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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: 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

GO - Biological processi

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
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000747181 – 671Chemotaxis protein CheAAdd BLAST671

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 29Combined sources26
Helixi34 – 53Combined sources20
Helixi57 – 74Combined sources18
Helixi82 – 102Combined sources21
Helixi114 – 123Combined sources10
Beta strandi177 – 184Combined sources8
Helixi192 – 205Combined sources14
Beta strandi209 – 215Combined sources7
Helixi217 – 221Combined sources5
Beta strandi225 – 237Combined sources13
Helixi239 – 247Combined sources9
Beta strandi249 – 251Combined sources3
Beta strandi253 – 260Combined sources8
Beta strandi295 – 299Combined sources5
Helixi300 – 322Combined sources23
Helixi324 – 326Combined sources3
Beta strandi354 – 357Combined sources4
Helixi359 – 362Combined sources4
Helixi365 – 375Combined sources11
Beta strandi380 – 385Combined sources6
Beta strandi390 – 392Combined sources3
Helixi393 – 413Combined sources21
Helixi418 – 424Combined sources7
Beta strandi428 – 439Combined sources12
Beta strandi442 – 449Combined sources8
Helixi456 – 465Combined sources10
Beta strandi466 – 468Combined sources3
Helixi471 – 474Combined sources4
Helixi479 – 483Combined sources5
Helixi484 – 487Combined sources4
Turni489 – 492Combined sources4
Helixi493 – 498Combined sources6
Helixi499 – 501Combined sources3
Helixi506 – 516Combined sources11
Beta strandi520 – 526Combined sources7
Turni527 – 529Combined sources3
Beta strandi530 – 538Combined sources9
Beta strandi542 – 551Combined sources10
Beta strandi554 – 559Combined sources6
Helixi560 – 562Combined sources3
Beta strandi563 – 567Combined sources5
Helixi571 – 573Combined sources3
Beta strandi575 – 577Combined sources3
Beta strandi580 – 585Combined sources6
Beta strandi588 – 594Combined sources7
Helixi595 – 598Combined sources4
Beta strandi611 – 617Combined sources7
Beta strandi620 – 637Combined sources18
Helixi641 – 644Combined sources4
Beta strandi648 – 655Combined sources8
Beta strandi657 – 659Combined sources3
Beta strandi661 – 665Combined sources5
Helixi667 – 669Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3JA6electron microscopy12.70C/E293-671[»]
3UR1X-ray4.50A355-671[»]
4JPBX-ray3.19A355-671[»]
4XIVX-ray3.00A/B289-540[»]
ProteinModelPortaliQ56310.
SMRiQ56310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56310.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 102HPtPROSITE-ProRule annotationAdd BLAST102
Domaini291 – 541Histidine kinasePROSITE-ProRule annotationAdd BLAST251
Domaini543 – 671CheW-likePROSITE-ProRule annotationAdd BLAST129

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

eggNOGiENOG4105CBS. Bacteria.
COG0643. LUCA.
InParanoidiQ56310.
KOiK03407.
OMAiIILNMRM.

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.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
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.
SM01231. H-kinase_dim. 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)DescriptionActionsGraphical viewLength
Sequence conflicti304D → G in AAA96387 (PubMed:8550470).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30501 Genomic DNA. Translation: AAA96387.1.
AE000512 Genomic DNA. Translation: AAD35784.1.
PIRiD72346.
RefSeqiNP_228511.1. NC_000853.1.
WP_004081040.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35784; AAD35784; TM_0702.
GeneIDi898369.
KEGGitma:TM0702.
PATRICi23936322. VBITheMar51294_0714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30501 Genomic DNA. Translation: AAA96387.1.
AE000512 Genomic DNA. Translation: AAD35784.1.
PIRiD72346.
RefSeqiNP_228511.1. NC_000853.1.
WP_004081040.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3JA6electron microscopy12.70C/E293-671[»]
3UR1X-ray4.50A355-671[»]
4JPBX-ray3.19A355-671[»]
4XIVX-ray3.00A/B289-540[»]
ProteinModelPortaliQ56310.
SMRiQ56310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protocols and materials databases

DNASUi898369.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35784; AAD35784; TM_0702.
GeneIDi898369.
KEGGitma:TM0702.
PATRICi23936322. VBITheMar51294_0714.

Phylogenomic databases

eggNOGiENOG4105CBS. Bacteria.
COG0643. LUCA.
InParanoidiQ56310.
KOiK03407.
OMAiIILNMRM.

Enzyme and pathway databases

BRENDAi2.7.13.3. 6331.

Miscellaneous databases

EvolutionaryTraceiQ56310.

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.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
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.
SM01231. H-kinase_dim. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 140 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

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.