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Protein

Chemotaxis response regulator protein-glutamate methylesterase

Gene

cheB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The MCP methylation state of the cell is crucial for sensory responses and adaptations.

Catalytic activityi

Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1641
Active sitei1901
Active sitei2861

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis response regulator protein-glutamate methylesterase (EC:3.1.1.61)
Gene namesi
Name:cheB
Ordered Locus Names:STM1917
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene display a strong clockwise motor bias; in combination with a yhjH disruption cells switch to a counterclockwise bias.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001580271 – 349Chemotaxis response regulator protein-glutamate methylesteraseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei564-aspartylphosphate1 Publication1

Post-translational modificationi

Phosphorylated by CheA.1 Publication
Two forms were isolated, the intact protein and a proteolytic fragment (146-349) that is 15-fold more active than its precursor.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04042.
PRIDEiP04042.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1917.

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi13 – 24Combined sources12
Beta strandi29 – 37Combined sources9
Helixi38 – 48Combined sources11
Beta strandi51 – 56Combined sources6
Beta strandi60 – 62Combined sources3
Helixi64 – 73Combined sources10
Beta strandi79 – 83Combined sources5
Helixi87 – 99Combined sources13
Beta strandi103 – 106Combined sources4
Beta strandi108 – 111Combined sources4
Helixi116 – 132Combined sources17
Helixi135 – 138Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi158 – 163Combined sources6
Helixi167 – 175Combined sources9
Beta strandi184 – 189Combined sources6
Helixi195 – 206Combined sources12
Beta strandi208 – 213Combined sources6
Beta strandi224 – 227Combined sources4
Beta strandi232 – 239Combined sources8
Beta strandi242 – 248Combined sources7
Beta strandi253 – 255Combined sources3
Beta strandi256 – 258Combined sources3
Helixi260 – 270Combined sources11
Helixi272 – 274Combined sources3
Beta strandi275 – 279Combined sources5
Beta strandi281 – 285Combined sources5
Helixi288 – 296Combined sources9
Beta strandi300 – 304Combined sources5
Turni306 – 308Combined sources3
Beta strandi310 – 313Combined sources4
Helixi314 – 320Combined sources7
Beta strandi325 – 328Combined sources4
Helixi330 – 332Combined sources3
Helixi333 – 341Combined sources9
Turni342 – 346Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2OX-ray2.40A/B1-349[»]
1CHDX-ray1.75A147-349[»]
ProteinModelPortaliP04042.
SMRiP04042.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 122Response regulatoryPROSITE-ProRule annotationAdd BLAST118
Domaini152 – 344CheB-type methylesteraseAdd BLAST193

Domaini

The N-terminal domain interferes with esterase activity and is not essential for catalysis.

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CMP. Bacteria.
COG2201. LUCA.
HOGENOMiHOG000151423.
KOiK03412.
OMAiMLEMHRA.
PhylomeDBiP04042.

Family and domain databases

Gene3Di3.40.50.180. 1 hit.
HAMAPiMF_00099. CheB_methylest. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFiPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF52738. SSF52738. 1 hit.
PROSITEiPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04042-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP
60 70 80 90 100
DVLTLDVEMP RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG
110 120 130 140 150
AIDFVTKPQL GIREGMLAYS EMIAEKVRTA ARARIAAHKP MAAPTTLKAG
160 170 180 190 200
PLLSSEKLIA IGASTGGTEA IRHVLQPLPL SSPAVIITQH MPPGFTRSFA
210 220 230 240 250
ERLNKLCQIS VKEAEDGERV LPGHAYIAPG DKHMELARSG ANYQIKIHDG
260 270 280 290 300
PPVNRHRPSV DVLFHSVAKH AGRNAVGVIL TGMGNDGAAG MLAMYQAGAW
310 320 330 340
TIAQNEASCV VFGMPREAIN MGGVSEVVDL SQVSQQMLAK ISAGQAIRI
Length:349
Mass (Da):37,552
Last modified:November 1, 1986 - v1
Checksum:i79BAFC2D202F2F8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL20833.1.
PIRiA00547. XYEBET.
RefSeqiNP_460874.1. NC_003197.1.
WP_000036392.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20833; AAL20833; STM1917.
GeneIDi1253438.
KEGGistm:STM1917.
PATRICi32382389. VBISalEnt20916_2033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL20833.1.
PIRiA00547. XYEBET.
RefSeqiNP_460874.1. NC_003197.1.
WP_000036392.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2OX-ray2.40A/B1-349[»]
1CHDX-ray1.75A147-349[»]
ProteinModelPortaliP04042.
SMRiP04042.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1917.

Proteomic databases

PaxDbiP04042.
PRIDEiP04042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20833; AAL20833; STM1917.
GeneIDi1253438.
KEGGistm:STM1917.
PATRICi32382389. VBISalEnt20916_2033.

Phylogenomic databases

eggNOGiENOG4105CMP. Bacteria.
COG2201. LUCA.
HOGENOMiHOG000151423.
KOiK03412.
OMAiMLEMHRA.
PhylomeDBiP04042.

Miscellaneous databases

EvolutionaryTraceiP04042.

Family and domain databases

Gene3Di3.40.50.180. 1 hit.
HAMAPiMF_00099. CheB_methylest. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFiPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF52738. SSF52738. 1 hit.
PROSITEiPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHEB_SALTY
AccessioniPrimary (citable) accession number: P04042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: November 2, 2016
This is version 146 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, Direct protein sequencing, 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.