P07363 (CHEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chemotaxis protein CheA
EC=2.7.13.3

Gene names

Name:	cheA
Ordered Locus Names:	b1888, JW1877

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subunit structure	An in vitro complex of CheW/CheA(L)/CheA(S) in a 1:1:1 ratio increases the autophosphorylation of CheA and is required for the binding of CheY, the phosphorylation substrate. This complex accounts for 10% of the total number of molecules. Ref.7
Subcellular location	Cytoplasm.
Domain	May have three functional domains: one for interaction with CheB and CheY, a second for regulating phosphorylation and controlling the stability of the protein, and a third for receiving input signals regulating CheA activity. Ref.6
Sequence similarities	Contains 1 cheW-like domain. Contains 1 histidine kinase domain. Contains 1 HPt domain.

Ontologies

Keywords
Biological process	Chemotaxis Two-component regulatory system
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from mutant phenotype PubMed 8820640. Source: EcoCyc establishment of localization in cell Inferred from direct assay PubMed 19502407. Source: EcoCyc phosphorelay signal transduction system Inferred from direct assay PubMed 2558046. Source: EcoliWiki positive regulation of protein dephosphorylation Inferred from mutant phenotype PubMed 8820640. Source: EcoCyc protein autophosphorylation Inferred from direct assay PubMed 2558046. Source: EcoliWiki signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay sensor kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cheY	P0AE67	3	EBI-1026773,EBI-546693
cheZ	P0A9H9	3	EBI-1026773,EBI-546726

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform cheA(L) (identifier: P07363-1)

Also known as: long; large;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform cheA(S) (identifier: P07363-2)

Also known as: short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 654

654

Chemotaxis protein CheA

PRO_0000032373

Regions

Domain

1 – 105

105

HPt

Domain

257 – 509

253

Histidine kinase

Domain

511 – 646

136

CheW-like

Amino acid modifications

Modified residue

48

1

Phosphohistidine; by autocatalysis

Natural variations

Alternative sequence

1 – 97

97

Missing in isoform cheA(S).

VSP_018886

Experimental info

Sequence conflict

166

1

R → P in AAA23573. Ref.1

Sequence conflict

166

1

R → P in AAA23574. Ref.1

Sequence conflict

548 – 565

18

GERVL…IVELW → ASGCWKCGVNICPSSNCG in AAA23564. Ref.5

Sequence conflict

606

1

V → A in AAA23564. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

654

Helix Strand Turn

Details...

Helix

5 – 7

3

Helix

9 – 29

21

Helix

37 – 56

20

Helix

60 – 77

18

Helix

85 – 106

22

Helix

113 – 130

18

Beta strand

140 – 145

6

Beta strand

151 – 154

4

Beta strand

161 – 164

4

Helix

171 – 182

12

Beta strand

186 – 190

5

Beta strand

195 – 198

4

Beta strand

201 – 204

4

Helix

205 – 212

8

Turn

213 – 215

3

Beta strand

220 – 224

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform cheA(L) (long) (large) [UniParc]. Last modified November 1, 1997. Version 3. Checksum: 009B824154E269B4	FASTA	654	71,382
	10 20 30 40 50 60 MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI KGGAGTFGFS 70 80 90 100 110 120 VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKQSQE PDAASFDYIC 130 140 150 160 170 180 QALRQLALEA KGETPSAVTR LSVVAKSEPQ DEQSRSQSPR RIILSRLKAG EVDLLEEELG 190 200 210 220 230 240 HLTTLTDVVK GADSLSAILP GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL 250 260 270 280 290 300 AAEQAPTGRV EREKTTRSNE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH 310 320 330 340 350 360 GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ VELTLVGSST 370 380 390 400 410 420 ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV GNLILSAEHQ GGNICIEVTD 430 440 450 460 470 480 DGAGLNRERI LAKAASQGLT VSENMSDDEV AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR 490 500 510 520 530 540 NIQKMGGHVE IQSKQGTGTT IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA 550 560 570 580 590 600 DLHPLAGGER VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI 610 620 630 640 650 GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA NTAA
	Isoform cheA(S) (short) [UniParc]. Checksum: 8982A8C04F2AEDBA	FASTA	557	60,422
	10 20 30 40 50 60 MQEQLDAYKQ SQEPDAASFD YICQALRQLA LEAKGETPSA VTRLSVVAKS EPQDEQSRSQ 70 80 90 100 110 120 SPRRIILSRL KAGEVDLLEE ELGHLTTLTD VVKGADSLSA ILPGDIAEDD ITAVLCFVIE 130 140 150 160 170 180 ADQITFETVE VSPKISTPPV LKLAAEQAPT GRVEREKTTR SNESTSIRVA VEKVDQLINL 190 200 210 220 230 240 VGELVITQSM LAQRSSELDP VNHGDLITSM GQLQRNARDL QESVMSIRMM PMEYVFSRYP 250 260 270 280 290 300 RLVRDLAGKL GKQVELTLVG SSTELDKSLI ERIIDPLTHL VRNSLDHGIE LPEKRLAAGK 310 320 330 340 350 360 NSVGNLILSA EHQGGNICIE VTDDGAGLNR ERILAKAASQ GLTVSENMSD DEVAMLIFAP 370 380 390 400 410 420 GFSTAEQVTD VSGRGVGMDV VKRNIQKMGG HVEIQSKQGT GTTIRILLPL TLAILDGMSV 430 440 450 460 470 480 RVADEVFILP LNAVMESLQP READLHPLAG GERVLEVRGE YLPIVELWKV FNVAGAKTEA 490 500 510 520 530 540 TQGIVVILQS GGRRYALLVD QLIGQHQVVV KNLESNYRKV PGISAATILG DGSVALIVDV 550 SALQAINREQ RMANTAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tandem translation starts in the cheA locus of Escherichia coli." Kofoid E.C., Parkinson J.S. J. Bacteriol. 173:2116-2119(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli." Mutoh N., Simon M.I. J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654.
[6]	"Mutants defective in bacterial chemotaxis show modified protein phosphorylation." Oosawa K., Hess J.F., Simon M.I. Cell 53:89-96(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, DOMAINS.
[7]	"Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY." McNally D.F., Matsumura P. Proc. Natl. Acad. Sci. U.S.A. 88:6269-6273(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[8]	"Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker." Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W. Biochemistry 35:433-443(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-233.
[9]	"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy." McEvoy M.M., Muhandiram D.R., Kyw L.E., Dahlquist F.W. Biochemistry 35:5633-5640(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 124-257.
[10]	"Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR." Zhou H., Dahlquist F.W. Biochemistry 36:699-710(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-134.
[11]	"Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY." Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P. Nat. Struct. Biol. 5:25-29(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228.
[12]	"Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway." McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W. Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34669 Genomic DNA. Translation: AAA23573.1.
M34669 Genomic DNA. Translation: AAA23574.1.
U00096 Genomic DNA. Translation: AAC74958.1.
AP009048 Genomic DNA. Translation: BAA15709.1.
M13462 Genomic DNA. Translation: AAA23564.1.

PIR

QRECCS. H64951.

RefSeq

NP_416402.1. NC_000913.2.
YP_490150.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A0O	X-ray	2.95	B/D/F/H	124-257	[»]
1EAY	X-ray	2.00	C/D	156-228	[»]
1FFG	X-ray	2.10	B/D	124-257	[»]
1FFS	X-ray	2.40	B/D	124-257	[»]
1FFW	X-ray	2.70	B/D	124-257	[»]
1FWP	NMR	-	A	124-257	[»]
2LP4	NMR	-	A	1-225	[»]

DisProt

DP00407.

ProteinModelPortal

P07363.

SMR

P07363. Positions 5-133, 158-226, 261-640.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6053N.

IntAct

P07363. 33 interactions.

MINT

MINT-1312842.

STRING

511145.b1888.

Proteomic databases

PaxDb

P07363.

PRIDE

P07363.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74958; AAC74958; b1888.
BAA15709; BAA15709; BAA15709.

GeneID

12932040.
946401.

KEGG

ecj:Y75_p1864.
eco:b1888.

PATRIC

32119103. VBIEscCol129921_1969.

Organism-specific databases

EchoBASE

EB0144.

EcoGene

EG10146. cheA.

Phylogenomic databases

eggNOG

COG0643.

HOGENOM

HOG000255263.

KO

K03407.

OMA

HVEIASK.

ProtClustDB

PRK10547.

Enzyme and pathway databases

BioCyc

EcoCyc:CHEA-SMALL.
EcoCyc:PROTEIN-CHEA.
ECOL316407:JW1877-MONOMER.

BRENDA

2.7.13.3. 2026.

Gene expression databases

Genevestigator

P07363.

Family and domain databases

Gene3D

1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 1 hit.

InterPro

IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_ATP-bd.
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]

Pfam

PF01584. CheW. 1 hit.
PF09078. CheY-binding. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF50341. CheW. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
SSF47226. Hpt. 1 hit.

PROSITE

PS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07363.

Entry information

Entry name

CHEA_ECOLI

Accession

Primary (citable) accession number: P07363
Secondary accession number(s): P76302

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 144 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program