Reviewed, UniProtKB/Swiss-Prot P07801 (CHER_SALTY)

Names and origin

Protein names

Recommended name:
    Chemotaxis protein methyltransferase
    EC=2.1.1.80

Gene names

Name:	cheR
Ordered Locus Names:	STM1918

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Chemotaxis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein-glutamate O-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 288

288

Chemotaxis protein methyltransferase

PRO_0000176039

Regions

Domain

15 – 286

272

CheR-type methyltransferase

Region

212 – 213

2

S-adenosyl-L-methionine binding

Region

230 – 231

2

S-adenosyl-L-methionine binding

Sites

Binding site

92

1

S-adenosyl-L-methionine

Binding site

94

1

S-adenosyl-L-methionine

Binding site

98

1

S-adenosyl-L-methionine

Binding site

129

1

S-adenosyl-L-methionine

Binding site

154

1

S-adenosyl-L-methionine

Secondary structure

1

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288

Helix Strand Turn

Details...

Helix

24 – 38

15

Helix

44 – 46

3

Helix

47 – 61

15

Helix

66 – 75

10

Helix

81 – 89

9

Turn

96 – 101

6

Helix

102 – 112

11

Beta strand

117 – 122

6

Turn

125 – 127

3

Helix

128 – 141

14

Beta strand

147 – 155

9

Helix

157 – 165

9

Beta strand

167 – 169

3

Helix

170 – 173

4

Helix

178 – 184

7

Beta strand

185 – 187

3

Beta strand

194 – 198

5

Helix

200 – 203

4

Beta strand

206 – 210

5

Beta strand

224 – 229

6

Helix

233 – 235

3

Helix

238 – 248

11

Helix

249 – 251

3

Beta strand

252 – 260

9

Turn

267 – 269

3

Beta strand

273 – 277

5

Beta strand

280 – 283

4

Sequences

	Sequence		Length	Mass (Da)
	P07801-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 4D344E6F326DD482	FASTA	288	32,924
	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

References

	« Hide 'large scale' referencesShow '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: 3298235] [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. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [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: 9115443] [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: 9628482] [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

EMBLGenBankDDBJ

J02757 Genomic DNA. Translation: AAA27035.1.
AE008785 Genomic DNA. Translation: AAL20834.1.

PIR

XYEBGM. A29303.

RefSeq

NP_460875.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AF7	X-ray	2.00	A	11-284	[»]
1BC5	X-ray	2.20	A	16-284	[»]

ModBase

Search...

Genome annotation databases

GeneID

1253439.

GenomeReviews

Gene locus STM1918 in contig AE006468_GR.

KEGG

stm:STM1918.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P07801.

OMA

P07801. IAGHSEN.

Enzyme and pathway databases

BioCyc

STYP99287:STM1918-MON.

BRENDA

2.1.1.80. 2.

Family and domain databases

InterPro

IPR000780. CheR_MeTrfase.
[Graphical view]

Pfam

PF01739. CheR. 1 hit.
PF03705. CheR_N. 1 hit.
[Graphical view]

PRINTS

PR00996. CHERMTFRASE.

SMART

SM00138. MeTrc. 1 hit.
[Graphical view]

PROSITE

PS50123. CHER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHER_SALTY

Accession

Primary (citable) accession number: P07801

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)