Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chemotaxis protein methyltransferase

Gene

cheR

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.

Catalytic activityi

S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921S-adenosyl-L-methionine
Binding sitei94 – 941S-adenosyl-L-methionine
Binding sitei98 – 981S-adenosyl-L-methionine
Binding sitei129 – 1291S-adenosyl-L-methionine
Binding sitei154 – 1541S-adenosyl-L-methionine

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1930-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein methyltransferase (EC:2.1.1.80)
Gene namesi
Name:cheR
Ordered Locus Names:STM1918
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Chemotaxis protein methyltransferasePRO_0000176039Add
BLAST

Proteomic databases

PaxDbiP07801.
PRIDEiP07801.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1918.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3815Combined sources
Helixi44 – 463Combined sources
Helixi47 – 6115Combined sources
Helixi66 – 7510Combined sources
Helixi81 – 899Combined sources
Turni96 – 1016Combined sources
Helixi102 – 11211Combined sources
Beta strandi117 – 1226Combined sources
Turni125 – 1273Combined sources
Helixi128 – 14114Combined sources
Beta strandi147 – 1559Combined sources
Helixi157 – 1659Combined sources
Beta strandi167 – 1693Combined sources
Helixi170 – 1734Combined sources
Helixi178 – 1847Combined sources
Beta strandi185 – 1873Combined sources
Helixi190 – 1923Combined sources
Beta strandi194 – 1985Combined sources
Helixi200 – 2034Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi224 – 2296Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 24811Combined sources
Helixi249 – 2513Combined sources
Beta strandi252 – 2609Combined sources
Turni267 – 2693Combined sources
Beta strandi273 – 2775Combined sources
Beta strandi280 – 2834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF7X-ray2.00A11-284[»]
1BC5X-ray2.20A16-284[»]
ProteinModelPortaliP07801.
SMRiP07801. Positions 11-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 286272CheR-type methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 2132S-adenosyl-L-methionine binding
Regioni230 – 2312S-adenosyl-L-methionine binding

Sequence similaritiesi

Contains 1 cheR-type methyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
HOGENOMiHOG000254353.
KOiK00575.
OMAiFVGHAEN.
OrthoDBiEOG6ZD69Q.
PhylomeDBiP07801.

Family and domain databases

Gene3Di1.10.155.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR026024. Chemotaxis_MeTrfase_CheR.
IPR022642. CheR_C.
IPR000780. CheR_MeTrfase.
IPR022641. CheR_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01739. CheR. 1 hit.
PF03705. CheR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000410. CheR. 1 hit.
PRINTSiPR00996. CHERMTFRASE.
SMARTiSM00138. MeTrc. 1 hit.
[Graphical view]
SUPFAMiSSF47757. SSF47757. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS50123. CHER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSLPSGQT SVLLQMTQRL ALSDAHFRRI CQLIYQRAGI VLADHKRDMV
60 70 80 90 100
YNRLVRRLRA LGLDDFGRYL SMLEANQNSA EWQAFINALT TNLTAFFREA
110 120 130 140 150
HHFPILAEHA RRRHGEYRVW SAAASTGEEP YSIAITLADA LGMAPGRWKV
160 170 180 190 200
FASDIDTEVL EKARSGIYRL SELKTLSPQQ LQRYFMRGTG PHEGLVRVRQ
210 220 230 240 250
ELANYVEFSS VNLLEKQYNV PGPFDAIFCR NVMIYFDKTT QEDILRRFVP
260 270 280
LLKPDGLLFA GHSENFSNLV REFSLRGQTV YALSKDKA
Length:288
Mass (Da):32,924
Last modified:August 1, 1988 - v1
Checksum:i4D344E6F326DD482
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02757 Genomic DNA. Translation: AAA27035.1.
AE006468 Genomic DNA. Translation: AAL20834.1.
PIRiA29303. XYEBGM.
RefSeqiNP_460875.1. NC_003197.1.
WP_000204362.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20834; AAL20834; STM1918.
GeneIDi1253439.
KEGGistm:STM1918.
PATRICi32382391. VBISalEnt20916_2034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02757 Genomic DNA. Translation: AAA27035.1.
AE006468 Genomic DNA. Translation: AAL20834.1.
PIRiA29303. XYEBGM.
RefSeqiNP_460875.1. NC_003197.1.
WP_000204362.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF7X-ray2.00A11-284[»]
1BC5X-ray2.20A16-284[»]
ProteinModelPortaliP07801.
SMRiP07801. Positions 11-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1918.

Proteomic databases

PaxDbiP07801.
PRIDEiP07801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20834; AAL20834; STM1918.
GeneIDi1253439.
KEGGistm:STM1918.
PATRICi32382391. VBISalEnt20916_2034.

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
HOGENOMiHOG000254353.
KOiK00575.
OMAiFVGHAEN.
OrthoDBiEOG6ZD69Q.
PhylomeDBiP07801.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1930-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07801.

Family and domain databases

Gene3Di1.10.155.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR026024. Chemotaxis_MeTrfase_CheR.
IPR022642. CheR_C.
IPR000780. CheR_MeTrfase.
IPR022641. CheR_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01739. CheR. 1 hit.
PF03705. CheR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000410. CheR. 1 hit.
PRINTSiPR00996. CHERMTFRASE.
SMARTiSM00138. MeTrc. 1 hit.
[Graphical view]
SUPFAMiSSF47757. SSF47757. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS50123. CHER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria."
    Simms S.A., Stock A.M., Stock J.B.
    J. Biol. Chem. 262:8537-8543(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine."
    Djordjevic S., Stock A.M.
    Structure 5:545-558(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-284 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
  4. "Chemotaxis receptor recognition by protein methyltransferase CheR."
    Djordjevic S., Stock A.M.
    Nat. Struct. Biol. 5:446-450(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-284 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND TAR.

Entry informationi

Entry nameiCHER_SALTY
AccessioniPrimary (citable) accession number: P07801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: December 9, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.