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Reviewed, UniProtKB/Swiss-Prot Q30ZJ5 (CHEB2_DESDG)

Last modified November 3, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Chemotaxis response regulator protein-glutamate methylesterase 2
    EC=3.1.1.61
Gene names
Name: cheB2
Ordered Locus Names: Dde_2104
OrganismDesulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Sequence similarities

Contains 1 cheB-type methylesterase domain.

Contains 1 response regulatory domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000225459

Regions

Domain6 – 123118Response regulatory
Domain165 – 356192CheB-type methylesterase

Sites

Active site1771 By similarity
Active site2031 By similarity
Active site2991 By similarity

Amino acid modifications

Modified residue5714-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30ZJ5-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 2FE75F6D0C172C0A

FASTA35638,050
        10         20         30         40         50         60 
MARHIKVLIV DDSALVRQTL TDIFSADPEL EVVGTASDPF VAVKRMETVV PDVILLDVAM 

        70         80         90        100        110        120 
PRMDGLTFLR KIMSQHPIPV VICSAVTEQG AEASFKAMEY GAVEIIQKPK VSTKQFLEES 

       130        140        150        160        170        180 
SIRICDAVKA AARAQLRKLA AKRFEVTPKL SADAMLPANA GRSVVQRTEK VVVVGASTGG 

       190        200        210        220        230        240 
TEALRVLLEA MPPDCPPIAI VQHMPEHFTA AFAGRLNSTC RIQVKEASDG DVMQRGQALI 

       250        260        270        280        290        300 
APGNLHLLLK RSGSRYYVET KEGPLVRRHR PSVDVLFRSA ARYAGNNAVA AIMTGMGDDG 

       310        320        330        340        350 
AAGMKELHET GAYTIAQDEA TCVVYGMPHE AVKLGGVDAV LPLGALAAAI VKACNS 

« Hide

References

[1]"Complete sequence of Desulfovibrio desulfuricans G20."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goodwin L.A., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000112 Genomic DNA. Translation: ABB38901.1.
RefSeqYP_388596.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ30ZJ5.

Genome annotation databases

GeneID3757112.
GenomeReviewsGene locus Dde_2104 in contig CP000112_GR.
KEGGdde:Dde_2104.
NMPDRfig|207559.3.peg.2064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ30ZJ5.
OMAVMCSSLT.

Enzyme and pathway databases

BioCycDDES207559:DDE_2104-MON.

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...

Entry information

Entry nameCHEB2_DESDG
AccessionPrimary (citable) accession number: Q30ZJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: December 6, 2005
Last modified: November 3, 2009
This is version 29 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)

Relevant documents

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