SpoIIE. 1 hit.
[Graphical view]
ProDomiPD685490. PSer_Pase_RsbU_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF101215. SSF101215. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFREVIEQR YHQLLSRYIA ELTETSLYQA QKFSRKTIEH QIPPEEIISI
60 70 80 90 100
HRKVLKELYP SLPEDVFHSL DFLIEVMIGY GMAYQEHQTL RGIQQEIKSE
110 120 130 140 150
IEIAANVQQT LLGTKVPQEE ALDIGAISVP AKQMSGDYYH FVKDKESINI
160 170 180 190 200
AIADVIGKGI PAALCMSMIK YAMDSLPETG IHPSQVLKNL NRVVEQNVDA
210 220 230 240 250
SMFITMFYAN YNMDKHQFTY ASAGHEPGFY YSQKDNTFYD LEAKGLVLGI
260 270 280 290 300
SQDYDYKQFD QHLEKGDMIV LFSDGVTECR TENGFLERPD LQKLIEEHMC
310 320 330
SSAQEMVKNI YDSLLKLQDF QLHDDFTLIV LRRKV
Length:335
Mass (Da):38,631
Last modified:July 15, 1998 - v3
Checksum:i5BD37C05B1A930E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti323 – 3231H → Q (PubMed:8002610).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85083.1.
X81652 Genomic DNA. Translation: CAB57214.1. Sequence problems.
AB001488 Genomic DNA. Translation: BAA19307.1.
AL009126 Genomic DNA. Translation: CAB12277.1.
PIRiH69701.
RefSeqiNP_388351.1. NC_000964.3.
WP_003234295.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12277; CAB12277; BSU04700.
GeneIDi939939.
KEGGibsu:BSU04700.
PATRICi18972524. VBIBacSub10457_0490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35574 Genomic DNA. Translation: AAA85083.1.
X81652 Genomic DNA. Translation: CAB57214.1. Sequence problems.
AB001488 Genomic DNA. Translation: BAA19307.1.
AL009126 Genomic DNA. Translation: CAB12277.1.
PIRiH69701.
RefSeqiNP_388351.1. NC_000964.3.
WP_003234295.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W53X-ray1.60A1-84[»]
2J6YX-ray1.85A/B/C/D/E1-111[»]
2J6ZX-ray1.95A1-111[»]
2J70X-ray1.95A1-111[»]
ProteinModelPortaliP40399.
SMRiP40399. Positions 1-84, 107-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-410N.
STRINGi224308.Bsubs1_010100002658.

Proteomic databases

PaxDbiP40399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12277; CAB12277; BSU04700.
GeneIDi939939.
KEGGibsu:BSU04700.
PATRICi18972524. VBIBacSub10457_0490.

Organism-specific databases

GenoListiBSU04700. [Micado]

Phylogenomic databases

eggNOGiCOG2208.
HOGENOMiHOG000269934.
InParanoidiP40399.
KOiK07315.
OMAiFQLRDDF.
OrthoDBiEOG6ZH2CT.
PhylomeDBiP40399.

Enzyme and pathway databases

BioCyciBSUB:BSU04700-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40399.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR017944. KaiA/RbsU_helical_domain.
IPR001932. PPM-type_phosphatase_dom.
IPR014787. PSer_Pase_RsbU_N.
[Graphical view]
PfamiPF08673. RsbU_N. 1 hit.
PF07228. SpoIIE. 1 hit.
[Graphical view]
ProDomiPD685490. PSer_Pase_RsbU_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF101215. SSF101215. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sigma B in response to environmental signals."
    Wise A.A., Price C.W.
    J. Bacteriol. 177:123-133(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  2. "The Bacillus subtilis rsbU gene product is necessary for RsbX-dependent regulation of sigma B."
    Voelker U., Dufour A., Haldenwang W.G.
    J. Bacteriol. 177:114-122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / BSA46.
  3. "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome."
    Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  5. "Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor."
    Yang X., Kang C.M., Brody M.S., Price C.W.
    Genes Dev. 10:2265-2275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  6. "Serine kinase activity of a Bacillus subtilis switch protein is required to transduce environmental stress signals but not to activate its target PP2C phosphatase."
    Kang C.M., Vijay K., Price C.W.
    Mol. Microbiol. 30:189-196(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  7. "Crystallization and preliminary crystallographic analysis of the kinase-recruitment domain of the PP2C-type phosphatase RsbU."
    Dutta S., Lewis R.J.
    Acta Crystallogr. D 59:191-193(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION OF N-TERMINAL DOMAIN, PROTEIN SEQUENCE OF 112-121.

Entry informationi

Entry nameiRSBU_BACSU
AccessioniPrimary (citable) accession number: P40399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: July 22, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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 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.