DESK_BACSU
ID DESK_BACSU Reviewed; 370 AA.
AC O34757; Q796C8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sensor histidine kinase DesK;
DE EC=2.7.13.3;
GN Name=desK; Synonyms=yocF; OrderedLocusNames=BSU19190;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION.
RX PubMed=11285232; DOI=10.1093/emboj/20.7.1681;
RA Aguilar P.S., Hernandez-Arriaga A.M., Cybulski L.E., Erazo A.C.,
RA de Mendoza D.;
RT "Molecular basis of thermosensing: a two-component signal transduction
RT thermometer in Bacillus subtilis.";
RL EMBO J. 20:1681-1691(2001).
RN [4]
RP FUNCTION, AND GENE NAME.
RX PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA Fujita Y.;
RT "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT regulatory systems.";
RL J. Bacteriol. 183:7365-7370(2001).
RN [5]
RP FUNCTION.
RX PubMed=12207704; DOI=10.1046/j.1365-2958.2002.03103.x;
RA Cybulski L.E., Albanesi D., Mansilla M.C., Altabe S., Aguilar P.S.,
RA de Mendoza D.;
RT "Mechanism of membrane fluidity optimization: isothermal control of the
RT Bacillus subtilis acyl-lipid desaturase.";
RL Mol. Microbiol. 45:1379-1388(2002).
RN [6]
RP FUNCTION.
RX PubMed=14734164; DOI=10.1016/s0378-1097(03)00852-8;
RA Hunger K., Beckering C.L., Marahiel M.A.;
RT "Genetic evidence for the temperature-sensing ability of the membrane
RT domain of the Bacillus subtilis histidine kinase DesK.";
RL FEMS Microbiol. Lett. 230:41-46(2004).
RN [7]
RP FUNCTION.
RX PubMed=15090506; DOI=10.1128/jb.186.9.2655-2663.2004;
RA Albanesi D., Mansilla M.C., de Mendoza D.;
RT "The membrane fluidity sensor DesK of Bacillus subtilis controls the signal
RT decay of its cognate response regulator.";
RL J. Bacteriol. 186:2655-2663(2004).
RN [8]
RP REVIEW.
RX PubMed=15711796; DOI=10.1007/s00203-005-0759-8;
RA Mansilla M.C., de Mendoza D.;
RT "The Bacillus subtilis desaturase: a model to understand phospholipid
RT modification and temperature sensing.";
RL Arch. Microbiol. 183:229-235(2005).
CC -!- FUNCTION: Member of the two-component regulatory system DesR/DesK,
CC responsible for cold induction of the des gene coding for the Delta5
CC acyl-lipid desaturase. Acts as a sensor of the membrane fluidity.
CC Probably activates DesR by phosphorylation.
CC {ECO:0000269|PubMed:11285232, ECO:0000269|PubMed:11717295,
CC ECO:0000269|PubMed:12207704, ECO:0000269|PubMed:14734164,
CC ECO:0000269|PubMed:15090506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INTERACTION:
CC O34757; O34757: desK; NbExp=3; IntAct=EBI-15806221, EBI-15806221;
CC O34757; O34723: desR; NbExp=3; IntAct=EBI-15806221, EBI-15806271;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AF027868; AAB84437.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13811.1; -; Genomic_DNA.
DR PIR; C69901; C69901.
DR RefSeq; NP_389800.1; NC_000964.3.
DR RefSeq; WP_003231271.1; NZ_JNCM01000036.1.
DR PDB; 3EHF; X-ray; 3.10 A; A/B/C/D=175-370.
DR PDB; 3EHG; X-ray; 1.74 A; A=243-370.
DR PDB; 3EHH; X-ray; 2.10 A; A/B=154-370.
DR PDB; 3EHJ; X-ray; 2.50 A; A/B=154-370.
DR PDB; 3GIE; X-ray; 2.65 A; A/B=154-370.
DR PDB; 3GIF; X-ray; 2.70 A; A/B=154-370.
DR PDB; 3GIG; X-ray; 3.50 A; A/B=154-370.
DR PDB; 5IUJ; X-ray; 3.20 A; A/B/D/E=154-370.
DR PDB; 5IUK; X-ray; 2.90 A; A/B/D/E=154-370.
DR PDB; 5IUL; X-ray; 3.15 A; A/B/D/E=154-370.
DR PDB; 5IUM; X-ray; 3.16 A; A/B=154-370.
DR PDB; 5IUN; X-ray; 2.79 A; A/B/E=150-370.
DR PDBsum; 3EHF; -.
DR PDBsum; 3EHG; -.
DR PDBsum; 3EHH; -.
DR PDBsum; 3EHJ; -.
DR PDBsum; 3GIE; -.
DR PDBsum; 3GIF; -.
DR PDBsum; 3GIG; -.
DR PDBsum; 5IUJ; -.
DR PDBsum; 5IUK; -.
DR PDBsum; 5IUL; -.
DR PDBsum; 5IUM; -.
DR PDBsum; 5IUN; -.
DR AlphaFoldDB; O34757; -.
DR SMR; O34757; -.
DR DIP; DIP-48966N; -.
DR IntAct; O34757; 1.
DR STRING; 224308.BSU19190; -.
DR TCDB; 9.B.238.3.5; the uncharacterized bacterial 5 tms protein-1 (ubp1) family.
DR PaxDb; O34757; -.
DR PRIDE; O34757; -.
DR DNASU; 939678; -.
DR EnsemblBacteria; CAB13811; CAB13811; BSU_19190.
DR GeneID; 939678; -.
DR KEGG; bsu:BSU19190; -.
DR PATRIC; fig|224308.179.peg.2097; -.
DR eggNOG; COG4585; Bacteria.
DR InParanoid; O34757; -.
DR OMA; LWFYTLA; -.
DR PhylomeDB; O34757; -.
DR BioCyc; BSUB:BSU19190-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR EvolutionaryTrace; O34757; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:CACAO.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:CACAO.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF07730; HisKA_3; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..370
FT /note="Sensor histidine kinase DesK"
FT /id="PRO_0000360780"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 186..369
FT /note="Histidine kinase"
FT MOD_RES 188
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:3EHJ"
FT HELIX 171..208
FT /evidence="ECO:0007829|PDB:3EHH"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3EHH"
FT HELIX 213..235
FT /evidence="ECO:0007829|PDB:3EHH"
FT TURN 236..241
FT /evidence="ECO:0007829|PDB:3EHH"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:3EHG"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3EHG"
FT HELIX 277..297
FT /evidence="ECO:0007829|PDB:3EHG"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:3EHG"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:3EHG"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3GIE"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:3EHG"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:3EHG"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:3EHG"
SQ SEQUENCE 370 AA; 42673 MW; 3A22FD6A3630A13D CRC64;
MIKNHFTFQK LNGITPYIWT IFFILPFYFI WKSSSTFVII VGIILTLLFF SVYRFAFVSK
GWTIYLWGFL LIGISTASIT LFSYIYFAFF IAYFIGNIKE RVPFHILYYV HLISAAVAAN
FSLVLKKEFF LTQIPFVVIT LISAILLPFS IKSRKERERL EEKLEDANER IAELVKLEER
QRIARDLHDT LGQKLSLIGL KSDLARKLIY KDPEQAAREL KSVQQTARTS LNEVRKIVSS
MKGIRLKDEL INIKQILEAA DIMFIYEEEK WPENISLLNE NILSMCLKEA VTNVVKHSQA
KTCRVDIQQL WKEVVITVSD DGTFKGEENS FSKGHGLLGM RERLEFANGS LHIDTENGTK
LTMAIPNNSK
