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P17906

- RSBX_BACSU

UniProt

P17906 - RSBX_BACSU

Protein

Phosphoserine phosphatase RsbX

Gene

rsbX

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    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

    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 – 65
    Beta strandi8 – 1710
    Beta strandi26 – 338
    Beta strandi35 – 4814
    Helixi49 – 6517
    Turni66 – 683
    Helixi71 – 8111
    Turni82 – 843
    Beta strandi88 – 969
    Turni97 – 1004
    Beta strandi101 – 1099
    Beta strandi111 – 1155
    Beta strandi127 – 1293
    Beta strandi140 – 1445
    Beta strandi150 – 1545
    Helixi163 – 1697
    Helixi173 – 1797
    Helixi180 – 1834
    Beta strandi184 – 1863
    Beta strandi191 – 1988

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MIQVEENEHI QTLVYQLNKE GKSICGDSFF MKADDKELIC AVADGLGSGS    50
    LANESSAAIK DLVENYASED VESIIERCNQ AMKNKRGATA SILKINFEQR 100
    QFTYCSVGNV RFILHSPSGE SFYPLPISGY LSGKPQKYKT HTATYEKGSK 150
    FIIHTDGLNV PDIRSHLKKG QSVEEISNSL KMYTTSRKDD LTYILGQLS 199
    Length:199
    Mass (Da):22,144
    Last modified:November 1, 1990 - v1
    Checksum:i2AAEFB96FB072E33
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 112 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