[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3510184 [NCBI, ExPASy, EBI, Israel, Japan] Mutoh N., Simon M.I.; "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli."; J. Bacteriol. 165:161-166(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan] Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.; "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."; DNA Res. 3:379-392(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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.
SIMILARITY: Contains 1 cheR-type methyltransferase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13463; AAA23568.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74954.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15700.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64951; XYECCR.

RefSeq

AP_002504.1; -.
NP_416398.1; -.

3D structure databases

HSSP

P07801; 1AF7. [HSSP ENTRY / PDB]

SMR

P07364; 11-284.

ModBase

P07364.

Protein-protein interaction databases

DIP

DIP:9273N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:CHER-MON; -.

Organism-specific databases

EchoBASE

EB0146; -.

EcoGene

EG10148; cheR.

Ontologies

GO:0008983;	Molecular function: protein-glutamate O-methyltransferase activity (inferred from electronic annotation from EC).
GO:0006935;	Biological process: chemotaxis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000780; CheR_MeTrfase.
Graphical view of domain structure.

Pfam

PF01739; CheR; 1.
PF03705; CheR_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00996; CHERMTFRASE.

SMART

SM00138; MeTrc; 1.
SMART graphical view of domain structure.

PROSITE

PS50123; CHER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

946396; -.

GenomeReviews

U00096_GR; b1884.
AP009048_GR; JW1873.

KEGG

ecj:JW1873; -.
eco:b1884; -.

Phylogenomic databases

HOGENOM

P07364; -.

Genome annotation databases

CMR

P07364; b1884.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chemotaxis; Complete proteome; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 286`	`286`	`Chemotaxis protein methyltransferase.`	`PRO_0000176033`
`DOMAIN`	`15 286`	`272`	`CheR-type methyltransferase.`
`REGION`	`212 213`	`2`	`S-adenosyl-L-methionine binding (By similarity).`
`REGION`	`230 231`	`2`	`S-adenosyl-L-methionine binding (By similarity).`
`BINDING`	`92 92`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`94 94`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`98 98`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`129 129`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`154 154`		`S-adenosyl-L-methionine (By similarity).`
`CONFLICT`	`113 113`		`R -> G (in Ref. 1; AAA23568).`

Sequence information

Length: 286 AA [This is the length of the unprocessed precursor]

Molecular weight: 32849 Da [This is the MW of the unprocessed precursor]

CRC64: 2AFA307DD406B135 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSSLPCGQT SLLLQMTERL ALSDAHFRRI SQLIYQRAGI VLADHKRDMV YNRLVRRLRS 

        70         80         90        100        110        120 
LGLTDFGHYL NLLESNQHSG EWQAFINSLT TNLTAFFREA HHFPLLADHA RRRSGEYRVW 

       130        140        150        160        170        180 
SAAASTGEEP YSIAMTLADT LGTAPGRWKV FASDIDTEVL EKARSGIYRH EELKNLTPQQ 

       190        200        210        220        230        240 
LQRYFMRGTG PHEGLVRVRQ ELANYVDFAP LNLLAKQYTV PGPFDAIFCR NVMIYFDQTT 

       250        260        270        280 
QQEILRRFVP LLKPDGLLFA GHSENFSHLE RRFTLRGQTV YALSKD

P07364 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools