ID MCP2_THEMA Reviewed; 530 AA.
AC Q9X0M7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Methyl-accepting chemotaxis protein 2;
GN Name=mcp2; OrderedLocusNames=TM_1143;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC 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 GLN-274; GLU-281 AND GLU-505, AND DEAMIDATION AT GLN-274 AND
RP GLN-498.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-529.
RX PubMed=16622408; DOI=10.1038/nsmb1085;
RA Park S.-Y., Borbat P.P., Gonzalez-Bonet G., Bhatnagar J., Pollard A.M.,
RA Freed J.H., Bilwes A.M., Crane B.R.;
RT "Reconstruction of the chemotaxis receptor-kinase assembly.";
RL Nat. Struct. Mol. Biol. 13:400-407(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; AAD36219.1; -; Genomic_DNA.
DR PIR; C72291; C72291.
DR RefSeq; NP_228949.1; NC_000853.1.
DR RefSeq; WP_004080253.1; NZ_CP011107.1.
DR PDB; 2CH7; X-ray; 2.50 A; A/B=225-529.
DR PDB; 3JA6; EM; 12.70 A; G/I/K/M/O/Q=225-529, H/J/L/N/P/R=225-528.
DR PDBsum; 2CH7; -.
DR PDBsum; 3JA6; -.
DR AlphaFoldDB; Q9X0M7; -.
DR SMR; Q9X0M7; -.
DR DIP; DIP-29072N; -.
DR STRING; 243274.TM_1143; -.
DR PaxDb; 243274-THEMA_08630; -.
DR EnsemblBacteria; AAD36219; AAD36219; TM_1143.
DR KEGG; tma:TM1143; -.
DR eggNOG; COG0840; Bacteria.
DR InParanoid; Q9X0M7; -.
DR OrthoDB; 107771at2; -.
DR EvolutionaryTrace; Q9X0M7; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..530
FT /note="Methyl-accepting chemotaxis protein 2"
FT /id="PRO_0000250994"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 152..222
FT /note="HAMP"
FT DOMAIN 244..480
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 274
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:16707700"
FT MOD_RES 281
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:16707700"
FT MOD_RES 498
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000269|PubMed:16707700"
FT MOD_RES 505
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:16707700"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 225..341
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 344..372
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 378..414
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 417..432
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 435..518
FT /evidence="ECO:0007829|PDB:2CH7"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:2CH7"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:2CH7"
SQ SEQUENCE 530 AA; 57929 MW; C04149A4F46890CE CRC64;
MSLKGKTLLV STITLAAVVL VALLGGSVFL KAGQNVRKAF EEYELAVEAL DKLGELETKV
ALFVNNAAKI EEVSSLFNEL KKVADKIPSL KEHMDALERN ISEIISGKTE VVSRIQSSVD
QVKEDIMANL DRTRENLDKE ISYSSELIRN VLFIVLPIVA VASGVFLFVM ISRSLRLLKP
VMEASRSLRN NDLTINIQEA KGKDEISTLL NEFKASIEYL RNNLKDVQTE TFSVAESIEE
ISKANEEITN QLLGISKEMD NISTRIESIS ASVQETTAGS EEISSATKNI ADSAQQAASF
ADQSTQLAKE AGDALKKVIE VTRMISNSAK DVERVVESFQ KGAEEITSFV ETINAIAEQT
NLLALNAAIE AARAGEAGRG FAVVADEIRK LAEESQQASE NVRRVVNEIR SIAEDAGKVS
SEITARVEEG TKLADEADEK LNSIVGAVER INEMLQNIAA AIEEQTAAVD EITTAMTENA
KNAEEITNSV KEVNARLQEI SASTEEVTSR VQTIRENVQM LKEIVARYKI
//
