Chemotaxis protein CheA - Salmonella typhimurium

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P09384 (CHEA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chemotaxis protein CheA
EC=2.7.13.3

Gene names

Name:	cheA
Ordered Locus Names:	STM1921

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	671 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	Trimer or tetramer.
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.
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
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 electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 671

671

Chemotaxis protein CheA

PRO_0000074710

Regions

Domain

1 – 105

105

HPt

Domain

274 – 526

253

Histidine kinase

Domain

528 – 663

136

CheW-like

Amino acid modifications

Modified residue

Phosphohistidine; by autocatalysis

Secondary structure

671

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P09384 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 07AFFC34FBA5DB01
Show »

FASTA

671

73,013

        10         20         30         40         50         60 
MSMDISDFYQ TFFDEADELL ADMEQHLLDL VPESPDAEQL NAIFRAAHSI KGGAGTFGFT 

        70         80         90        100        110        120 
ILQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKNSEE PDAASFEYIC 

       130        140        150        160        170        180 
NALRQLALEA KGETTPAVVE TAALSAAIQE ESVAETESPR DESKLRIVLS RLKANEVDLL 

       190        200        210        220        230        240 
EEELGNLATL TDVVKGADSL SATLDGSVAE DDIVAVLCFV IEADQIAFEK VVAAPVEKAQ 

       250        260        270        280        290        300 
EKTEVAPVAP PAVVAPAAKS AAHEHHAGRE KPARERESTS IRVAVEKVDQ LINLVGELVI 

       310        320        330        340        350        360 
TQSMLAQRSN ELDPVNHGDL ITSMGQLQRN ARDLQESVMS IRMMPMEYVF SRFPRLVRDL 

       370        380        390        400        410        420 
AGKLGKQVEL TLVGSSTELD KSLIERIIDP LTHLVRNSLD HGIEMPEKRL EAGKNVVGNL 

       430        440        450        460        470        480 
ILSAEHQGGN ICIEVTDDGA GLNRERILAK AMSQGMAVNE NMTDDEVGML IFAPGFSTAE 

       490        500        510        520        530        540 
QVTDVSGRGV GMDVVKRNIQ EMGGHVEIQS KQGSGTTIRI LLPLTLAILD GMSVRVAGEV 

       550        560        570        580        590        600 
FILPLNAVME SLQPREEDLH PLAGGERVLE VRGEYLPLVE LWKVFDVDGA KTEATQGIVV 

       610        620        630        640        650        660 
ILQSAGRRYA LLVDQLIGQH QVVVKNLESN YRKVPGISAA TILGDGSVAL IVDVSALQGL 

       670 
NREQRMAITA A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CheA protein, a central regulator of bacterial chemotaxis, belongs to a family of proteins that control gene expression in response to changing environmental conditions." Stock A., Chen T., Welsh D., Stock J. Proc. Natl. Acad. Sci. U.S.A. 85:1403-1407(1988) [PubMed: 3278311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03611 Genomic DNA. Translation: AAA27034.1.
AE006468 Genomic DNA. Translation: AAL20837.1.

PIR

A28959.

RefSeq

NP_460878.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I5N	X-ray	2.14	A/B/C/D	1-138	[»]

ProteinModelPortal

P09384.

SMR

P09384. Positions 5-133, 163-231.

ModBase

Search...

Proteomic databases

PRIDE

P09384.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1253442.

GenomeReviews

Gene locus STM1921 in contig AE006468_GR.

KEGG

stm:STM1921.

PATRIC

32382399. VBISalEnt20916_2038.

Phylogenomic databases

HOGENOM

HBG705053.

OMA

LARICAV.

ProtClustDB

PRK10547.

Enzyme and pathway databases

BioCyc

STYP99287:STM1921-MONOMER.

BRENDA

2.7.13.3. 5542.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR002545. CheW.
IPR015162. CheY-binding.
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]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.70.400. G3DSA:3.30.70.400. 1 hit.
G3DSA:1.20.120.160. Sig_transdc_His_kin_Hpt_dom. 1 hit.
G3DSA:1.10.287.560. Sig_transdc_His_kin_subgr_dim. 1 hit.

K03407.

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...

Entry information

Entry name

CHEA_SALTY

Accession

Primary (citable) accession number: P09384

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents