Skip Header

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

P62641 (CHEB1_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:LIC_12455
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

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.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-glutamate methylesterase activity

Inferred from electronic annotation. Source: EC

two-component response regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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_0000157999

Regions

Domain7 – 125119Response regulatory
Domain162 – 355194CheB-type methylesterase

Sites

Active site1741 By similarity
Active site2011 By similarity
Active site2971 By similarity

Amino acid modifications

Modified residue5814-aspartylphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P62641 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: FE34A505FEC17E6B

FASTA35738,712
        10         20         30         40         50         60 
MIPNPVRAVI IDDSLLVRNI ISDQIQKDSK IHVVATGKTG MDCIDLAQKM NPDVIILDVE 

        70         80         90        100        110        120 
MPVMDGLTAL HELQKKKLGI PVIMLSVLTQ NGAEATFKAL EYGAIDFVPK PSSVFQFDPE 

       130        140        150        160        170        180 
EIGNILKSKI LAYFESKIQI PSQNLLKKAP AYSKVPAGSH LKKSPIQAIC IGTSTGGPRA 

       190        200        210        220        230        240 
LQEVFSRIPA DISLPILVVQ HMPAGFTKAF ATRLNDHAKI KVKEAEDGEP IEPNTGYVAP 

       250        260        270        280        290        300 
GDAHLSIQSK GGRKWIALNR EAPVNGHRPS IEVLLDSAIE EYKSGIIGVI MTGMGKDGSA 

       310        320        330        340        350 
AIVRVREIGG STIAQDEQTS VIYGMNRQAV EMGGVEYIEP VTEIINRIQI ILKERGI

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016823 Genomic DNA. Translation: AAS71021.1.
RefSeqYP_002384.1. NC_005823.1.

3D structure databases

ProteinModelPortalP62641.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2772514.
GenomeReviewsGene locus LIC_12455 in contig AE016823_GR.
KEGGlic:LIC12455.
PATRIC22377548. VBILepInt6257_2932.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG705324.
OMAVPIFVVQ.
PhylomeDBP62641.
ProtClustDBCLSK573833.

Enzyme and pathway databases

BioCycLINT-130-01:LINT-130-01-002384-MONOMER.
LINT267671:LIC_12455-MONOMER.

Family and domain databases

HAMAPMF_00099. CheB_methylest.
[Tree]
InterProIPR011006. CheY-like_superfamily.
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.
KOK03412.
PfamPF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTSM00448. REC. 1 hit.
[Graphical view]
SUPFAMSSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit.
SSF52172. CheY_like. 1 hit.
PROSITEPS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHEB1_LEPIC
AccessionPrimary (citable) accession number: P62641
Secondary accession number(s): Q72PL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents