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P04042

- CHEB_SALTY

UniProt

P04042 - CHEB_SALTY

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
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1986)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    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

    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...
    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

    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: October 1, 2014
    This is version 133 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