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Protein

Sensor histidine kinase DcuS

Gene

dcuS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system DcuR/DcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate transporter dctA. Activates DcuR by phosphorylation.

Catalytic activityi

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

Enzyme regulationi

Autophosphorylation is stimulated by the presence of C4-dicarboxylates such as fumarate, succinate, malate, and tartrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071C4-dicarboxylate
Binding sitei110 – 1101C4-dicarboxylate
Binding sitei121 – 1211C4-dicarboxylate; via amide nitrogen and carbonyl oxygen
Binding sitei147 – 1471C4-dicarboxylate

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • phosphorelay sensor kinase activity Source: EcoliWiki
  • protein histidine kinase activity Source: EcoliWiki
  • signal transducer activity Source: EcoliWiki

GO - Biological processi

  • phosphorelay signal transduction system Source: EcoliWiki
  • protein homooligomerization Source: EcoCyc
  • protein phosphorylation Source: EcoliWiki
  • regulation of transcription, DNA-templated Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:DCUS-MONOMER.
ECOL316407:JW4086-MONOMER.
BRENDAi2.7.13.3. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Sensor histidine kinase DcuS (EC:2.7.13.3)
Alternative name(s):
Fumarate sensor
Gene namesi
Name:dcuS
Synonyms:yjdH
Ordered Locus Names:b4125, JW4086
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12465. dcuS.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence analysisAdd
BLAST
Transmembranei21 – 4121HelicalSequence analysisAdd
BLAST
Topological domaini42 – 181140PeriplasmicSequence analysisAdd
BLAST
Transmembranei182 – 20221HelicalSequence analysisAdd
BLAST
Topological domaini203 – 543341CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • intracellular Source: GOC
  • plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071R → A: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene. 1 Publication
Mutagenesisi110 – 1101H → A: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene. 1 Publication
Mutagenesisi147 – 1471R → A: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene. 1 Publication
Mutagenesisi248 – 2481N → A, D or G: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates. 1 Publication
Mutagenesisi304 – 3041N → D: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Sensor histidine kinase DcuSPRO_0000074750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Post-translational modificationi

Autophosphorylated. The phosphoryl group is rapidly transferred to DcuR.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AEC8.

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-1134683,EBI-1134683

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261981. 12 interactions.
DIPiDIP-9414N.
IntActiP0AEC8. 3 interactions.
STRINGi511145.b4125.

Structurei

Secondary structure

1
543
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 6418Combined sources
Helixi67 – 726Combined sources
Helixi77 – 793Combined sources
Helixi82 – 9211Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi106 – 1083Combined sources
Helixi113 – 1153Combined sources
Helixi123 – 1253Combined sources
Helixi127 – 1304Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi145 – 1539Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi159 – 16810Combined sources
Helixi169 – 1779Combined sources
Helixi214 – 2174Combined sources
Helixi221 – 2299Combined sources
Beta strandi236 – 2394Combined sources
Turni240 – 2423Combined sources
Helixi249 – 2557Combined sources
Turni259 – 2635Combined sources
Helixi277 – 2848Combined sources
Beta strandi294 – 2985Combined sources
Beta strandi317 – 3193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJGNMR-A45-180[»]
2W0NNMR-A211-325[»]
3BY8X-ray1.45A42-181[»]
ProteinModelPortaliP0AEC8.
SMRiP0AEC8. Positions 45-179, 211-537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEC8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini212 – 323112PASPROSITE-ProRule annotationAdd
BLAST
Domaini346 – 538193Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 1423C4-dicarboxylate binding

Domaini

The periplasmic domain is involved in C4-dicarboxylate binding and sensing. The structural disorder in the cytoplasmic PAS domain has an important role in signal transduction to the kinase domain and may be the decisive structural feature that characterizes the activated kinase.3 Publications

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CEQ. Bacteria.
COG3290. LUCA.
HOGENOMiHOG000241936.
InParanoidiP0AEC8.
KOiK07701.
OMAiHYQNGWL.
PhylomeDBiP0AEC8.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR033463. sCache_3.
IPR029151. Sensor-like.
IPR004358. Sig_transdc_His_kin-like_C.
IPR016120. Sig_transdc_His_kin_SpoOB.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00989. PAS. 1 hit.
PF17203. sCache_3_2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF55890. SSF55890. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHSLPYRML RKRPMKLSTT VILMVSAVLF SVLLVVHLIY FSQISDMTRD
60 70 80 90 100
GLANKALAVA RTLADSPEIR QGLQKKPQES GIQAIAEAVR KRNDLLFIVV
110 120 130 140 150
TDMQSLRYSH PEAQRIGQPF KGDDILKALN GEENVAINRG FLAQALRVFT
160 170 180 190 200
PIYDENHKQI GVVAIGLELS RVTQQINDSR WSIIWSVLFG MLVGLIGTCI
210 220 230 240 250
LVKVLKKILF GLEPYEISTL FEQRQAMLQS IKEGVVAVDD RGEVTLINDA
260 270 280 290 300
AQELLNYRKS QDDEKLSTLS HSWSQVVDVS EVLRDGTPRR DEEITIKDRL
310 320 330 340 350
LLINTVPVRS NGVIIGAIST FRDKTEVRKL MQRLDGLVNY ADALRERSHE
360 370 380 390 400
FMNKLHVILG LLHLKSYKQL EDYILKTANN YQEEIGSLLG KIKSPVIAGF
410 420 430 440 450
LISKINRATD LGHTLILNSE SQLPDSGSED QVATLITTLG NLIENALEAL
460 470 480 490 500
GPEPGGEISV TLHYRHGWLH CEVNDDGPGI APDKIDHIFD KGVSTKGSER
510 520 530 540
GVGLALVKQQ VENLGGSIAV ESEPGIFTQF FVQIPWDGER SNR
Length:543
Mass (Da):60,551
Last modified:December 6, 2005 - v1
Checksum:i653C369344CBA238
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97025.1.
U00096 Genomic DNA. Translation: AAC77086.1.
AP009048 Genomic DNA. Translation: BAE78127.1.
PIRiD65222.
RefSeqiNP_418549.1. NC_000913.3.
WP_001216477.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77086; AAC77086; b4125.
BAE78127; BAE78127; BAE78127.
GeneIDi948639.
KEGGiecj:JW4086.
eco:b4125.
PATRICi32123815. VBIEscCol129921_4256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97025.1.
U00096 Genomic DNA. Translation: AAC77086.1.
AP009048 Genomic DNA. Translation: BAE78127.1.
PIRiD65222.
RefSeqiNP_418549.1. NC_000913.3.
WP_001216477.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJGNMR-A45-180[»]
2W0NNMR-A211-325[»]
3BY8X-ray1.45A42-181[»]
ProteinModelPortaliP0AEC8.
SMRiP0AEC8. Positions 45-179, 211-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261981. 12 interactions.
DIPiDIP-9414N.
IntActiP0AEC8. 3 interactions.
STRINGi511145.b4125.

Proteomic databases

PaxDbiP0AEC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77086; AAC77086; b4125.
BAE78127; BAE78127; BAE78127.
GeneIDi948639.
KEGGiecj:JW4086.
eco:b4125.
PATRICi32123815. VBIEscCol129921_4256.

Organism-specific databases

EchoBASEiEB2358.
EcoGeneiEG12465. dcuS.

Phylogenomic databases

eggNOGiENOG4105CEQ. Bacteria.
COG3290. LUCA.
HOGENOMiHOG000241936.
InParanoidiP0AEC8.
KOiK07701.
OMAiHYQNGWL.
PhylomeDBiP0AEC8.

Enzyme and pathway databases

BioCyciEcoCyc:DCUS-MONOMER.
ECOL316407:JW4086-MONOMER.
BRENDAi2.7.13.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AEC8.
PROiP0AEC8.

Family and domain databases

Gene3Di1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR033463. sCache_3.
IPR029151. Sensor-like.
IPR004358. Sig_transdc_His_kin-like_C.
IPR016120. Sig_transdc_His_kin_SpoOB.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF00989. PAS. 1 hit.
PF17203. sCache_3_2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00387. HATPase_c. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMiSSF103190. SSF103190. 1 hit.
SSF55785. SSF55785. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF55890. SSF55890. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDCUS_ECOLI
AccessioniPrimary (citable) accession number: P0AEC8
Secondary accession number(s): P39272, P76795, Q2M6H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: September 7, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The region encompassing approximately residues 42 to 181 has been shown to be periplasmic, however exactly which residues are periplasmic is not clear.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.