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Reviewed, UniProtKB/Swiss-Prot Q39T95 (CHEB2_GEOMG)

Last modified November 3, 2009. Version 35. 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: Gmet_2304
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length360 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 – 360360Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000264277

Regions

Domain5 – 120116Response regulatory
Domain163 – 356194CheB-type methylesterase

Sites

Active site1751 By similarity
Active site2021 By similarity
Active site2981 By similarity

Amino acid modifications

Modified residue5614-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39T95-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: E727D511511D4470

FASTA36038,865
        10         20         30         40         50         60 
MRKIRVVVID DSAFNRRAII KMLESMPEVV VAGYANDGEE GIRKVIDLKP DLVTLDLEMP 

        70         80         90        100        110        120 
KMDGFTLLRI IMGYCPTPVI VISAKSDDEK VFKALELGAV DFVAKPSQGI SEELLTITDD 

       130        140        150        160        170        180 
IQQKVRGVFS LNMKEIIRRE KVEVLAPPPV APKKAEAEPR RVVPCRLDVV AIGSSTGGPP 

       190        200        210        220        230        240 
AIQRILSSFR EALPLAIVIS QHMPAGFTRT FAERLNRLSV FEVKEAADGD TVWPGRVLIA 

       250        260        270        280        290        300 
PGGHNMVFEK SSGSVVVRVR KPSPEDRYIP SVDAMLASCA EVFGPRTLGV VLTGMGNDGS 

       310        320        330        340        350        360 
RGVRAIKGAG GQALAEAESS AVVFGMPREA IATGVVDKVV PLDLIAREIR MRCGVATDLD 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000148 Genomic DNA. Translation: ABB32529.1.
RefSeqYP_385254.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ39T95.

Genome annotation databases

GeneID3740459.
GenomeReviewsGene locus Gmet_2304 in contig CP000148_GR.
KEGGgme:Gmet_2304.
NMPDRfig|269799.3.peg.2548.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ39T95.
OMASQHMPAG.

Enzyme and pathway databases

BioCycGMET269799:GMET_2304-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_GEOMG
AccessionPrimary (citable) accession number: Q39T95
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 22, 2005
Last modified: November 3, 2009
This is version 35 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