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P04042

- CHEB_SALTY

UniProt

P04042 - CHEB_SALTY

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Protein
Chemotaxis response regulator protein-glutamate methylesterase
Gene
cheB, STM1917
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641
Active sitei190 – 1901
Active sitei286 – 2861

GO - Molecular functioni

  1. phosphorelay response regulator activity Source: InterPro
  2. protein-glutamate methylesterase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. chemotaxis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1929-MONOMER.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Chemotaxis response regulator protein-glutamate methylesteraseUniRule annotation
PRO_0000158027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 5614-aspartylphosphateUniRule annotation

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.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP04042.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1917.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Helixi13 – 2412
Beta strandi29 – 379
Helixi38 – 4811
Beta strandi51 – 566
Beta strandi60 – 623
Helixi64 – 7310
Beta strandi79 – 835
Helixi87 – 9913
Beta strandi103 – 1064
Beta strandi108 – 1114
Helixi116 – 13217
Helixi135 – 1384
Beta strandi153 – 1553
Beta strandi158 – 1636
Helixi167 – 1759
Beta strandi184 – 1896
Helixi195 – 20612
Beta strandi208 – 2136
Beta strandi224 – 2274
Beta strandi232 – 2398
Beta strandi242 – 2487
Beta strandi253 – 2553
Beta strandi256 – 2583
Helixi260 – 27011
Helixi272 – 2743
Beta strandi275 – 2795
Beta strandi281 – 2855
Helixi288 – 2969
Beta strandi300 – 3045
Turni306 – 3083
Beta strandi310 – 3134
Helixi314 – 3207
Beta strandi325 – 3284
Helixi330 – 3323
Helixi333 – 3419
Turni342 – 3465

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2OX-ray2.40A/B1-349[»]
1CHDX-ray1.75A147-349[»]
ProteinModelPortaliP04042.
SMRiP04042. Positions 1-347.

Miscellaneous databases

EvolutionaryTraceiP04042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 122118Response regulatory
Add
BLAST
Domaini152 – 344193CheB-type methylesterase
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000151423.
KOiK03412.
OMAiEVVDLHQ.
OrthoDBiEOG6PKFC7.
PhylomeDBiP04042.

Family and domain databases

Gene3Di3.40.50.180. 1 hit.
HAMAPiMF_00099. CheB_methylest.
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

MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP    50
DVLTLDVEMP RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG 100
AIDFVTKPQL GIREGMLAYS EMIAEKVRTA ARARIAAHKP MAAPTTLKAG 150
PLLSSEKLIA IGASTGGTEA IRHVLQPLPL SSPAVIITQH MPPGFTRSFA 200
ERLNKLCQIS VKEAEDGERV LPGHAYIAPG DKHMELARSG ANYQIKIHDG 250
PPVNRHRPSV DVLFHSVAKH AGRNAVGVIL TGMGNDGAAG MLAMYQAGAW 300
TIAQNEASCV VFGMPREAIN MGGVSEVVDL SQVSQQMLAK ISAGQAIRI 349
Length:349
Mass (Da):37,552
Last modified:November 1, 1986 - v1
Checksum:i79BAFC2D202F2F8B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL20833.1.
PIRiA00547. XYEBET.
RefSeqiNP_460874.1. NC_003197.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL20833.1 .
PIRi A00547. XYEBET.
RefSeqi NP_460874.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A2O X-ray 2.40 A/B 1-349 [» ]
1CHD X-ray 1.75 A 147-349 [» ]
ProteinModelPortali P04042.
SMRi P04042. Positions 1-347.
ModBasei Search...

Protein-protein interaction databases

STRINGi 99287.STM1917.

Proteomic databases

PRIDEi P04042.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20833 ; AAL20833 ; STM1917 .
GeneIDi 1253438.
KEGGi stm:STM1917.
PATRICi 32382389. VBISalEnt20916_2033.

Phylogenomic databases

HOGENOMi HOG000151423.
KOi K03412.
OMAi EVVDLHQ.
OrthoDBi EOG6PKFC7.
PhylomeDBi P04042.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-1929-MONOMER.

Miscellaneous databases

EvolutionaryTracei P04042.

Family and domain databases

Gene3Di 3.40.50.180. 1 hit.
HAMAPi MF_00099. CheB_methylest.
InterProi IPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view ]
Pfami PF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view ]
PIRSFi PIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTi SM00448. REC. 1 hit.
[Graphical view ]
SUPFAMi SSF52172. SSF52172. 1 hit.
SSF52738. SSF52738. 1 hit.
PROSITEi PS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

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: September 3, 2014
This is version 132 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

External Data

Dasty 3

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