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P07801 (CHER_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chemotaxis protein methyltransferase
EC=2.1.1.80
Gene names
Name:cheR
Ordered Locus Names:STM1918
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Sequence similarities

Contains 1 cheR-type methyltransferase domain.

Ontologies

Keywords
   Biological processChemotaxis
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein-glutamate O-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Chemotaxis protein methyltransferase
PRO_0000176039

Regions

Domain15 – 286272CheR-type methyltransferase
Region212 – 2132S-adenosyl-L-methionine binding
Region230 – 2312S-adenosyl-L-methionine binding

Sites

Binding site921S-adenosyl-L-methionine
Binding site941S-adenosyl-L-methionine
Binding site981S-adenosyl-L-methionine
Binding site1291S-adenosyl-L-methionine
Binding site1541S-adenosyl-L-methionine

Secondary structure

1 .................................................. 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07801 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 4D344E6F326DD482

FASTA28832,924
        10         20         30         40         50         60 
MTSSLPSGQT SVLLQMTQRL ALSDAHFRRI CQLIYQRAGI VLADHKRDMV YNRLVRRLRA 

        70         80         90        100        110        120 
LGLDDFGRYL SMLEANQNSA EWQAFINALT TNLTAFFREA HHFPILAEHA RRRHGEYRVW 

       130        140        150        160        170        180 
SAAASTGEEP YSIAITLADA LGMAPGRWKV FASDIDTEVL EKARSGIYRL SELKTLSPQQ 

       190        200        210        220        230        240 
LQRYFMRGTG PHEGLVRVRQ ELANYVEFSS VNLLEKQYNV PGPFDAIFCR NVMIYFDKTT 

       250        260        270        280 
QEDILRRFVP LLKPDGLLFA GHSENFSNLV REFSLRGQTV YALSKDKA

« Hide

References

« Hide 'large scale' references
[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]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02757 Genomic DNA. Translation: AAA27035.1.
AE006468 Genomic DNA. Translation: AAL20834.1.
PIRXYEBGM. A29303.
RefSeqNP_460875.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AF7X-ray2.00A11-284[»]
1BC5X-ray2.20A16-284[»]
ProteinModelPortalP07801.
SMRP07801. Positions 11-284.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM1918.

Proteomic databases

PaxDbP07801.
PRIDEP07801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20834; AAL20834; STM1918.
GeneID1253439.
KEGGstm:STM1918.
PATRIC32382391. VBISalEnt20916_2034.

Phylogenomic databases

eggNOGCOG1352.
HOGENOMHOG000254353.
KOK00575.
OMAGLYIAGH.
ProtClustDBPRK10611.

Family and domain databases

Gene3D1.10.155.10. 1 hit.
InterProIPR026024. Chemotaxis_MeTrfase_CheR.
IPR022642. CheR_C.
IPR000780. CheR_MeTrfase.
IPR022641. CheR_N.
[Graphical view]
PfamPF01739. CheR. 1 hit.
PF03705. CheR_N. 1 hit.
[Graphical view]
PIRSFPIRSF000410. CheR. 1 hit.
PRINTSPR00996. CHERMTFRASE.
SMARTSM00138. MeTrc. 1 hit.
[Graphical view]
SUPFAMSSF47757. CheR_mtfrase. 1 hit.
PROSITEPS50123. CHER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07801.

Entry information

Entry nameCHER_SALTY
AccessionPrimary (citable) accession number: P07801
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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