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Reviewed, UniProtKB/Swiss-Prot Q8VL08 (CHEB2_AZOBR)

Last modified June 16, 2009. Version 36. 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 2 operon
    EC=3.1.1.61
Gene names
Name: cheB
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length394 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 – 394394Chemotaxis response regulator protein-glutamate methylesterase of group 2 operon HAMAP MF_00099
PRO_0000157974

Regions

Domain27 – 145119Response regulatory
Domain191 – 393203CheB-type methylesterase

Sites

Active site2111 By similarity
Active site2381 By similarity
Active site3351 By similarity

Amino acid modifications

Modified residue7814-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VL08-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 55FBCF8D432A02BD

FASTA39440,986
        10         20         30         40         50         60 
MSDGFGRPPP PAPAGHPTGA AGGDPVRVMV VDDSAVIRGL LTRALEGDTE IRVVASVGDG 

        70         80         90        100        110        120 
QMAVNALQRN SLDVIVLDIE MPVMDGLTAI PKLLAVAPQV KIIMASTLTL RGADISMRCL 

       130        140        150        160        170        180 
SAGAADYIPK PTSTREIGGA DAFKRELVSK VKALGAAARR AGSRTRGELR PLNPVPAAFL 

       190        200        210        220        230        240 
KREPPPVTLR PAPAVGSVGQ VKPDVIAIGS STGGPQALFE VLAHLKTGVT QPILITQHMP 

       250        260        270        280        290        300 
ATFTTILAEH ITRQCGMNAQ EAKDGEPVVP GRCYIAPGDF HMLVTQRAGA NVISLTKDPP 

       310        320        330        340        350        360 
ENFCRPAVDP MMRSILRAFG GRKVLACILT GMGQDGLKGC TEVVNAGGTL IAQDEASSVV 

       370        380        390 
WGMPGAVAQA GICSAVLPLK EIGPYIRKFA SRAA 

« Hide

References

[1]"A major chemotaxis gene cluster in Azospirillum brasilense and relationships between chemotaxis operons in alpha-proteobacteria."
Hauwaerts D., Alexandre G., Das S.K., Vanderleyden J., Zhulin I.B.
FEMS Microbiol. Lett. 208:61-67(2002) [PubMed: 11934495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

Cross-references

Sequence databases

AF450326 Genomic DNA. Translation: AAL47024.1.

3D structure databases

HSSPHSSP built from PDB template 1CHD based on UniProtKB P04042.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.61. 1315.

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_AZOBR
AccessionPrimary (citable) accession number: Q8VL08
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2002
Last modified: June 16, 2009
This is version 36 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