MPCT_HALS3
ID MPCT_HALS3 Reviewed; 627 AA.
AC B0R367;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Transducer protein MpcT;
DE AltName: Full=Membrane potential change transducer protein;
GN Name=mpcT; Synonyms=htr14; OrderedLocusNames=OE_1536R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, METHYLATION, DISRUPTION PHENOTYPE, AND GENE
RP NAME.
RC STRAIN=R1 / S9 / L33;
RX PubMed=15752193; DOI=10.1111/j.1365-2958.2005.04516.x;
RA Koch M.K., Oesterhelt D.;
RT "MpcT is the transducer for membrane potential changes in Halobacterium
RT salinarum.";
RL Mol. Microbiol. 55:1681-1694(2005).
RN [3]
RP METHYLATION AT GLU-310; GLU-416 AND GLU-507.
RC STRAIN=R1 / S9;
RX PubMed=18514223; DOI=10.1016/j.jmb.2008.04.063;
RA Koch M.K., Staudinger W.F., Siedler F., Oesterhelt D.;
RT "Physiological sites of deamidation and methyl esterification in sensory
RT transducers of Halobacterium salinarum.";
RL J. Mol. Biol. 380:285-302(2008).
RN [4]
RP INTERACTION WITH CHEA; CHEY AND CHEW1.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=23171228; DOI=10.1186/1471-2180-12-272;
RA Schlesner M., Miller A., Besir H., Aivaliotis M., Streif J., Scheffer B.,
RA Siedler F., Oesterhelt D.;
RT "The protein interaction network of a taxis signal transduction system in a
RT halophilic archaeon.";
RL BMC Microbiol. 12:272-272(2012).
CC -!- FUNCTION: Mediates bacteriorhodopsin- and halorhodopsin-dependent
CC photoresponses by detecting membrane potential changes. Probably
CC transduces the signal to the histidine kinase CheA.
CC {ECO:0000269|PubMed:15752193}.
CC -!- SUBUNIT: Interacts with CheA, CheY and CheW1.
CC {ECO:0000269|PubMed:23171228}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15752193};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15752193}.
CC -!- PTM: Methylated by CheR. {ECO:0000269|PubMed:15752193,
CC ECO:0000269|PubMed:18514223}.
CC -!- DISRUPTION PHENOTYPE: Deletion abolishes bacteriorhodopsin- and
CC halorhodopsin-dependent phototaxis. {ECO:0000269|PubMed:15752193}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AM774415; CAP13179.1; -; Genomic_DNA.
DR RefSeq; WP_010902217.1; NC_010364.1.
DR AlphaFoldDB; B0R367; -.
DR SMR; B0R367; -.
DR EnsemblBacteria; CAP13179; CAP13179; OE_1536R.
DR GeneID; 5952494; -.
DR KEGG; hsl:OE_1536R; -.
DR HOGENOM; CLU_000445_107_18_2; -.
DR OMA; ANIQITH; -.
DR PhylomeDB; B0R367; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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; 3.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Membrane; Methylation; Repeat; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..627
FT /note="Transducer protein MpcT"
FT /id="PRO_0000428992"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 78..132
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 192..247
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 266..502
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 505..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
FT MOD_RES 416
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
FT MOD_RES 507
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
SQ SEQUENCE 627 AA; 65656 MW; E5F2867FA6CA2A75 CRC64;
MNITQAYKRS LWWSMDMVGA TGSVERKMLT AVGLQFLAAG GMAFLTVFTA GTVQLIGVGG
MLALSVVAFY NTYLIAEADF VEPLVALEDA ADDIAAGEFE RADIPSSKRD DEIASLVASF
DGMQSNLEVA SRQADALARQ AFDDPALDES VPGAFGESIT EMADSLEAYT AELEDKTAEL
EHQQAELERQ SEQLRALVDA LSEATDAARA GDLTATVDAA ALDVTDDHRA AVEDFNQLLE
TLADTISDIQ SFSDAVLAVS RTTDERVDAV ADRSAAVSES VTEIADGANQ QTNQLNNIAA
EMDTVSATVE EIAASANDVA KTAQAAADRG EDGRGEVEET IEALRALREQ SQAVAETVES
LAAEVERIDG ITALIEDIAE ETNMLALNAS IEAARTGSDG DGFAVVADEV KDLAEETREQ
AADISEIVDA VTEKAEDASI AIGEVDAEVE RKITKAEGVL RDFEAIVDEV ANVNHAVQEI
SDATDQGAQS VTDVVGMVEE VASVSEETAA ESDTVADNAA EQTDATDEVA DQMDELAEQT
AALAGMLDDF TVPADAGTAD QSVADDSPTA QPPAADDEPA AAVVDQPQPA SDAEDEEGVP
DSGGESVAVS DGGWADDRSS FTWADSQ
