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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)DescriptionActionsGraphical viewLength
Binding sitei92S-adenosyl-L-methionine1
Binding sitei94S-adenosyl-L-methionine1
Binding sitei98S-adenosyl-L-methionine1
Binding sitei129S-adenosyl-L-methionine1
Binding sitei154S-adenosyl-L-methionine1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

S-adenosyl-L-methionine

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001760391 – 288Chemotaxis protein methyltransferaseAdd BLAST288

Proteomic databases

PaxDbiP07801.
PRIDEiP07801.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1918.

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 38Combined sources15
Helixi44 – 46Combined sources3
Helixi47 – 61Combined sources15
Helixi66 – 75Combined sources10
Helixi81 – 89Combined sources9
Turni96 – 101Combined sources6
Helixi102 – 112Combined sources11
Beta strandi117 – 122Combined sources6
Turni125 – 127Combined sources3
Helixi128 – 141Combined sources14
Beta strandi147 – 155Combined sources9
Helixi157 – 165Combined sources9
Beta strandi167 – 169Combined sources3
Helixi170 – 173Combined sources4
Helixi178 – 184Combined sources7
Beta strandi185 – 187Combined sources3
Helixi190 – 192Combined sources3
Beta strandi194 – 198Combined sources5
Helixi200 – 203Combined sources4
Beta strandi206 – 210Combined sources5
Beta strandi224 – 229Combined sources6
Helixi233 – 235Combined sources3
Helixi238 – 248Combined sources11
Helixi249 – 251Combined sources3
Beta strandi252 – 260Combined sources9
Turni267 – 269Combined sources3
Beta strandi273 – 277Combined sources5
Beta strandi280 – 283Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 286CheR-type methyltransferasePROSITE-ProRule annotationAdd BLAST272

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 213S-adenosyl-L-methionine binding2
Regioni230 – 231S-adenosyl-L-methionine binding2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105BZU. Bacteria.
ENOG410XNMH. LUCA.
HOGENOMiHOG000254353.
KOiK00575.
OMAiFVGHAEN.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AF7X-ray2.00A11-284[»]
1BC5X-ray2.20A16-284[»]
ProteinModelPortaliP07801.
SMRiP07801.
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.
PhylomeDBiP07801.

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...

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: November 2, 2016
This is version 120 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.