[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13048 / DSM 30053 / IFO 13534 / JCM 1235 / NCTC 10006; PubMed=2496104 [NCBI, ExPASy, EBI, Israel, Japan] Dahl M.K., Boos W., Manson M.D.; "Evolution of chemotactic-signal transducers in enteric bacteria."; J. Bacteriol. 171:2361-2371(1989).

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

M26411; AAA24799.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E32302; E32302.

3D structure databases

HSSP

P07801; 1BC5. [HSSP ENTRY / PDB]

SMR

P21824; 14-100.

ModBase

P21824.

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

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

PRINTS

PR00996; CHERMTFRASE.

PROSITE

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

ProtoNet

P21824.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >100`	`>100`	`Chemotaxis protein methyltransferase.`	`PRO_0000176034`
`DOMAIN`	`18 >100`	`>83`	`CheR-type methyltransferase.`
`BINDING`	`95 95`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`97 97`		`S-adenosyl-L-methionine (By similarity).`
`NON_TER`	`100 100`

Sequence information

Length: 100 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 11438 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: C352DD9CDB959F68 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKQDDINAAR ESGSAVAQMA QRLPLSDAHF RRISQLIYQR AGIVLAPHKR EMVYNRLVRR 

        70         80         90        100 
LRLLGIHDFG DYLALLESDP HSAEWQAFIN ALTTNLTAFF

P21824 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