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Q1LH11 (CHEB1_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chemotaxis response regulator protein-glutamate methylesterase 1

EC=3.1.1.61
Gene names
Name:cheB1
Ordered Locus Names:Rmet_3693
Encoded onPlasmid megaplasmid CH34
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR By similarity. 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 regulatory domain inhibits the activity of the C-terminal effector domain. HAMAP MF_00099

Post-translational modification

Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain By similarity. HAMAP MF_00099

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-glutamate methylesterase activity

Inferred from electronic annotation. Source: EC

two-component response regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Chemotaxis response regulator protein-glutamate methylesterase 1 HAMAP MF_00099
PRO_0000264300

Regions

Domain7 – 124118Response regulatory
Domain158 – 350193CheB-type methylesterase

Sites

Active site1701 By similarity
Active site1961 By similarity
Active site2921 By similarity

Amino acid modifications

Modified residue5814-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LH11 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 6E1B43BD2A897D77

FASTA35738,474
        10         20         30         40         50         60 
MTAAKIKVLC VDDSALIRSL MSEIINSQPD MEVVGTAPDP LVARDLIKRV NPDVLTLDVE 

        70         80         90        100        110        120 
MPRMDGLDFL ERLMRLRPMP VLMVSSLTER GSEITMRALE LGAVDFVTKP KLGIREGLLD 

       130        140        150        160        170        180 
YTQTIADKIR AASRARVRAR AEQSAGAAPV APMLRAPLLS TEKLIIVGAS TGGTEAIKDF 

       190        200        210        220        230        240 
LTPLPPDSPA VMIVQHMPAG FTKSFAHRLN GLCRITVKEA EHGERVLPGY AYIAPGDSHL 

       250        260        270        280        290        300 
LLARSGANYV AHLSQEAPVN RHRPSVDVLF DSAAIHGGKN VTGVILTGMG KDGARGMLRM 

       310        320        330        340        350 
REAGAYNLAQ DEQSCIVFGM PKEAIAAGGV HEVVPLHQMS QRVMAHLATF GARAQRV 

« Hide

References

[1]"Complete sequence of the megaplasmid of Ralstonia metallidurans CH34."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000353 Genomic DNA. Translation: ABF10565.1.
RefSeqYP_585834.1. NC_007974.2.

3D structure databases

ProteinModelPortalQ1LH11.
SMRQ1LH11. Positions 4-348.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LH11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4040664.
GenomeReviewsGene locus Rmet_3693 in contig CP000353_GR.
KEGGrme:Rmet_3693.
PATRIC20292098. VBIRalMet4734_4100.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2201.
HOGENOMHBG705324.
OMAFVTKPKL.
PhylomeDBQ1LH11.
ProtClustDBPRK00742.

Enzyme and pathway databases

BioCycRMET266264:RMET_3693-MONOMER.

Family and domain databases

HAMAPMF_00099. CheB_methylest.
[Tree]
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]
Gene3DG3DSA:3.40.50.180. Chemotax_RR_pGlu_Me-esterase. 1 hit.
KOK03412.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit.
SSF52172. CheY_like. 1 hit.
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB1_RALME
AccessionPrimary (citable) accession number: Q1LH11
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 40 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