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P04042 (CHEB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chemotaxis response regulator protein-glutamate methylesterase

EC=3.1.1.61
Gene names
Name:cheB
Ordered Locus Names:STM1917
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00099

Catalytic activity

Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP-Rule MF_00099

Subcellular location

Cytoplasm HAMAP-Rule MF_00099.

Domain

The N-terminal domain interferes with esterase activity and is not essential for catalysis. HAMAP-Rule MF_00099

Post-translational modification

Phosphorylated by CheA. Ref.4

Two forms were isolated, the intact protein and a proteolytic fragment (146-349) that is 15-fold more active than its precursor. HAMAP-Rule MF_00099

Disruption phenotype

Cells lacking this gene display a strong clockwise motor bias; in combination with a yhjH disruption cells switch to a counterclockwise bias. Ref.6

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

sensory perception of chemical stimulus

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphorelay response regulator activity

Inferred from electronic annotation. Source: InterPro

protein-glutamate methylesterase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Chemotaxis response regulator protein-glutamate methylesterase HAMAP-Rule MF_00099
PRO_0000158027

Regions

Domain5 – 122118Response regulatory
Domain152 – 344193CheB-type methylesterase

Sites

Active site1641
Active site1901
Active site2861

Amino acid modifications

Modified residue5614-aspartylphosphate HAMAP-Rule MF_00099

Secondary structure

..................................................................... 349
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04042 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 79BAFC2D202F2F8B

FASTA34937,552
        10         20         30         40         50         60 
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP DVLTLDVEMP 

        70         80         90        100        110        120 
RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG AIDFVTKPQL GIREGMLAYS 

       130        140        150        160        170        180 
EMIAEKVRTA ARARIAAHKP MAAPTTLKAG PLLSSEKLIA IGASTGGTEA IRHVLQPLPL 

       190        200        210        220        230        240 
SSPAVIITQH MPPGFTRSFA ERLNKLCQIS VKEAEDGERV LPGHAYIAPG DKHMELARSG 

       250        260        270        280        290        300 
ANYQIKIHDG PPVNRHRPSV DVLFHSVAKH AGRNAVGVIL TGMGNDGAAG MLAMYQAGAW 

       310        320        330        340 
TIAQNEASCV VFGMPREAIN MGGVSEVVDL SQVSQQMLAK ISAGQAIRI 

« Hide

References

« Hide 'large scale' references
[1]"Multiple forms of the CheB methylesterase in bacterial chemosensing."
Simms S.A., Keane M.G., Stock J.
J. Biol. Chem. 260:10161-10168(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[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. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Active site of the enzyme which demethylates receptors during bacterial chemotaxis."
Simms S.A., Cornman E.W., Mottonen J., Stock J.
J. Biol. Chem. 262:29-31(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 277-306.
[4]"Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis."
Hess J.F., Oosawa K., Kaplan N., Simon M.I.
Cell 53:79-87(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"Activation of methylesterase CheB: evidence of a dual role for the regulatory domain."
Anand G.S., Goudreau P.N., Stock A.M.
Biochemistry 37:14038-14047(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."
Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.
Mol. Cell 38:128-139(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023.
[7]"Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB."
West A.H., Martinez-Hackert E., Stock A.M.
J. Mol. Biol. 250:276-290(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 152-349.
[8]"Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain."
Djordjevic S., Goudreau P.N., Xu Q., Stock A.M., West A.H.
Proc. Natl. Acad. Sci. U.S.A. 95:1381-1386(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL20833.1.
PIRXYEBET. A00547.
RefSeqNP_460874.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2OX-ray2.40A/B1-349[»]
1CHDX-ray1.75A147-349[»]
ProteinModelPortalP04042.
SMRP04042. Positions 1-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1917.

Proteomic databases

PRIDEP04042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20833; AAL20833; STM1917.
GeneID1253438.
KEGGstm:STM1917.
PATRIC32382389. VBISalEnt20916_2033.

Phylogenomic databases

HOGENOMHOG000151423.
KOK03412.
OMAANYQVKL.
OrthoDBEOG6PKFC7.
ProtClustDBPRK00742.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1929-MONOMER.

Family and domain databases

Gene3D3.40.50.180. 1 hit.
HAMAPMF_00099. CheB_methylest.
InterProIPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52172. SSF52172. 1 hit.
SSF52738. SSF52738. 1 hit.
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04042.

Entry information

Entry nameCHEB_SALTY
AccessionPrimary (citable) accession number: P04042
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references