Reviewed, UniProtKB/Swiss-Prot P40399 (RSBU_BACSU)

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW phosphoserine phosphatase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 335

335

Phosphoserine phosphatase rsbU

PRO_0000057790

Regions

Domain

131 – 335

205

PP2C-like

Experimental info

Sequence conflict

323

1

H → Q Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

335

Helix Strand Turn

Details...

Helix

2 – 21

20

Helix

24 – 39

16

Helix

44 – 58

15

Helix

64 – 83

20

Sequences

	Sequence		Length	Mass (Da)
	P40399-1 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: 5BD37C05B1A930E3	FASTA	335	38,631
	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

References

	« Hide 'large scale' referencesShow '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: 8002610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg.
[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: 8002609] [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: 9384377] [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: 8824586] [Abstract] Cited for: FUNCTION. Strain: 168 / Marburg.
[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: 9786195] [Abstract] Cited for: ENZYME REGULATION. Strain: 168 / Marburg.
[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: 12499568] [Abstract] Cited for: CRYSTALLIZATION OF N-TERMINAL DOMAIN, PROTEIN SEQUENCE OF 112-121.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

H69701.

RefSeq

NP_388351.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:410N.

Protein family/group databases

PptaseDB

P3D0406128.

Genome annotation databases

GeneID

939939.

GenomeReviews

Gene locus BSU04700 in contig AL009126_GR.

KEGG

bsu:BSU04700.

NMPDR

fig|224308.1.peg.470.

Organism-specific databases

SubtiList

BG11057. rsbU. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P40399.

OMA

MFITMFY.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU0470-MON.

BRENDA

3.1.3.3. 150.

Family and domain databases

InterPro

IPR017944. KaiA/RbsU_helical_domain.
IPR001932. PP2C-related.
IPR014787. PSer_Pase_RsbU_N.
IPR010822. Spore_II_E_C.
[Graphical view]

Gene3D

G3DSA:1.10.1240.30. KaiA/RbsU_helical_dom. 1 hit.

Pfam

PF08673. RsbU_N. 1 hit.
PF07228. SpoIIE. 1 hit.
[Graphical view]

SMART

SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RSBU_BACSU

Accession

Primary (citable) accession number: P40399

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 15, 1998
Last modified:	November 3, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)