ID   MCP3_THEMA              Reviewed;         539 AA.
AC   Q9X0N0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Methyl-accepting chemotaxis protein 3;
GN   Name=mcp3; OrderedLocusNames=TM_1146;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   METHYLATION AT GLU-255; GLU-284; GLU-479 AND GLU-515.
RX   PubMed=16707700; DOI=10.1128/jb.00181-06;
RA   Perez E., Zheng H., Stock A.M.;
RT   "Identification of methylation sites in Thermotoga maritima chemotaxis
RT   receptors.";
RL   J. Bacteriol. 188:4093-4100(2006).
CC   -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC       concentration of attractants and repellents in the environment,
CC       transduce a signal from the outside to the inside of the cell, and
CC       facilitate sensory adaptation through the variation of the level of
CC       methylation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD36222.1; -; Genomic_DNA.
DR   PIR; F72288; F72288.
DR   RefSeq; NP_228952.1; NC_000853.1.
DR   RefSeq; WP_004080235.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X0N0; -.
DR   SMR; Q9X0N0; -.
DR   STRING; 243274.THEMA_08610; -.
DR   EnsemblBacteria; AAD36222; AAD36222; TM_1146.
DR   KEGG; tma:TM1146; -.
DR   eggNOG; COG0840; Bacteria.
DR   InParanoid; Q9X0N0; -.
DR   OMA; MTTIHEA; -.
DR   OrthoDB; 477199at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chemotaxis; Membrane; Methylation; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..539
FT                   /note="Methyl-accepting chemotaxis protein 3"
FT                   /id="PRO_0000250995"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          181..234
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          253..489
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   MOD_RES         255
FT                   /note="Glutamate methyl ester (Glu)"
FT                   /evidence="ECO:0000269|PubMed:16707700"
FT   MOD_RES         284
FT                   /note="Glutamate methyl ester (Glu)"
FT                   /evidence="ECO:0000269|PubMed:16707700"
FT   MOD_RES         479
FT                   /note="Glutamate methyl ester (Glu)"
FT                   /evidence="ECO:0000269|PubMed:16707700"
FT   MOD_RES         515
FT                   /note="Glutamate methyl ester (Glu)"
FT                   /evidence="ECO:0000269|PubMed:16707700"
SQ   SEQUENCE   539 AA;  58621 MW;  5330E1E48B1295BA CRC64;
     MKSVASKLLL GFGLVCAGLV LFGLLTFYNI LSLEKIVADT ANINRAIVEL AINQAGVLVA
     VQNKDKSLLS SSVEGLRTSL DDIKAYQSDF SGENLKLLQE SIAHLEEMIR ITDSLIVDGV
     DQSIYDRFVE LQAEIRNPLR KLVQNLGVEN VSMTKNIKRN IIFFLVVVCA AAMFIAIFTT
     RNLTTPLKKL AVLVENLSHG VLNVEIEKIR SKDEIGKAAM AVEKLREILL DIITGINKAS
     SEVSSSSEEL SATSEELSAN VNSISEALVS LNKEADENSA TLEEFTASIE ELSSTADSNS
     KSAQAMLEST QRVHEQVEKS TERIREITEK AHSTREMSEN TKQALNRLLS MAENINSIVD
     TINSIAEQTN LLALNAAIEA ARAGEAGRGF AVVADEIRKL AEESKAATQQ IGEILGKLRD
     EINNSSKIVE STASAIEETA SLVESIKDVF ESIRIAMEDV QSRVESVAAS TQEQSASLEE
     LSAGVTRLTE LLNKTRENTS SANSALQEAN AALEELSASA QSLAELAQEL QRRIEFFKI