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Reviewed, UniProtKB/Swiss-Prot Q2W5V5 (CHEB2_MAGSA)

Last modified November 3, 2009. Version 33. 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: amb1966
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length352 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 – 352352Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000264287

Regions

Domain6 – 124119Response regulatory
Domain162 – 350189CheB-type methylesterase

Sites

Active site1731 By similarity
Active site2001 By similarity
Active site2921 By similarity

Amino acid modifications

Modified residue5714-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W5V5-1 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: B7E7ECF3575EF499

FASTA35237,022
        10         20         30         40         50         60 
MRKKIKVLIV EDSLVVRELL KHIIGSDERF EVMAAVTSAE DCLEMLETQQ PDVISLDIRL 

        70         80         90        100        110        120 
PGMNGLDATL KIMSRRPTPI VVVAAQVDDN ELNIAMNALR AGALSVVEKP VGVTNAGYDT 

       130        140        150        160        170        180 
MAAKICTQLA IMSQVQVVRQ GINRGLNFGS DDTPARVSQG RPGTYSMVGI VASTGGPQAL 

       190        200        210        220        230        240 
VQLLGGLGAD FPLPILLVQH ITSSFLEGFV TWLSGTTPFE ARIAQDGEKP VAGKVYVAPV 

       250        260        270        280        290        300 
DHHLGLVNDQ LVILDLPAVC NQKPSGTVLF GSMARDIGKH GIGVVLTGMG ADGSEGLRQM 

       310        320        330        340        350 
ADKGAYTIVE DASTCVVNGM PAAAAKLGAA RETLPLPAIA ARLRDLALGG EK 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed: 16303747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP007255 Genomic DNA. Translation: BAE50770.1.
RefSeqYP_421329.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2W5V5.

Genome annotation databases

GeneID3804483.
GenomeReviewsGene locus amb1966 in contig AP007255_GR.
KEGGmag:amb1966.
NMPDRfig|342108.5.peg.1726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2W5V5.
OMATTRRIMA.

Enzyme and pathway databases

BioCycMMAG342108:AMB1966-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_MAGSA
AccessionPrimary (citable) accession number: Q2W5V5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 10, 2006
Last modified: November 3, 2009
This is version 33 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