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P06628 (SP0F_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sporulation initiation phosphotransferase F

EC=2.7.-.-
Alternative name(s):
Stage 0 sporulation protein F
Gene names
Name:spo0F
Ordered Locus Names:BSU37130
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

Binds 1 magnesium ion per subunit.

Subcellular location

Cytoplasm Probable.

Post-translational modification

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

Sequence similarities

Contains 1 response regulatory domain.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

kinAP164972EBI-6418009,EBI-6405707

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 124124Sporulation initiation phosphotransferase F
PRO_0000081244

Regions

Domain1 – 119119Response regulatory

Sites

Metal binding101Magnesium
Metal binding111Magnesium
Metal binding541Magnesium
Metal binding561Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue5414-aspartylphosphate

Secondary structure

........................ 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06628 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 4130377E3558D698

FASTA12414,228
        10         20         30         40         50         60 
MMNEKILIVD DQYGIRILLN EVFNKEGYQT FQAANGLQAL DIVTKERPDL VLLDMKIPGM 

        70         80         90        100        110        120 
DGIEILKRMK VIDENIRVII MTAYGELDMI QESKELGALT HFAKPFDIDE IRDAVKKYLP 


LKSN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRSZBS0F. A24737.
RefSeqNP_391594.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP06628.
SMRP06628. Positions 4-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58965N.
IntActP06628. 3 interactions.
STRING224308.BSU37130.

Chemistry

BindingDBP06628.
ChEMBLCHEMBL2111331.

Proteomic databases

PaxDbP06628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15730; CAB15730; BSU37130.
GeneID937041.
KEGGbsu:BSU37130.
PATRIC18979462. VBIBacSub10457_3893.

Organism-specific databases

GenoListBSU37130. [Micado]

Phylogenomic databases

eggNOGCOG0784.
HOGENOMHOG000034820.
KOK02490.
OMAIRVIIMT.
OrthoDBEOG6WHNMG.
ProtClustDBCLSK873695.

Enzyme and pathway databases

BioCycBSUB:BSU37130-MONOMER.

Family and domain databases

InterProIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52172. SSF52172. 1 hit.
PROSITEPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06628.

Entry information

Entry nameSP0F_BACSU
AccessionPrimary (citable) accession number: P06628
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList