Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q56310 (CHEA_THEMA)

Last modified November 24, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Chemotaxis protein cheA
    EC=2.7.13.3
Gene names
Name: cheA
Ordered Locus Names: TM_0702
OrganismThermotoga maritima [Complete proteome] [HAMAP]
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Hide | Top

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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.

Catalytic activity

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

Subcellular location

Cytoplasm Potential.

Sequence similarities

Contains 1 cheW-like domain.

Contains 1 histidine kinase domain.

Contains 1 HPt domain.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cheYQ563121EBI-1039701,EBI-1039694

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 671671Chemotaxis protein cheA
PRO_0000074718

Regions

Domain1 – 102102HPt
Domain291 – 541251Histidine kinase
Domain543 – 671129CheW-like

Amino acid modifications

Modified residue451Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict3041D → G in AAA96387. Ref.1

Secondary structure

1 ......................................................................................... 671
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q56310-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: F264398B88DA34E1

FASTA67175,556
        10         20         30         40         50         60 
MMEEYLGVFV DETKEYLQNL NDTLLELEKN PEDMELINEA FRALHTLKGM AGTMGFSSMA 

        70         80         90        100        110        120 
KLCHTLENIL DKARNSEIKI TSDLLDKIFA GVDMITRMVD KIVSEGSDDI GENIDVFSDT 

       130        140        150        160        170        180 
IKSFASSGKE KPSEIKNETE TKGEEEHKGE STSNEEVVVL PEEVAHVLQE ARNKGFKTFY 

       190        200        210        220        230        240 
IKVILKEGTQ LKSARIYLVF HKLEELKCEV VRTIPSVEEI EEEKFENEVE LFVISPVDLE 

       250        260        270        280        290        300 
KLSEALSSIA DIERVIIKEV TAVTEESGAE KRTEKEEKTE KTEEKAERKK VISQTVRVDI 

       310        320        330        340        350        360 
EKLDNLMDLM GELVIARSRI LETLKKYNIK ELDESLSHLS RITLDLQNVV MKIRMVPISF 

       370        380        390        400        410        420 
VFNRFPRMVR DLAKKMNKEV NFIMRGEDTE LDRTFVEEIG EPLLHLLRNA IDHGIEPKEE 

       430        440        450        460        470        480 
RIAKGKPPIG TLILSARHEG NNVVIEVEDD GRGIDKEKII RKAIEKGLID ESKAATLSDQ 

       490        500        510        520        530        540 
EILNFLFVPG FSTKEKVSEV SGRGVGMDVV KNVVESLNGS ISIESEKDKG TKVTIRLPLT 

       550        560        570        580        590        600 
LAIIQALLVK VNNLVYAIPI ANIDTILSIS KEDIQRVQDR DVIVIRGEVI PVYRLWEVLQ 

       610        620        630        640        650        660 
IEHKEELEEM EAVIVRVGNR KYGIVVDDLL GQDDIVIKSL GKVFSEVKEF SGAAILGDGS 

       670 
IALIINVSGI V

« Hide

Hide | Top

References

« Hide 'large scale' references
[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: 8550470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
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: 9989504] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 293-671.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

U30501 Genomic DNA. Translation: AAA96387.1.
AE000512 Genomic DNA. Translation: AAD35784.1.
PIRD72346.
RefSeqNP_228511.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B3QX-ray2.60A/B293-671[»]
1I58X-ray1.60A/B355-540[»]
1I59X-ray1.80A/B355-540[»]
1I5AX-ray1.90A/B355-540[»]
1I5BX-ray1.94A/B355-540[»]
1I5CX-ray1.90A/B355-540[»]
1I5DX-ray2.90A350-540[»]
1TQGX-ray0.98A4-104[»]
1U0SX-ray1.90A175-260[»]
2CH4X-ray3.50A/B355-671[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29071N.
IntActQ56310. 1 interaction.

Genome annotation databases

GeneID898369.
GenomeReviewsGene locus TM_0702 in contig AE000512_GR.
KEGGtma:TM0702.
NMPDRfig|243274.1.peg.695.
TIGRTM_0702.

Phylogenomic databases

HOGENOMQ56310.
OMASERIINM

Enzyme and pathway databases

BioCycTMAR243274:TM_0702-MON.
BRENDA2.7.13.3. 16699.

Family and domain databases

InterProIPR003594. ATP_bd_ATPase.
IPR002545. CheW.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_P-trf.
IPR004105. Sig_transdc_His_kin_subgr_dim.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
IPR010808. Sig_transdc_His_kinase_P2-bd.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
PfamPF01584. CheW. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
PF07194. P2. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
PROSITEPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCHEA_THEMA
AccessionPrimary (citable) accession number: Q56310
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: November 24, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents