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Reviewed, UniProtKB/Swiss-Prot P04042 (CHEB_SALTY)

Last modified June 16, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 MF_00099

Catalytic activity

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

Subcellular location

Cytoplasm. HAMAP MF_00099

Domain

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

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Sites

Active site1641 HAMAP MF_00099
Active site1901 HAMAP MF_00099
Active site2861 HAMAP MF_00099

Amino acid modifications

Modified residue5614-aspartylphosphate HAMAP MF_00099

Secondary structure

1 .................................................................. 349
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P04042-1 [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

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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: 2991277] [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: 11677609] [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: 3539934] [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: 3280143] [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: 9760239] [Abstract]
Cited for: CHARACTERIZATION.
[6]"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: 7608974] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 152-349.
[7]"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: 9465023] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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Cross-references

Sequence databases

AE008785 Genomic DNA. Translation: AAL20833.1.
PIRXYEBET. A00547.
RefSeqNP_460874.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A2OX-ray2.40A/B1-349[»]
1CHDX-ray1.75A147-349[»]
ModBaseSearch...

Genome annotation databases

GeneID1253438.
GenomeReviewsGene locus STM1917 in contig AE006468_GR.
KEGGstm:STM1917.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP04042.
OMAP04042. SGANYVI.

Enzyme and pathway databases

BioCycSTYP99287:STM1917-MON.
BRENDA3.1.1.61. 2.

Family and domain databases

HAMAPMF_00099.
[Tree]
InterProIPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
Gene3DG3DSA:3.40.50.180. Chemotax_RR_pGlu_Me-esterase. 1 hit.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
ProDomPD005328. CheB_methylest. 1 hit.
PD000039. Response_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00448. REC. 1 hit.
[Graphical view]
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: June 16, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents