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Protein

Transcriptional regulatory protein DesR

Gene

desR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi155 – 17420H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU19200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein DesR
Gene namesi
Name:desR
Synonyms:yocG
Ordered Locus Names:BSU19200
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Transcriptional regulatory protein DesRPRO_0000360772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphatePROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by DesK.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO34723.

Interactioni

Protein-protein interaction databases

DIPiDIP-48967N.
STRINGi224308.Bsubs1_010100010596.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni7 – 104Combined sources
Helixi12 – 2110Combined sources
Beta strandi27 – 293Combined sources
Helixi37 – 4610Combined sources
Beta strandi49 – 546Combined sources
Beta strandi58 – 603Combined sources
Helixi64 – 674Combined sources
Turni68 – 714Combined sources
Beta strandi75 – 828Combined sources
Helixi87 – 937Combined sources
Beta strandi98 – 1014Combined sources
Helixi106 – 11712Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 1303Combined sources
Helixi140 – 15112Combined sources
Helixi155 – 1617Combined sources
Helixi166 – 19227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LDZX-ray2.31A/B1-199[»]
4LE0X-ray2.27A/B1-135[»]
4LE1X-ray1.95A/B1-135[»]
4LE2X-ray2.54A/B/C/D1-135[»]
ProteinModelPortaliO34723.
SMRiO34723. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 117115Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini131 – 19666HTH luxR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH luxR-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108S01. Bacteria.
COG2197. LUCA.
HOGENOMiHOG000034813.
InParanoidiO34723.
KOiK07693.
OMAiYRNKQIA.
OrthoDBiEOG69GZGV.
PhylomeDBiO34723.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISIFIAEDQ QMLLGALGSL LNLEDDMEVV GKGTTGQDAV DFVKKRQPDV
60 70 80 90 100
CIMDIEMPGK TGLEAAEELK DTGCKIIILT TFARPGYFQR AIKAGVKGYL
110 120 130 140 150
LKDSPSEELA NAIRSVMNGK RIYAPELMED LYSEANPLTD REKEVLELVA
160 170 180 190
DGKNTKEIAQ ELSIKSGTVR NYISMILEKL EVKNRIEAIT RSKEKGWFK
Length:199
Mass (Da):22,177
Last modified:January 1, 1998 - v1
Checksum:i8D27B10320FA4974
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027868 Genomic DNA. Translation: AAB84438.1.
AL009126 Genomic DNA. Translation: CAB13812.1.
PIRiD69901.
RefSeqiNP_389801.1. NC_000964.3.
WP_004399356.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB13812; CAB13812; BSU19200.
GeneIDi939664.
KEGGibsu:BSU19200.
PATRICi18975689. VBIBacSub10457_2035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027868 Genomic DNA. Translation: AAB84438.1.
AL009126 Genomic DNA. Translation: CAB13812.1.
PIRiD69901.
RefSeqiNP_389801.1. NC_000964.3.
WP_004399356.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LDZX-ray2.31A/B1-199[»]
4LE0X-ray2.27A/B1-135[»]
4LE1X-ray1.95A/B1-135[»]
4LE2X-ray2.54A/B/C/D1-135[»]
ProteinModelPortaliO34723.
SMRiO34723. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48967N.
STRINGi224308.Bsubs1_010100010596.

Proteomic databases

PaxDbiO34723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13812; CAB13812; BSU19200.
GeneIDi939664.
KEGGibsu:BSU19200.
PATRICi18975689. VBIBacSub10457_2035.

Phylogenomic databases

eggNOGiENOG4108S01. Bacteria.
COG2197. LUCA.
HOGENOMiHOG000034813.
InParanoidiO34723.
KOiK07693.
OMAiYRNKQIA.
OrthoDBiEOG69GZGV.
PhylomeDBiO34723.

Enzyme and pathway databases

BioCyciBSUB:BSU19200-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS50043. HTH_LUXR_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Strain: 168.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiDESR_BACSU
AccessioniPrimary (citable) accession number: O34723
Secondary accession number(s): Q796C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 120 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
  3. SIMILARITY comments
    Index of protein domains and families

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.