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Reviewed, UniProtKB/Swiss-Prot Q2FQU2 (CHEB2_METHJ)

Last modified November 3, 2009. Version 28. 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: Mhun_0988
OrganismMethanospirillum hungatei (strain JF-1 / DSM 864) [Complete proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length350 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 – 350350Chemotaxis response regulator protein-glutamate methylesterase 2 HAMAP MF_00099
PRO_0000264339

Regions

Domain3 – 118116Response regulatory
Domain158 – 348191CheB-type methylesterase

Sites

Active site1701 By similarity
Active site1971 By similarity
Active site2901 By similarity

Amino acid modifications

Modified residue5414-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FQU2-1 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 7F4FF7EC18BD6643

FASTA35038,184
        10         20         30         40         50         60 
MIRVLLVDDS PVTLMVLQSI LEKEPDISVI GQAKNGKEAI ILASRLAPDI ITMDINMPDL 

        70         80         90        100        110        120 
DGFATTRQIM ERTPVPIIIV SGIDNLEEIR ASFRAVEAGA LAVFRKPPAY GDPDYEEAVS 

       130        140        150        160        170        180 
EFVNAIRTYS EVKVIRRRSN HLKVPKPEAS TIQIPFQIHQ DIRVIVIGAS TGGPQVIQEI 

       190        200        210        220        230        240 
ISNLPLGFPL PLVLVQHMSP GFIEGLALWL TESTGFPVSI AREGEVLQPG KLYVAPDGIH 

       250        260        270        280        290        300 
TGVTSDLRFS FSISPPEHNL RPSVSYLFRS AAKNLGSHVL GILLSGMGSD GAEELLQIRQ 

       310        320        330        340        350 
NGGCTIIQDR DSSFVYGMPG AAEMLNAGMF SLPPVEIARF LRSLSERRQL 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000254 Genomic DNA. Translation: ABD40738.1.
RefSeqYP_502457.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2FQU2.

Genome annotation databases

GeneID3924035.
GenomeReviewsGene locus Mhun_0988 in contig CP000254_GR.
KEGGmhu:Mhun_0988.
NMPDRfig|323259.5.peg.1041.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2FQU2.
OMAEESSAVW.

Enzyme and pathway databases

BioCycMHUN323259:MHUN_0988-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_METHJ
AccessionPrimary (citable) accession number: Q2FQU2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 21, 2006
Last modified: November 3, 2009
This is version 28 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