Methyl-accepting chemotaxis protein II

Details

Name
Methyl-accepting chemotaxis protein II
Synonyms
  • Aspartate chemoreceptor protein
  • cheM
  • MCP-II
Gene Name
tar
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0011006|Methyl-accepting chemotaxis protein II
MFNRIRVVTMLMMVLGVFALLQLVSGGLLFSSLQHNQQGFVISNELRQQQSELTSTWDLM
LQTRINLSRSAARMMMDASNQQSSAKTDLLQNAKTTLAQAAAHYANFKNMTPLPAMAEAS
ANVDEKYQRYQAALAELIQFLDNGNMDAYFAQPTQGMQNALGEALGNYARVSENLYRQTF
DQSAHDYRFAQWQLGVLAVVLVLILMVVWFGIRHALLNPLARVITHIREIASGDLTKTLT
VSGRNEIGELAGTVEHMQRSLIDTVTQVREGSDAIYSGTSEIAAGNTDLSSRTEQQASAL
EETAASMEQLTATVKQNADNARQASQLAQSASETARHGGKVVDGVVNTMHEIADSSKKIA
DIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE
DSVSRVDTGSVLVESAGETMTDIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDR
VTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLASRPLAVNKPEMRLSVNAQSGNTPQ
SLAARDDANWETF
Number of residues
553
Molecular Weight
59613.55
Theoretical pI
4.83
GO Classification
Functions
transmembrane signaling receptor activity
Processes
chemotaxis
Components
integral component of membrane / plasma membrane
General Function
Transmembrane signaling receptor activity
Specific Function
Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
Pfam Domain Function
Transmembrane Regions
7-33 191-211
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0011007|Methyl-accepting chemotaxis protein II (tar)
ATGTTTAACCGTATCCGCGTTGTCACAATGCTGATGATGGTGCTGGGGGTTTTCGCACTG
CTACAGCTTGTTTCCGGTGGTTTGCTGTTTTCTTCATTACAGCATAACCAGCAAGGTTTT
GTTATTTCTAACGAATTACGTCAGCAACAAAGCGAACTCACGTCGACATGGGACTTAATG
CTGCAAACGCGCATTAACCTGAGCCGCTCCGCCGCACGCATGATGATGGACGCTTCTAAC
CAGCAGAGCAGCGCCAAAACGGATTTACTCCAGAATGCAAAAACGACTCTCGCACAGGCG
GCGGCGCACTACGCCAATTTCAAAAATATGACGCCATTGCCAGCGATGGCGGAGGCCAGC
GCGAACGTCGATGAAAAATATCAGCGCTATCAGGCCGCATTAGCCGAACTTATTCAGTTT
CTGGACAATGGCAATATGGATGCCTACTTCGCCCAGCCAACCCAGGGAATGCAAAACGCG
TTGGGCGAGGCGCTGGGCAATTACGCCCGGGTGAGCGAAAACCTGTACCGCCAGACATTT
GATCAAAGTGCTCATGACTACCGTTTTGCGCAATGGCAACTGGGGGTTCTTGCGGTCGTG
CTGGTGCTGATTTTGATGGTGGTTTGGTTCGGCATTCGTCATGCCCTGCTTAACCCATTA
GCGCGAGTGATTACTCATATCCGTGAAATTGCCAGCGGCGATCTGACGAAAACGCTCACC
GTCTCAGGACGTAATGAAATTGGCGAACTGGCGGGAACGGTTGAACATATGCAACGCTCG
CTGATTGACACCGTAACGCAGGTTCGTGAAGGTTCGGATGCGATTTATTCCGGCACCAGT
GAAATTGCCGCCGGTAATACCGACCTCTCTTCCCGTACCGAACAGCAGGCCTCCGCTCTG
GAGGAGACGGCTGCCAGCATGGAACAACTGACGGCCACCGTGAAGCAAAACGCCGATAAC
GCCCGCCAGGCTTCGCAACTGGCGCAAAGCGCCTCCGAGACCGCGCGTCATGGCGGCAAA
GTGGTCGACGGCGTAGTAAACACTATGCACGAAATTGCCGACAGTTCGAAAAAAATCGCT
GACATTATCAGCGTTATCGACGGTATTGCCTTCCAGACTAACATTCTGGCGCTGAACGCG
GCGGTAGAAGCGGCGCGCGCGGGAGAGCAGGGGCGCGGTTTTGCGGTCGTGGCAGGCGAG
GTGCGTAATCTGGCCAGCCGCAGCGCCCAGGCGGCGAAAGAAATAAAAGCGTTGATTGAA
GATTCCGTCTCGCGTGTCGATACCGGTTCTGTGCTGGTGGAAAGCGCCGGGGAAACCATG
ACTGACATCGTCAATGCCGTTACGCGCGTCACGGATATCATGGGCGAAATCGCCTCCGCC
TCGGATGAGCAAAGCCGGGGTATCGATCAGGTCGCTTTGGCCGTTTCCGAAATGGATCGC
GTAACGCAACAGAACGCCTCGCTGGTTCAGGAATCCGCAGCGGCCGCCGCCGCGCTGGAA
GAGCAGGCCAGCCGTCTGACCCAGGCGGTATCGGCTTTCCGCCTGGCATCGCGACCGCTG
GCGGTAAATAAACCTGAGATGCGTTTGTCAGTGAACGCTCAGTCCGGCAATACGCCGCAG
TCATTAGCCGCCAGGGATGATGCGAACTGGGAAACCTTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP02941
UniProtKB Entry NameMCP2_SALTY
GenBank Gene IDJ01809
General References
  1. Russo AF, Koshland DE Jr: Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing. Science. 1983 Jun 3;220(4601):1016-20. [Article]
  2. McClelland M, Sanderson KE, Spieth J, Clifton SW, 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 RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
  3. Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, Jancarik J, Koshland DE Jr, Kim SH: Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science. 1991 Nov 29;254(5036):1342-7. [Article]
  4. Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH: The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem. 1993 May 5;268(13):9787-92. [Article]
  5. Yeh JI, Biemann HP, Prive GG, Pandit J, Koshland DE Jr, Kim SH: High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J Mol Biol. 1996 Sep 20;262(2):186-201. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB023651,10-PhenanthrolineexperimentalunknownDetails