Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P17906

- RSBX_BACSU

UniProt

P17906 - RSBX_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoserine phosphatase RsbX

Gene

rsbX

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.4 Publications

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. response to heat Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciBSUB:BSU04740-MONOMER.

Protein family/group databases

PptaseDBiP3D0406129.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine phosphatase RsbX (EC:3.1.3.3)
Alternative name(s):
Sigma-B negative effector
Gene namesi
Name:rsbX
Ordered Locus Names:BSU04740
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU04740. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Phosphoserine phosphatase RsbXPRO_0000057791Add
BLAST

Proteomic databases

PaxDbiP17906.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU04740.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Beta strandi8 – 1710Combined sources
Beta strandi26 – 338Combined sources
Beta strandi35 – 4814Combined sources
Helixi49 – 6517Combined sources
Turni66 – 683Combined sources
Helixi71 – 8111Combined sources
Turni82 – 843Combined sources
Beta strandi88 – 969Combined sources
Turni97 – 1004Combined sources
Beta strandi101 – 1099Combined sources
Beta strandi111 – 1155Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi150 – 1545Combined sources
Helixi163 – 1697Combined sources
Helixi173 – 1797Combined sources
Helixi180 – 1834Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi191 – 1988Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3W40X-ray1.30A/B1-199[»]
3W41X-ray1.42A1-199[»]
3W42X-ray1.06A/B1-199[»]
3W43X-ray1.22A1-199[»]
3W44X-ray2.30A/B1-199[»]
3W45X-ray1.70A/B1-199[»]
ProteinModelPortaliP17906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 199178PP2C-likeAdd
BLAST

Sequence similaritiesi

Contains 1 PP2C-like domain.Curated

Phylogenomic databases

eggNOGiNOG07987.
HOGENOMiHOG000270275.
InParanoidiP17906.
KOiK05518.
OMAiRCNQAMK.
OrthoDBiEOG6K401B.
PhylomeDBiP17906.

Family and domain databases

InterProiIPR001932. PP2C-like_dom.
[Graphical view]
PfamiPF07228. SpoIIE. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.

Sequencei

Sequence statusi: Complete.

P17906-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIQVEENEHI QTLVYQLNKE GKSICGDSFF MKADDKELIC AVADGLGSGS
60 70 80 90 100
LANESSAAIK DLVENYASED VESIIERCNQ AMKNKRGATA SILKINFEQR
110 120 130 140 150
QFTYCSVGNV RFILHSPSGE SFYPLPISGY LSGKPQKYKT HTATYEKGSK
160 170 180 190
FIIHTDGLNV PDIRSHLKKG QSVEEISNSL KMYTTSRKDD LTYILGQLS
Length:199
Mass (Da):22,144
Last modified:November 1, 1990 - v1
Checksum:i2AAEFB96FB072E33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34995 Genomic DNA. Translation: AAA22714.1.
AB001488 Genomic DNA. Translation: BAA19311.1.
AL009126 Genomic DNA. Translation: CAB12281.1.
PIRiD36131.
RefSeqiNP_388355.1. NC_000964.3.
WP_003246608.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12281; CAB12281; BSU04740.
GeneIDi938155.
KEGGibsu:BSU04740.
PATRICi18972532. VBIBacSub10457_0494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34995 Genomic DNA. Translation: AAA22714.1 .
AB001488 Genomic DNA. Translation: BAA19311.1 .
AL009126 Genomic DNA. Translation: CAB12281.1 .
PIRi D36131.
RefSeqi NP_388355.1. NC_000964.3.
WP_003246608.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3W40 X-ray 1.30 A/B 1-199 [» ]
3W41 X-ray 1.42 A 1-199 [» ]
3W42 X-ray 1.06 A/B 1-199 [» ]
3W43 X-ray 1.22 A 1-199 [» ]
3W44 X-ray 2.30 A/B 1-199 [» ]
3W45 X-ray 1.70 A/B 1-199 [» ]
ProteinModelPortali P17906.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU04740.

Protein family/group databases

PptaseDBi P3D0406129.

Proteomic databases

PaxDbi P17906.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12281 ; CAB12281 ; BSU04740 .
GeneIDi 938155.
KEGGi bsu:BSU04740.
PATRICi 18972532. VBIBacSub10457_0494.

Organism-specific databases

GenoListi BSU04740. [Micado ]

Phylogenomic databases

eggNOGi NOG07987.
HOGENOMi HOG000270275.
InParanoidi P17906.
KOi K05518.
OMAi RCNQAMK.
OrthoDBi EOG6K401B.
PhylomeDBi P17906.

Enzyme and pathway databases

BioCyci BSUB:BSU04740-MONOMER.

Family and domain databases

InterProi IPR001932. PP2C-like_dom.
[Graphical view ]
Pfami PF07228. SpoIIE. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Similar organization of the sigB and spoIIA operons encoding alternate sigma factors of Bacillus subtilis RNA polymerase."
    Kalman S., Duncan M.L., Thomas S.M., Price C.W.
    J. Bacteriol. 172:5575-5585(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "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.
  3. "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.
  4. "Gene encoding the 37,000-dalton minor sigma factor of Bacillus subtilis RNA polymerase: isolation, nucleotide sequence, chromosomal locus, and cryptic function."
    Duncan M.L., Kalman S.S., Thomas S.M., Price C.W.
    J. Bacteriol. 169:771-778(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
    Strain: 168.
  5. "Activation of Bacillus subtilis transcription factor sigma B by a regulatory pathway responsive to stationary-phase signals."
    Boylan S.A., Rutherford A., Thomas S.M., Price C.W.
    J. Bacteriol. 174:3695-3706(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  6. "Regulation of sigma B levels and activity in Bacillus subtilis."
    Benson A.K., Haldenwang W.G.
    J. Bacteriol. 175:2347-2356(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: PY22.
  7. "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.
  8. "Isolation and characterization of Bacillus subtilis sigB operon mutations that suppress the loss of the negative regulator RsbX."
    Smirnova N., Scott J., Voelker U., Haldenwang W.G.
    J. Bacteriol. 180:3671-3680(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: PY22.

Entry informationi

Entry nameiRSBX_BACSU
AccessioniPrimary (citable) accession number: P17906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 114 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

3D-structure, Complete proteome, 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