Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8Q009 (CHEB1_METMA)

Last modified January 19, 2010. Version 46. 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 of group 1 operon
    EC=3.1.1.61
Gene names
Name: cheB1
Ordered Locus Names: MM_0329
OrganismMethanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier2209 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099
PRO_0000158053

Regions

Domain10 – 127118Response regulatory
Domain159 – 353195CheB-type methylesterase

Sites

Active site1711 By similarity
Active site1981 By similarity
Active site2951 By similarity

Amino acid modifications

Modified residue6114-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Q009-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 16FD4AF0D4EDF6B9

FASTA35738,425
        10         20         30         40         50         60 
MNEFGDSMIR TLIVDDSAFM RMAIRSMLAS SPDIKIAGDA CNGKEAVDKS KSLHPDIIIM 

        70         80         90        100        110        120 
DVNMPVMDGL TAVKTIMSTD PVPIIMFSTL TVEGSKEALE ALQLGAIDFV PKSESHHDVN 

       130        140        150        160        170        180 
KIEKELVDKI RNIHSSNPSI LRLINMRKFK GEVVRGKWSC AGDFAVLIGS STGGPSSLEQ 

       190        200        210        220        230        240 
VIPRLPGDLP APVFVVQHMP EGNFCKQLAE RLNFLSELEI KEARNNEKVT AGVVYIAPGG 

       250        260        270        280        290        300 
YHMTVKKALG VTRIKLIKSQ PVHAVMPAVD VIAESMLDVY GKNIVAAILT GMGFDGAAGF 

       310        320        330        340        350 
KKIRDAGGST IACSEDTCVI FGMPKAAIAA GGIDTVKPIF EIPEEIVRMS EVKCNGK 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM30025.1.
RefSeqNP_632353.2.

3D structure databases

SMRQ8Q009. Positions 7-349.
ModBaseSearch...

Genome annotation databases

GeneID1478671.
GenomeReviewsGene locus MM_0329 in contig AE008384_GR.
KEGGmma:MM_0329.
NMPDRfig|192952.1.peg.329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG705324.
OMAILIDEDM.

Enzyme and pathway databases

BioCycMMAZ192952:MM0329-MONOMER.
BRENDA3.1.1.61. 261165.

Family and domain databases

HAMAPMF_00099. CheB_methylest.
[Tree]
InterProIPR011006. CheY-like.
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.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB1_METMA
AccessionPrimary (citable) accession number: Q8Q009
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2002
Last modified: January 19, 2010
This is version 46 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