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P06628

- SP0F_BACSU

UniProt

P06628 - SP0F_BACSU

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Protein
Sporulation initiation phosphotransferase F
Gene
spo0F, BSU37130
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 activityInferred from electronic annotationi Source: UniProtKB-KW
  2. metal ion bindingInferred from electronic annotationi Source: UniProtKB-KW
  3. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
  4. protein bindingInferred from physical interactioni PubMed 19040634 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. sporulation resulting in formation of a cellular sporeInferred from electronic annotationi Source: UniProtKB-KW
  1. kinase activityInferred from electronic annotationi Source: UniProtKB-KW
  2. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

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 Inferred

GO - Cellular componenti

  1. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Sporulation initiation phosphotransferase F
PRO_0000081244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphate

Post-translational modificationi

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

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

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.

Miscellaneous databases

EvolutionaryTraceiP06628.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 119119Response regulatory
Add
BLAST

Sequence similaritiesi

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]FASTA

« 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.
PIRiSZBS0F. A24737.
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 SZBS0F. A24737.
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...

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

« Hide 'large scale' publications
  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.
  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 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: July 9, 2014
This is version 127 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

External Data

Dasty 3

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