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P06628

- SP0F_BACSU

UniProt

P06628 - SP0F_BACSU

Protein

Sporulation initiation phosphotransferase F

Gene

spo0F

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.

    Cofactori

    Binds 1 magnesium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi10 – 101Magnesium
    Metal bindingi11 – 111Magnesium
    Metal bindingi54 – 541Magnesium
    Metal bindingi56 – 561Magnesium; via carbonyl oxygen

    GO - Molecular functioni

    1. kinase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. phosphorelay response regulator activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Sporulation, Two-component regulatory system

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU37130-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sporulation initiation phosphotransferase F (EC:2.7.-.-)
    Alternative name(s):
    Stage 0 sporulation protein F
    Gene namesi
    Name:spo0F
    Ordered Locus Names:BSU37130
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU37130. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 124124Sporulation initiation phosphotransferase FPRO_0000081244Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 5414-aspartylphosphate1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated by KinA and KinB. Dephosphorylated by RapA and RapB.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP06628.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    kinAP164972EBI-6418009,EBI-6405707

    Protein-protein interaction databases

    DIPiDIP-58965N.
    IntActiP06628. 3 interactions.
    STRINGi224308.BSU37130.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi13 – 2412
    Turni25 – 273
    Beta strandi29 – 357
    Helixi36 – 4611
    Beta strandi49 – 557
    Beta strandi58 – 603
    Helixi62 – 7211
    Beta strandi77 – 848
    Helixi87 – 9610
    Beta strandi101 – 1055
    Helixi108 – 11811
    Beta strandi122 – 1243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F51X-ray3.00E/F/G/H3-121[»]
    1FSPNMR-A1-124[»]
    1NATX-ray2.45A1-124[»]
    1PEYX-ray2.25A/B/C1-124[»]
    1PUXNMR-A1-124[»]
    1SRRX-ray1.90A/B/C1-124[»]
    2FSPNMR-A1-124[»]
    2FTKX-ray3.05E/F/G/H1-124[»]
    2JVINMR-A1-124[»]
    2JVJNMR-A1-124[»]
    2JVKNMR-A1-124[»]
    3Q15X-ray2.19C/D1-124[»]
    ProteinModelPortaliP06628.
    SMRiP06628. Positions 4-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06628.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119Response regulatoryPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 response regulatory domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0784.
    HOGENOMiHOG000034820.
    KOiK02490.
    OMAiIRVIIMT.
    OrthoDBiEOG6WHNMG.
    PhylomeDBiP06628.

    Family and domain databases

    InterProiIPR011006. CheY-like_superfamily.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view]
    PfamiPF00072. Response_reg. 1 hit.
    [Graphical view]
    SMARTiSM00448. REC. 1 hit.
    [Graphical view]
    SUPFAMiSSF52172. SSF52172. 1 hit.
    PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06628-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMNEKILIVD DQYGIRILLN EVFNKEGYQT FQAANGLQAL DIVTKERPDL    50
    VLLDMKIPGM DGIEILKRMK VIDENIRVII MTAYGELDMI QESKELGALT 100
    HFAKPFDIDE IRDAVKKYLP LKSN 124
    Length:124
    Mass (Da):14,228
    Last modified:January 1, 1988 - v1
    Checksum:i4130377E3558D698
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03497 Genomic DNA. Translation: CAA27217.1.
    M11081 Genomic DNA. Translation: AAA22787.1.
    M22039 Unassigned DNA. Translation: AAA16802.1.
    Z49782 Genomic DNA. Translation: CAA89872.1.
    AL009126 Genomic DNA. Translation: CAB15730.1.
    PIRiA24737. SZBS0F.
    RefSeqiNP_391594.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15730; CAB15730; BSU37130.
    GeneIDi937041.
    KEGGibsu:BSU37130.
    PATRICi18979462. VBIBacSub10457_3893.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03497 Genomic DNA. Translation: CAA27217.1 .
    M11081 Genomic DNA. Translation: AAA22787.1 .
    M22039 Unassigned DNA. Translation: AAA16802.1 .
    Z49782 Genomic DNA. Translation: CAA89872.1 .
    AL009126 Genomic DNA. Translation: CAB15730.1 .
    PIRi A24737. SZBS0F.
    RefSeqi NP_391594.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F51 X-ray 3.00 E/F/G/H 3-121 [» ]
    1FSP NMR - A 1-124 [» ]
    1NAT X-ray 2.45 A 1-124 [» ]
    1PEY X-ray 2.25 A/B/C 1-124 [» ]
    1PUX NMR - A 1-124 [» ]
    1SRR X-ray 1.90 A/B/C 1-124 [» ]
    2FSP NMR - A 1-124 [» ]
    2FTK X-ray 3.05 E/F/G/H 1-124 [» ]
    2JVI NMR - A 1-124 [» ]
    2JVJ NMR - A 1-124 [» ]
    2JVK NMR - A 1-124 [» ]
    3Q15 X-ray 2.19 C/D 1-124 [» ]
    ProteinModelPortali P06628.
    SMRi P06628. Positions 4-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-58965N.
    IntActi P06628. 3 interactions.
    STRINGi 224308.BSU37130.

    Chemistry

    BindingDBi P06628.
    ChEMBLi CHEMBL2111331.

    Proteomic databases

    PaxDbi P06628.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15730 ; CAB15730 ; BSU37130 .
    GeneIDi 937041.
    KEGGi bsu:BSU37130.
    PATRICi 18979462. VBIBacSub10457_3893.

    Organism-specific databases

    GenoListi BSU37130. [Micado ]

    Phylogenomic databases

    eggNOGi COG0784.
    HOGENOMi HOG000034820.
    KOi K02490.
    OMAi IRVIIMT.
    OrthoDBi EOG6WHNMG.
    PhylomeDBi P06628.

    Enzyme and pathway databases

    BioCyci BSUB:BSU37130-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06628.

    Family and domain databases

    InterProi IPR011006. CheY-like_superfamily.
    IPR001789. Sig_transdc_resp-reg_receiver.
    [Graphical view ]
    Pfami PF00072. Response_reg. 1 hit.
    [Graphical view ]
    SMARTi SM00448. REC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52172. SSF52172. 1 hit.
    PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Revised assignment for the Bacillus subtilis spo0F gene and its homology with spo0A and with two Escherichia coli genes."
      Yoshikawa H., Kazami J., Yamashita S., Chibazakura T., Sone H., Kawamura F., Oda M., Isaka M., Kobayashi Y., Saito H.
      Nucleic Acids Res. 14:1063-1072(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Deduced product of the stage 0 sporulation gene spo0F shares homology with the Spo0A, OmpR, and SfrA proteins."
      Trach K.A., Chapman J.W., Piggot P.J., Hoch J.A.
      Proc. Natl. Acad. Sci. U.S.A. 82:7260-7264(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    3. "Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome."
      Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.
      J. Bacteriol. 170:4194-4208(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    4. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    5. "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.
    6. "1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR."
      Feher V.A., Zapf J.W., Hoch J.A., Dahlquist F.W., Whiteley J.M., Cavanagh J.
      Protein Sci. 4:1801-1814(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    7. "High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition."
      Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntosh L.P., Rance M., Skelton N.J., Dahlquist F.W., Cavanagh J.
      Biochemistry 36:10015-10025(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, PHOSPHORYLATION AT ASP-54.
    8. "Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis."
      Madhusudan X., Zapf J., Whiteley J.M., Hoch J.A., Xuong N.H., Varughese K.I.
      Structure 4:679-690(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-13.
    9. "A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis."
      Madhusudan X., Zapf J., Hoch J.A., Whiteley J.M., Xuong N.H., Varughese K.I.
      Biochemistry 36:12739-12745(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
    10. "A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction."
      Zapf J., Sen U., Madhusudan X., Hoch J.A., Varughese K.I.
      Structure 8:851-862(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiSP0F_BACSU
    AccessioniPrimary (citable) accession number: P06628
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 128 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