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Reviewed, UniProtKB/Swiss-Prot O34757 (DESK_BACSU)

Last modified January 19, 2010. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sensor histidine kinase desK
    EC=2.7.13.3
Gene names
Name: desK
Synonyms: yocF
Ordered Locus Names: BSU19190
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Member of the two-component regulatory system desR/desK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates desR by phosphorylation. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Contains 1 histidine kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Sensor histidine kinase desK
PRO_0000360780

Regions

Topological domain1 – 1010Extracellular Potential
Transmembrane11 – 3121 Potential
Topological domain32 – 365Cytoplasmic Potential
Transmembrane37 – 5721 Potential
Topological domain58 – 7013Extracellular Potential
Transmembrane71 – 9121 Potential
Topological domain92 – 10312Cytoplasmic Potential
Transmembrane104 – 12421 Potential
Topological domain125 – 1284Extracellular Potential
Transmembrane129 – 14921 Potential
Topological domain150 – 370221Cytoplasmic Potential
Domain186 – 369184Histidine kinase

Amino acid modifications

Modified residue1881Phosphohistidine; by autocatalysis By similarity

Secondary structure

................. 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34757-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3A22FD6A3630A13D

FASTA37042,673
        10         20         30         40         50         60 
MIKNHFTFQK LNGITPYIWT IFFILPFYFI WKSSSTFVII VGIILTLLFF SVYRFAFVSK 

        70         80         90        100        110        120 
GWTIYLWGFL LIGISTASIT LFSYIYFAFF IAYFIGNIKE RVPFHILYYV HLISAAVAAN 

       130        140        150        160        170        180 
FSLVLKKEFF LTQIPFVVIT LISAILLPFS IKSRKERERL EEKLEDANER IAELVKLEER 

       190        200        210        220        230        240 
QRIARDLHDT LGQKLSLIGL KSDLARKLIY KDPEQAAREL KSVQQTARTS LNEVRKIVSS 

       250        260        270        280        290        300 
MKGIRLKDEL INIKQILEAA DIMFIYEEEK WPENISLLNE NILSMCLKEA VTNVVKHSQA 

       310        320        330        340        350        360 
KTCRVDIQQL WKEVVITVSD DGTFKGEENS FSKGHGLLGM RERLEFANGS LHIDTENGTK 

       370 
LTMAIPNNSK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis."
Aguilar P.S., Hernandez-Arriaga A.M., Cybulski L.E., Erazo A.C., de Mendoza D.
EMBO J. 20:1681-1691(2001) [PubMed: 11285232] [Abstract]
Cited for: FUNCTION.
[4]"Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems."
Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y.
J. Bacteriol. 183:7365-7370(2001) [PubMed: 11717295] [Abstract]
Cited for: FUNCTION, GENE NAME.
[5]"Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase."
Cybulski L.E., Albanesi D., Mansilla M.C., Altabe S., Aguilar P.S., de Mendoza D.
Mol. Microbiol. 45:1379-1388(2002) [PubMed: 12207704] [Abstract]
Cited for: FUNCTION.
[6]"Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK."
Hunger K., Beckering C.L., Marahiel M.A.
FEMS Microbiol. Lett. 230:41-46(2004) [PubMed: 14734164] [Abstract]
Cited for: FUNCTION.
[7]"The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator."
Albanesi D., Mansilla M.C., de Mendoza D.
J. Bacteriol. 186:2655-2663(2004) [PubMed: 15090506] [Abstract]
Cited for: FUNCTION.
[8]"The Bacillus subtilis desaturase: a model to understand phospholipid modification and temperature sensing."
Mansilla M.C., de Mendoza D.
Arch. Microbiol. 183:229-235(2005) [PubMed: 15711796] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027868 Genomic DNA. Translation: AAB84437.1.
AL009126 Genomic DNA. Translation: CAB13811.1.
PIRC69901.
RefSeqNP_389800.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EHFX-ray3.10A/B/C/D175-370[»]
3EHGX-ray1.74A243-370[»]
3EHHX-ray2.10A/B154-370[»]
3EHJX-ray2.50A/B154-370[»]
3GIEX-ray2.65A/B154-370[»]
3GIFX-ray2.70A/B154-370[»]
3GIGX-ray3.50A/B154-370[»]
ModBaseSearch...

Genome annotation databases

GeneID939678.
GenomeReviewsGene locus BSU19190 in contig AL009126_GR.
KEGGbsu:BSU19190.
NMPDRfig|224308.1.peg.1923.

Organism-specific databases

SubtiListBG13519. desK. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG700937.
OMALESTASM.

Enzyme and pathway databases

BioCycSUBTI:BSU19190-MONOMER.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
[Graphical view]
PfamPF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view]
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
PROSITEPS50109. HIS_KIN. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDESK_BACSU
AccessionPrimary (citable) accession number: O34757
Secondary accession number(s): Q796C8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 19, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents