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Reviewed, UniProtKB/Swiss-Prot Q52880 (CHEA_RHIME)

Last modified January 19, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chemotaxis protein cheA
    EC=2.7.13.3
Gene names
Name: cheA
Ordered Locus Names: R00639
ORF Names: SMc03007
OrganismRhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier382 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords
   Biological processChemotaxis
Two-component regulatory system
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: InterPro

two-component signal transduction system (phosphorelay)

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

two-component sensor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 758758Chemotaxis protein cheA
PRO_0000074716

Regions

Domain1 – 103103HPt
Domain367 – 607241Histidine kinase
Domain609 – 745137CheW-like

Amino acid modifications

Modified residue461Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict1891D → E in AAA86674. Ref.1
Sequence conflict1921S → A in AAA86674. Ref.1
Sequence conflict2151N → D in AAA86674. Ref.1
Sequence conflict2971E → K in AAA86674. Ref.1
Sequence conflict3081S → P in AAA86674. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q52880-1 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 9F03A8F24EA25D5D

FASTA75881,102
        10         20         30         40         50         60 
MDMNEIKEIF FQECEEQLAE LESGLLKLND GDRDPETVNA VFRAVHSIKG GAGAFGLDDL 

        70         80         90        100        110        120 
VSFAHVFETT LDCVRSNRLE PNQDVLKVML RSADVLADLT NAARDGGGVD EARSRQLIKE 

       130        140        150        160        170        180 
LEALANGELP QAAAESAPKT TPAGVAPAAP VVNEEGFQPV AFSFDDFETG DEPTIEPSTY 

       190        200        210        220        230        240 
EIVFKPKSDL YSKGNDATLL LRDLSRLGEM SIHCNMDTLP PLDRMNPEEA YFSWKISLKT 

       250        260        270        280        290        300 
DKGEEAIRSV FEFAEWDCEL DVALAGGTVG MDEDLPMQPV PFDLSILEDE AQAPAGEEDR 

       310        320        330        340        350        360 
AAASEGDSRN AAVAAAQTAS NVLQMAQSTA RVSPENARNS QSASAAQAAA QQAASAATPT 

       370        380        390        400        410        420 
IRVDLDRVDR LINLVGELVI NQAMLSQSVI ENDTNGTSSI NMGLEELQQL TREIQDSVMA 

       430        440        450        460        470        480 
IRAQPVKPVF QRMSRIVREI ADMTGKSVRL ITEGENTEVD KTVIDKLAEP LTHMIRNAVD 

       490        500        510        520        530        540 
HGLETPEKRV AAGKNPEGTV RLTAKHRSGR IVIELADDGA GINREKVRQK AIDNDLIAAD 

       550        560        570        580        590        600 
ANLSDEEVDN LIFHAGFSTA DKISDISGRG VGMDVVKRSI QALGGRINIS SKPGQGSIFT 

       610        620        630        640        650        660 
MSLPLTLAVL DGMVVTVANQ TLVVPLTAIV ETLQPEASAI HSFGSSQRLI SIRDSFCPLV 

       670        680        690        700        710        720 
DVGRILNFRG AQANPVEGVA LLVESEGGGQ RALMVDAIQG QRQVVIKSLE ANYTHVPGIA 

       730        740        750 
AATILGDGRV ALILDVDAIV AASRGQSLKP EMSLAAAG

« Hide

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References

« Hide 'large scale' references
[1]"Analysis of a chemotaxis operon in Rhizobium meliloti."
Greck M., Platzer J., Sourjik V., Schmitt R.
Mol. Microbiol. 15:989-1000(1995) [PubMed: 7623670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RU11/001.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U13166 Genomic DNA. Translation: AAA86674.1.
AL591688 Genomic DNA. Translation: CAC45211.1.
PIRS61834.
RefSeqNP_384745.1.

3D structure databases

SMRQ52880. Positions 2-126, 359-740.
ModBaseSearch...

Genome annotation databases

GeneID1232278.
GenomeReviewsGene locus R00639 in contig AL591688_GR.
KEGGsme:SMc03007.
NMPDRfig|266834.1.peg.1933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG705053.
OMAFPANAVE.

Enzyme and pathway databases

BioCycSMEL266834:SMC03007-MONOMER.
BRENDA2.7.13.3. 142.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR002545. CheW.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR004105. Sig_transdc_His_kin_subgr_dim.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[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.
[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...

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Entry information

Entry nameCHEA_RHIME
AccessionPrimary (citable) accession number: Q52880
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2001
Last modified: January 19, 2010
This is version 72 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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