O34757 (DESK_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sensor histidine kinase desK
EC=2.7.13.3

Gene names

Name:	desK
Synonyms:	yocF
Ordered Locus Names:	BSU19190

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein dimerization activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 370

370

Sensor histidine kinase desK

PRO_0000360780

Regions

Topological domain

1 – 10

10

Extracellular Potential

Transmembrane

11 – 31

21

Helical; Potential

Topological domain

32 – 36

5

Cytoplasmic Potential

Transmembrane

37 – 57

21

Helical; Potential

Topological domain

58 – 70

13

Extracellular Potential

Transmembrane

71 – 91

21

Helical; Potential

Topological domain

92 – 103

12

Cytoplasmic Potential

Transmembrane

104 – 124

21

Helical; Potential

Topological domain

125 – 128

4

Extracellular Potential

Transmembrane

129 – 149

21

Helical; Potential

Topological domain

150 – 370

221

Cytoplasmic Potential

Domain

186 – 369

184

Histidine kinase

Amino acid modifications

Modified residue

188

1

Phosphohistidine; by autocatalysis By similarity

Secondary structure

1

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370

Helix Strand Turn

Details...

Helix

246 – 259

14

Beta strand

263 – 265

3

Helix

277 – 297

21

Beta strand

301 – 310

10

Beta strand

313 – 320

8

Helix

341 – 346

6

Beta strand

351 – 354

4

Beta strand

360 – 366

7

Sequences

	Sequence		Length	Mass (Da)
	O34757 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 3A22FD6A3630A13D	FASTA	370	42,673
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

C69901.

RefSeq

NP_389800.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EHF	X-ray	3.10	A/B/C/D	175-370	[»]
3EHG	X-ray	1.74	A	243-370	[»]
3EHH	X-ray	2.10	A/B	154-370	[»]
3EHJ	X-ray	2.50	A/B	154-370	[»]
3GIE	X-ray	2.65	A/B	154-370	[»]
3GIF	X-ray	2.70	A/B	154-370	[»]
3GIG	X-ray	3.50	A/B	154-370	[»]

ProteinModelPortal

O34757.

SMR

O34757. Positions 164-368.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48966N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002836; EBBACP00000002836; EBBACG00000002831.

GeneID

939678.

GenomeReviews

Gene locus BSU19190 in contig AL009126_GR.

KEGG

bsu:BSU19190.

NMPDR

fig|224308.1.peg.1923.

PATRIC

18975687. VBIBacSub10457_2034.

Organism-specific databases

GenoList

BSU19190. [Micado]

Phylogenomic databases

GeneTree

EBGT00070000031823.

HOGENOM

HBG700937.

OMA

WTIFFIL.

PhylomeDB

O34757.

ProtClustDB

CLSK887413.

Enzyme and pathway databases

BioCyc

BSUB:BSU19190-MONOMER.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.

KO

K07778.

Pfam

PF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view]

SMART

SM00387. HATPase_c. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.

PROSITE

PS50109. HIS_KIN. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DESK_BACSU

Accession

Primary (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 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program