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P40399 (RSBU_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoserine phosphatase RsbU

EC=3.1.3.3
Alternative name(s):
Sigma factor SigB regulation protein RsbU
Gene names
Name:rsbU
Ordered Locus Names:BSU04700
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module. Ref.5

Catalytic activity

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

Enzyme regulation

Stimulated by a long-lived interaction with RsbT. Ref.6

Sequence similarities

Contains 1 PP2C-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Phosphoserine phosphatase RsbU
PRO_0000057790

Regions

Domain131 – 335205PP2C-like

Experimental info

Sequence conflict3231H → Q Ref.1

Secondary structure

......... 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40399 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: 5BD37C05B1A930E3

FASTA33538,631
        10         20         30         40         50         60 
MDFREVIEQR YHQLLSRYIA ELTETSLYQA QKFSRKTIEH QIPPEEIISI HRKVLKELYP 

        70         80         90        100        110        120 
SLPEDVFHSL DFLIEVMIGY GMAYQEHQTL RGIQQEIKSE IEIAANVQQT LLGTKVPQEE 

       130        140        150        160        170        180 
ALDIGAISVP AKQMSGDYYH FVKDKESINI AIADVIGKGI PAALCMSMIK YAMDSLPETG 

       190        200        210        220        230        240 
IHPSQVLKNL NRVVEQNVDA SMFITMFYAN YNMDKHQFTY ASAGHEPGFY YSQKDNTFYD 

       250        260        270        280        290        300 
LEAKGLVLGI SQDYDYKQFD QHLEKGDMIV LFSDGVTECR TENGFLERPD LQKLIEEHMC 

       310        320        330 
SSAQEMVKNI YDSLLKLQDF QLHDDFTLIV LRRKV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRH69701.
RefSeqNP_388351.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W53X-ray1.60A1-84[»]
2J6YX-ray1.85A/B/C/D/E1-111[»]
2J6ZX-ray1.95A1-111[»]
2J70X-ray1.95A1-111[»]
ProteinModelPortalP40399.
SMRP40399. Positions 1-84, 107-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-410N.
STRING224308.BSU04700.

Protein family/group databases

PptaseDBP3D0406128.

Proteomic databases

PaxDbP40399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12277; CAB12277; BSU04700.
GeneID939939.
KEGGbsu:BSU04700.
PATRIC18972524. VBIBacSub10457_0490.

Organism-specific databases

GenoListBSU04700. [Micado]

Phylogenomic databases

eggNOGCOG2208.
HOGENOMHOG000269934.
KOK07315.
OMASIHRKVL.
OrthoDBEOG6ZH2CT.
PhylomeDBP40399.

Enzyme and pathway databases

BioCycBSUB:BSU04700-MONOMER.

Family and domain databases

Gene3D1.10.1240.30. 1 hit.
3.60.40.10. 1 hit.
InterProIPR017944. KaiA/RbsU_helical_domain.
IPR001932. PP2C-like_dom.
IPR014787. PSer_Pase_RsbU_N.
[Graphical view]
PfamPF08673. RsbU_N. 1 hit.
PF07228. SpoIIE. 1 hit.
[Graphical view]
ProDomPD685490. PSer_Pase_RsbU_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF101215. SSF101215. 1 hit.
SSF81606. SSF81606. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40399.

Entry information

Entry nameRSBU_BACSU
AccessionPrimary (citable) accession number: P40399
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

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