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Reviewed, UniProtKB/Swiss-Prot O52262 (CHEB1_PSEPU)

Last modified June 16, 2009. Version 65. 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: cheB
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length374 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 – 374374Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099
PRO_0000158013

Regions

Domain4 – 121118Response regulatory
Domain183 – 374192CheB-type methylesterase

Sites

Active site1981 By similarity
Active site2251 By similarity
Active site3181 By similarity

Amino acid modifications

Modified residue5514-aspartylphosphate By similarity

Natural variations

Natural variant141 – 1477RPAPVAA → LAGAGRR in MK1. HAMAP MF_00099
Natural variant193 – 1942VA → LR in MK1. HAMAP MF_00099

Sequences

Sequence LengthMass (Da)Tools
O52262-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 47ED6595DF7BE388

FASTA37439,696
        10         20         30         40         50         60 
MAVKVLVVDD SGFFRRRVSE ILSADPTIQV VGTATNGKEA IDQALALKPD VITMDYEMPM 

        70         80         90        100        110        120 
MDGITAVRHI MQRCPTPVLM FSSLTHEGAR VTLDALDAGA VDYLPKNFED ISRNPDKVKQ 

       130        140        150        160        170        180 
MLCEKVHTIS RSNRRLGSYA RPAPVAAPVP ASSPAPASSF ASPAPARPAA TARAAAPAAS 

       190        200        210        220        230        240 
HSPAPKRKPY KLVAIGTSTG GPVALQRVLT QLPANFPAPI VLIQHMPAAF TKAFAERLDK 

       250        260        270        280        290        300 
LCRINVKEAE DGDMLRPGLA LLAPGGKQMM IDGRGTVKIL PGDERLNYKP CVDITFGSAA 

       310        320        330        340        350        360 
KSYGDKVLSV VLTGMGADGR EGARLLKQGG STVWAQDEAS CVIYGMPMAI VKANLADAVY 

       370 
SLDDIGKHLV EACV 

« Hide

References

[1]"Identification of a chemotaxis gene region from Pseudomonas putida."
Ditty J.L., Grimm A.C., Harwood C.S.
FEMS Microbiol. Lett. 159:267-273(1998) [PubMed: 9503621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PRS2000.
[2]"The G-protein FlhF has a role in polar flagellar placement and general stress response induction in Pseudomonas putida."
Pandza S., Baetens M., Park C.H., Au T., Keyhan M., Matin A.
Mol. Microbiol. 36:414-423(2000) [PubMed: 10792727] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MK1.

Cross-references

Sequence databases

AF031898 Genomic DNA. Translation: AAC08065.1.
AF183382 Genomic DNA. Translation: AAF67048.1.

3D structure databases

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

Enzyme and pathway databases

BRENDA3.1.1.61. 403.

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 nameCHEB1_PSEPU
AccessionPrimary (citable) accession number: O52262
Secondary accession number(s): Q9L942
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 65 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