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Q56310

- CHEA_THEMA

UniProt

Q56310 - CHEA_THEMA

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Protein

Chemotaxis protein CheA

Gene

cheA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphorelay sensor kinase activity Source: InterPro

GO - Biological processi

  1. cellular component movement Source: InterPro
  2. chemotaxis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Chemotaxis, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.13.3. 6331.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheA (EC:2.7.13.3)
Gene namesi
Name:cheA
Ordered Locus Names:TM_0702
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Chemotaxis protein CheAPRO_0000074718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-29071N.
IntActiQ56310. 1 interaction.
STRINGi243274.TM0702.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2926
Helixi34 – 5320
Helixi57 – 7418
Helixi82 – 10221
Helixi114 – 12310
Beta strandi177 – 1848
Helixi192 – 20514
Beta strandi209 – 2157
Helixi217 – 2215
Beta strandi225 – 23713
Helixi239 – 2479
Beta strandi249 – 2513
Beta strandi253 – 2608
Beta strandi295 – 2995
Helixi300 – 32223
Beta strandi354 – 3574
Helixi359 – 3624
Helixi365 – 37511
Beta strandi380 – 3856
Beta strandi390 – 3923
Helixi393 – 41321
Helixi418 – 4247
Beta strandi428 – 43912
Beta strandi442 – 4498
Helixi456 – 46510
Beta strandi466 – 4683
Helixi471 – 4744
Helixi479 – 4835
Helixi484 – 4874
Turni489 – 4924
Helixi493 – 4986
Helixi499 – 5013
Helixi506 – 51611
Beta strandi520 – 5267
Turni527 – 5293
Beta strandi530 – 5389
Beta strandi542 – 55110
Beta strandi554 – 5596
Helixi560 – 5623
Beta strandi563 – 5675
Helixi571 – 5733
Beta strandi575 – 5773
Beta strandi580 – 5856
Beta strandi588 – 5947
Helixi595 – 5984
Beta strandi611 – 6177
Beta strandi620 – 63718
Helixi641 – 6444
Beta strandi648 – 6558
Beta strandi657 – 6593
Beta strandi661 – 6655
Helixi667 – 6693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3QX-ray2.60A/B293-671[»]
1I58X-ray1.60A/B352-540[»]
1I59X-ray1.80A/B352-540[»]
1I5AX-ray1.90A/B352-540[»]
1I5BX-ray1.94A/B352-540[»]
1I5CX-ray1.90A/B352-540[»]
1I5DX-ray2.90A350-540[»]
1TQGX-ray0.98A4-104[»]
1U0SX-ray1.90A175-260[»]
2CH4X-ray3.50A/B355-671[»]
2LD6NMR-A1-131[»]
3UR1X-ray4.50A355-671[»]
4JPBX-ray3.19A355-671[»]
ProteinModelPortaliQ56310.
SMRiQ56310. Positions 4-104, 175-260, 293-671.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56310.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 102102HPtPROSITE-ProRule annotationAdd
BLAST
Domaini291 – 541251Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini543 – 671129CheW-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 cheW-like domain.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 HPt domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0643.
InParanoidiQ56310.
KOiK03407.
OMAiKISTPPM.
OrthoDBiEOG62RS8P.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.1110. 1 hit.
InterProiIPR004105. CheA-like_dim.
IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view]
PfamiPF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q56310-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMEEYLGVFV DETKEYLQNL NDTLLELEKN PEDMELINEA FRALHTLKGM
60 70 80 90 100
AGTMGFSSMA KLCHTLENIL DKARNSEIKI TSDLLDKIFA GVDMITRMVD
110 120 130 140 150
KIVSEGSDDI GENIDVFSDT IKSFASSGKE KPSEIKNETE TKGEEEHKGE
160 170 180 190 200
STSNEEVVVL PEEVAHVLQE ARNKGFKTFY IKVILKEGTQ LKSARIYLVF
210 220 230 240 250
HKLEELKCEV VRTIPSVEEI EEEKFENEVE LFVISPVDLE KLSEALSSIA
260 270 280 290 300
DIERVIIKEV TAVTEESGAE KRTEKEEKTE KTEEKAERKK VISQTVRVDI
310 320 330 340 350
EKLDNLMDLM GELVIARSRI LETLKKYNIK ELDESLSHLS RITLDLQNVV
360 370 380 390 400
MKIRMVPISF VFNRFPRMVR DLAKKMNKEV NFIMRGEDTE LDRTFVEEIG
410 420 430 440 450
EPLLHLLRNA IDHGIEPKEE RIAKGKPPIG TLILSARHEG NNVVIEVEDD
460 470 480 490 500
GRGIDKEKII RKAIEKGLID ESKAATLSDQ EILNFLFVPG FSTKEKVSEV
510 520 530 540 550
SGRGVGMDVV KNVVESLNGS ISIESEKDKG TKVTIRLPLT LAIIQALLVK
560 570 580 590 600
VNNLVYAIPI ANIDTILSIS KEDIQRVQDR DVIVIRGEVI PVYRLWEVLQ
610 620 630 640 650
IEHKEELEEM EAVIVRVGNR KYGIVVDDLL GQDDIVIKSL GKVFSEVKEF
660 670
SGAAILGDGS IALIINVSGI V
Length:671
Mass (Da):75,556
Last modified:May 30, 2000 - v2
Checksum:iF264398B88DA34E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041D → G in AAA96387. (PubMed:8550470)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30501 Genomic DNA. Translation: AAA96387.1.
AE000512 Genomic DNA. Translation: AAD35784.1.
PIRiD72346.
RefSeqiNP_228511.1. NC_000853.1.
WP_004081040.1. NC_023151.1.
YP_007977052.1. NC_021214.1.
YP_008990329.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35784; AAD35784; TM_0702.
GeneIDi18092087.
898369.
KEGGitma:TM0702.
tmi:THEMA_01155.
tmm:Tmari_0702.
PATRICi23936322. VBITheMar51294_0714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30501 Genomic DNA. Translation: AAA96387.1 .
AE000512 Genomic DNA. Translation: AAD35784.1 .
PIRi D72346.
RefSeqi NP_228511.1. NC_000853.1.
WP_004081040.1. NC_023151.1.
YP_007977052.1. NC_021214.1.
YP_008990329.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B3Q X-ray 2.60 A/B 293-671 [» ]
1I58 X-ray 1.60 A/B 352-540 [» ]
1I59 X-ray 1.80 A/B 352-540 [» ]
1I5A X-ray 1.90 A/B 352-540 [» ]
1I5B X-ray 1.94 A/B 352-540 [» ]
1I5C X-ray 1.90 A/B 352-540 [» ]
1I5D X-ray 2.90 A 350-540 [» ]
1TQG X-ray 0.98 A 4-104 [» ]
1U0S X-ray 1.90 A 175-260 [» ]
2CH4 X-ray 3.50 A/B 355-671 [» ]
2LD6 NMR - A 1-131 [» ]
3UR1 X-ray 4.50 A 355-671 [» ]
4JPB X-ray 3.19 A 355-671 [» ]
ProteinModelPortali Q56310.
SMRi Q56310. Positions 4-104, 175-260, 293-671.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29071N.
IntActi Q56310. 1 interaction.
STRINGi 243274.TM0702.

Protocols and materials databases

DNASUi 898369.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35784 ; AAD35784 ; TM_0702 .
GeneIDi 18092087.
898369.
KEGGi tma:TM0702.
tmi:THEMA_01155.
tmm:Tmari_0702.
PATRICi 23936322. VBITheMar51294_0714.

Phylogenomic databases

eggNOGi COG0643.
InParanoidi Q56310.
KOi K03407.
OMAi KISTPPM.
OrthoDBi EOG62RS8P.

Enzyme and pathway databases

BRENDAi 2.7.13.3. 6331.

Miscellaneous databases

EvolutionaryTracei Q56310.

Family and domain databases

Gene3Di 1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.1110. 1 hit.
InterProi IPR004105. CheA-like_dim.
IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_C.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view ]
Pfami PF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view ]
PRINTSi PR00344. BCTRLSENSOR.
SMARTi SM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view ]
SUPFAMi SSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima."
    Swanson R.V., Sanna M.G., Simon M.I.
    J. Bacteriol. 178:484-489(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Structure of CheA, a signal-transducing histidine kinase."
    Bilwes A.M., Alex L.A., Crane B.R., Simon M.I.
    Cell 96:131-141(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 293-671.

Entry informationi

Entry nameiCHEA_THEMA
AccessioniPrimary (citable) accession number: Q56310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 122 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3