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Protein

Chemotaxis protein CheA

Gene

cheA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 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.

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

BioCyciSENT99287:GCTI-1933-MONOMER.
BRENDAi2.7.13.3. 5542.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheA (EC:2.7.13.3)
Gene namesi
Name:cheA
Ordered Locus Names:STM1921
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Chemotaxis protein CheAPRO_0000074710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP09384.
PRIDEiP09384.

Interactioni

Subunit structurei

Trimer or tetramer.

Protein-protein interaction databases

DIPiDIP-61270N.
STRINGi99287.STM1921.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi9 – 2921Combined sources
Helixi37 – 5620Combined sources
Helixi60 – 7718Combined sources
Helixi85 – 10622Combined sources
Helixi113 – 13018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I5NX-ray2.14A/B/C/D1-138[»]
ProteinModelPortaliP09384.
SMRiP09384. Positions 5-133, 163-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09384.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 105105HPtPROSITE-ProRule annotationAdd
BLAST
Domaini274 – 526253Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini528 – 663136CheW-likePROSITE-ProRule annotationAdd
BLAST

Domaini

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 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.
HOGENOMiHOG000255263.
KOiK03407.
OMAiKSTAHEH.
PhylomeDBiP09384.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 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.
[Graphical view]
PfamiPF01584. 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]
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.

P09384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMDISDFYQ TFFDEADELL ADMEQHLLDL VPESPDAEQL NAIFRAAHSI
60 70 80 90 100
KGGAGTFGFT ILQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE
110 120 130 140 150
QLDAYKNSEE PDAASFEYIC NALRQLALEA KGETTPAVVE TAALSAAIQE
160 170 180 190 200
ESVAETESPR DESKLRIVLS RLKANEVDLL EEELGNLATL TDVVKGADSL
210 220 230 240 250
SATLDGSVAE DDIVAVLCFV IEADQIAFEK VVAAPVEKAQ EKTEVAPVAP
260 270 280 290 300
PAVVAPAAKS AAHEHHAGRE KPARERESTS IRVAVEKVDQ LINLVGELVI
310 320 330 340 350
TQSMLAQRSN ELDPVNHGDL ITSMGQLQRN ARDLQESVMS IRMMPMEYVF
360 370 380 390 400
SRFPRLVRDL AGKLGKQVEL TLVGSSTELD KSLIERIIDP LTHLVRNSLD
410 420 430 440 450
HGIEMPEKRL EAGKNVVGNL ILSAEHQGGN ICIEVTDDGA GLNRERILAK
460 470 480 490 500
AMSQGMAVNE NMTDDEVGML IFAPGFSTAE QVTDVSGRGV GMDVVKRNIQ
510 520 530 540 550
EMGGHVEIQS KQGSGTTIRI LLPLTLAILD GMSVRVAGEV FILPLNAVME
560 570 580 590 600
SLQPREEDLH PLAGGERVLE VRGEYLPLVE LWKVFDVDGA KTEATQGIVV
610 620 630 640 650
ILQSAGRRYA LLVDQLIGQH QVVVKNLESN YRKVPGISAA TILGDGSVAL
660 670
IVDVSALQGL NREQRMAITA A
Length:671
Mass (Da):73,013
Last modified:July 1, 1989 - v1
Checksum:i07AFFC34FBA5DB01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03611 Genomic DNA. Translation: AAA27034.1.
AE006468 Genomic DNA. Translation: AAL20837.1.
PIRiA28959.
RefSeqiNP_460878.1. NC_003197.1.
WP_000061302.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20837; AAL20837; STM1921.
GeneIDi1253442.
KEGGistm:STM1921.
PATRICi32382399. VBISalEnt20916_2038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03611 Genomic DNA. Translation: AAA27034.1.
AE006468 Genomic DNA. Translation: AAL20837.1.
PIRiA28959.
RefSeqiNP_460878.1. NC_003197.1.
WP_000061302.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I5NX-ray2.14A/B/C/D1-138[»]
ProteinModelPortaliP09384.
SMRiP09384. Positions 5-133, 163-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61270N.
STRINGi99287.STM1921.

Proteomic databases

PaxDbiP09384.
PRIDEiP09384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20837; AAL20837; STM1921.
GeneIDi1253442.
KEGGistm:STM1921.
PATRICi32382399. VBISalEnt20916_2038.

Phylogenomic databases

eggNOGiENOG4105CBS. Bacteria.
COG0643. LUCA.
HOGENOMiHOG000255263.
KOiK03407.
OMAiKSTAHEH.
PhylomeDBiP09384.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1933-MONOMER.
BRENDAi2.7.13.3. 5542.

Miscellaneous databases

EvolutionaryTraceiP09384.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 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.
[Graphical view]
PfamiPF01584. 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]
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_SALTY
AccessioniPrimary (citable) accession number: P09384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 137 of the entry and version 1 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.