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P40399

- RSBU_BACSU

UniProt

P40399 - RSBU_BACSU

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Protein

Phosphoserine phosphatase RsbU

Gene

rsbU

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

  1. phosphoprotein phosphatase activity Source: UniProtKB-KW
  2. phosphoserine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciBSUB:BSU04700-MONOMER.

Protein family/group databases

PptaseDBiP3D0406128.

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: 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.BSU04700.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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
Domaini131 – 335205PP2C-likeAdd
BLAST

Sequence similaritiesi

Contains 1 PP2C-like domain.Curated

Phylogenomic databases

eggNOGiCOG2208.
HOGENOMiHOG000269934.
InParanoidiP40399.
KOiK07315.
OMAiSIHRKVL.
OrthoDBiEOG6ZH2CT.
PhylomeDBiP40399.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR017944. KaiA/RbsU_helical_domain.
IPR001932. PP2C-like_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.

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:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi H69701.
RefSeqi NP_388351.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W53 X-ray 1.60 A 1-84 [» ]
2J6Y X-ray 1.85 A/B/C/D/E 1-111 [» ]
2J6Z X-ray 1.95 A 1-111 [» ]
2J70 X-ray 1.95 A 1-111 [» ]
ProteinModelPortali P40399.
SMRi P40399. Positions 1-84, 107-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-410N.
STRINGi 224308.BSU04700.

Protein family/group databases

PptaseDBi P3D0406128.

Proteomic databases

PaxDbi P40399.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12277 ; CAB12277 ; BSU04700 .
GeneIDi 939939.
KEGGi bsu:BSU04700.
PATRICi 18972524. VBIBacSub10457_0490.

Organism-specific databases

GenoListi BSU04700. [Micado ]

Phylogenomic databases

eggNOGi COG2208.
HOGENOMi HOG000269934.
InParanoidi P40399.
KOi K07315.
OMAi SIHRKVL.
OrthoDBi EOG6ZH2CT.
PhylomeDBi P40399.

Enzyme and pathway databases

BioCyci BSUB:BSU04700-MONOMER.

Miscellaneous databases

EvolutionaryTracei P40399.

Family and domain databases

Gene3Di 1.10.1240.30. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR017944. KaiA/RbsU_helical_domain.
IPR001932. PP2C-like_dom.
IPR014787. PSer_Pase_RsbU_N.
[Graphical view ]
Pfami PF08673. RsbU_N. 1 hit.
PF07228. SpoIIE. 1 hit.
[Graphical view ]
ProDomi PD685490. PSer_Pase_RsbU_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF101215. SSF101215. 1 hit.
SSF81606. SSF81606. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 118 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