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P04042

- CHEB_SALTY

UniProt

P04042 - CHEB_SALTY

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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: 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)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

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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 methylesterasePRO_0000158027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 5614-aspartylphosphate1 Publication

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

PRIDEiP04042.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1917.

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 2412Combined sources
Beta strandi29 – 379Combined sources
Helixi38 – 4811Combined sources
Beta strandi51 – 566Combined sources
Beta strandi60 – 623Combined sources
Helixi64 – 7310Combined sources
Beta strandi79 – 835Combined sources
Helixi87 – 9913Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi108 – 1114Combined sources
Helixi116 – 13217Combined sources
Helixi135 – 1384Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1636Combined sources
Helixi167 – 1759Combined sources
Beta strandi184 – 1896Combined sources
Helixi195 – 20612Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi232 – 2398Combined sources
Beta strandi242 – 2487Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi256 – 2583Combined sources
Helixi260 – 27011Combined sources
Helixi272 – 2743Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi281 – 2855Combined sources
Helixi288 – 2969Combined sources
Beta strandi300 – 3045Combined sources
Turni306 – 3083Combined sources
Beta strandi310 – 3134Combined sources
Helixi314 – 3207Combined sources
Beta strandi325 – 3284Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 3419Combined sources
Turni342 – 3465Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP04042.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 122118Response regulatoryAdd
BLAST
Domaini152 – 344193CheB-type methylesteraseAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 response regulatory domain.Curated

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

        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.

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 .
PIRi A00547. XYEBET.
RefSeqi NP_460874.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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: AUTOPHOSPHORYLATION.
  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), PHOSPHORYLATION AT ASP-56.

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 26, 2014
This is version 135 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