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Q52883 (CHEB1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:R00642
ORF Names:SMc03010
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length349 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

Miscellaneous

R.meliloti does not have a group 2 operon. 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 – 349349Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099
PRO_0000158019

Regions

Domain6 – 123118Response regulatory
Domain152 – 344193CheB-type methylesterase

Sites

Active site1641 By similarity
Active site1901 By similarity
Active site2861 By similarity

Amino acid modifications

Modified residue5714-aspartylphosphate By similarity

Experimental info

Sequence conflict311T → S in AAA86677. Ref.1
Sequence conflict1141T → P in AAA86677. Ref.1
Sequence conflict1521S → Y in AAA86677. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q52883 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 042C3986FC12FBA9

FASTA34936,908
        10         20         30         40         50         60 
MSAPARVLVV DDSATMRGLI SAVLNADPDI TVVGQAADAL EARQAIKQLD PDVVTLDIEM 

        70         80         90        100        110        120 
PNMNGLEFLD KIMRLRPMPV IMVSTLTHRG AEATIAALEI GAFDCVGKPQ PGDTHPFRDL 

       130        140        150        160        170        180 
ADKVKAAARS QRKSMITSNR AAAPAATAVS DSRAGRKIVA IGASTGGVEA LITVLQKFPA 

       190        200        210        220        230        240 
NCPPTVITQH MPHTFTKSFA ERLNRLCAPT VQEATDGARL EVGRVYLAPG GERHLEVHNA 

       250        260        270        280        290        300 
AAPCCRLVDH PPVNGHRPSV DVLFDSVAEL AGRNAIGVIL TGMGRDGAAG LLKLRHAGAR 

       310        320        330        340 
TFGQNEKTCV VYGMPRVAYE LGAVETQLPL GSIGEEILKT AAARKEGIE 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a chemotaxis operon in Rhizobium meliloti."
Greck M., Platzer J., Sourjik V., Schmitt R.
Mol. Microbiol. 15:989-1000(1995) [PubMed: 7623670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RU11/001.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13166 Genomic DNA. Translation: AAA86677.1.
AL591688 Genomic DNA. Translation: CAC45214.1.
PIRS61837.
RefSeqNP_384748.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ52883.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1232281.
GenomeReviewsGene locus R00642 in contig AL591688_GR.
KEGGsme:SMc03010.
NMPDRfig|266834.1.peg.1936.
PATRIC23630499. VBISinMel96828_2015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG705324.
OMACAGANTT.
ProtClustDBPRK00742.

Enzyme and pathway databases

BioCycSMEL266834:SMC03010-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_RHIME
AccessionPrimary (citable) accession number: Q52883
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 2, 2001
Last modified: January 25, 2012
This is version 93 of the entry and version 2 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