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Protein

Sporulation initiation phosphotransferase B

Gene

spo0B

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

Functioni

Key element in the phosphorelay regulating sporulation initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from spo0F to spo0A.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Sensory transduction, Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU27930-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation initiation phosphotransferase B (EC:2.7.-.-)
Alternative name(s):
Stage 0 sporulation protein B
Stage 0 sporulation protein D
Gene namesi
Name:spo0B
Synonyms:spo0D
Ordered Locus Names:BSU27930
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301H → A: Loss of sporulation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Sporulation initiation phosphotransferase BPRO_0000072052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphohistidine1 Publication

Post-translational modificationi

Phosphorylated by spo0F.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP06535.

PTM databases

iPTMnetiP06535.

Expressioni

Developmental stagei

Expressed during sporulation.

Interactioni

Subunit structurei

Homodimer. Dimerization is essential for activity as both monomers contribute to the formation of the active site.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015266.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 4430Combined sources
Helixi48 – 6922Combined sources
Turni70 – 723Combined sources
Helixi74 – 829Combined sources
Helixi83 – 853Combined sources
Beta strandi89 – 9911Combined sources
Turni104 – 1063Combined sources
Helixi107 – 12418Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi142 – 15413Combined sources
Helixi159 – 1613Combined sources
Helixi163 – 1664Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi182 – 19110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F51X-ray3.00A/B/C/D11-192[»]
1IXMX-ray2.60A/B1-192[»]
2FTKX-ray3.05A/B/C/D1-192[»]
ProteinModelPortaliP06535.
SMRiP06535. Positions 11-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06535.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000097276.
KOiK06375.
OMAiRHARHDW.
OrthoDBiEOG66F066.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.30. 1 hit.
InterProiIPR003661. HisK_dim/P.
IPR016120. Sig_transdc_His_kin_SpoOB.
IPR016122. SpoOB_C.
[Graphical view]
PfamiPF14682. SPOB_ab. 1 hit.
[Graphical view]
SMARTiSM01317. SPOB_ab. 1 hit.
[Graphical view]
SUPFAMiSSF55890. SSF55890. 1 hit.

Sequencei

Sequence statusi: Complete.

P06535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDVSKNQEE NISDTALTNE LIHLLGHSRH DWMNKLQLIK GNLSLQKYDR
60 70 80 90 100
VFEMIEEMVI DAKHESKLSN LKTPHLAFDF LTFNWKTHYM TLEYEVLGEI
110 120 130 140 150
KDLSAYDQKL AKLMRKLFHL FDQAVSRESE NHLTVSLQTD HPDRQLILYL
160 170 180 190
DFHGAFADPS AFDDIRQNGY EDVDIMRFEI TSHECLIEIG LD
Length:192
Mass (Da):22,543
Last modified:January 1, 1988 - v1
Checksum:i3A9A38B5FFB55647
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02655 Genomic DNA. Translation: CAA26489.1.
M24537 Genomic DNA. Translation: AAA22504.1.
K02664 Genomic DNA. Translation: AAB05348.1.
AL009126 Genomic DNA. Translation: CAB14753.1.
PIRiA22974. SZBS0B.
RefSeqiNP_390671.1. NC_000964.3.
WP_004399131.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14753; CAB14753; BSU27930.
GeneIDi935956.
KEGGibsu:BSU27930.
PATRICi18977456. VBIBacSub10457_2917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02655 Genomic DNA. Translation: CAA26489.1.
M24537 Genomic DNA. Translation: AAA22504.1.
K02664 Genomic DNA. Translation: AAB05348.1.
AL009126 Genomic DNA. Translation: CAB14753.1.
PIRiA22974. SZBS0B.
RefSeqiNP_390671.1. NC_000964.3.
WP_004399131.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F51X-ray3.00A/B/C/D11-192[»]
1IXMX-ray2.60A/B1-192[»]
2FTKX-ray3.05A/B/C/D1-192[»]
ProteinModelPortaliP06535.
SMRiP06535. Positions 11-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015266.

PTM databases

iPTMnetiP06535.

Proteomic databases

PaxDbiP06535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14753; CAB14753; BSU27930.
GeneIDi935956.
KEGGibsu:BSU27930.
PATRICi18977456. VBIBacSub10457_2917.

Phylogenomic databases

HOGENOMiHOG000097276.
KOiK06375.
OMAiRHARHDW.
OrthoDBiEOG66F066.

Enzyme and pathway databases

BioCyciBSUB:BSU27930-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP06535.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.30. 1 hit.
InterProiIPR003661. HisK_dim/P.
IPR016120. Sig_transdc_His_kin_SpoOB.
IPR016122. SpoOB_C.
[Graphical view]
PfamiPF14682. SPOB_ab. 1 hit.
[Graphical view]
SMARTiSM01317. SPOB_ab. 1 hit.
[Graphical view]
SUPFAMiSSF55890. SSF55890. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the spo0B locus reveals a polycistronic transcription unit."
    Ferrari F.A., Trach K.A., Hoch J.A.
    J. Bacteriol. 161:556-562(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein."
    Trach K., Hoch J.A.
    J. Bacteriol. 171:1362-1371(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence of the spo0B gene of Bacillus subtilis and regulation of its expression."
    Bouvier J., Stragier P., Bonamy C., Szulmajster J.
    Proc. Natl. Acad. Sci. U.S.A. 81:7012-7016(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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.
  5. "Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase."
    Varughese K.I., Madhusudan X., Zhou X.Z., Whiteley J.M., Hoch J.A.
    Mol. Cell 2:485-493(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  6. "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).
  7. "Phosphorylation of the Spo0B response regulator phosphotransferase of the phosphorelay initiating development in Bacillus subtilis."
    Tzeng Y.L., Zhou X.Z., Hoch J.A.
    J. Biol. Chem. 273:23849-23855(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT HIS-30, MUTAGENESIS OF HIS-30.

Entry informationi

Entry nameiSP0B_BACSU
AccessioniPrimary (citable) accession number: P06535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.