ID   HTR2_HALS3              Reviewed;         764 AA.
AC   B0R6B1;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Sensory rhodopsin II transducer;
DE   AltName: Full=HTR-II;
DE   AltName: Full=Methyl-accepting phototaxis protein II;
DE            Short=MPP-II;
GN   Name=htr2; Synonyms=htrII; OrderedLocusNames=OE_3481R;
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   METHYLATION.
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).
CC   -!- FUNCTION: Transduces signals from the phototaxis receptor sensory
CC       rhodopsin II (SR-II) to the flagellar motor. Responds to light changes
CC       through the variation of the level of methylation. Also acts as a
CC       chemotransducer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Methylated by CheR. {ECO:0000269|PubMed:18514223}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AM774415; CAP14280.1; -; Genomic_DNA.
DR   RefSeq; WP_010903287.1; NC_010364.1.
DR   AlphaFoldDB; B0R6B1; -.
DR   SMR; B0R6B1; -.
DR   EnsemblBacteria; CAP14280; CAP14280; OE_3481R.
DR   GeneID; 5954313; -.
DR   KEGG; hsl:OE_3481R; -.
DR   HOGENOM; CLU_000445_107_19_2; -.
DR   OMA; VEQTNML; -.
DR   PhylomeDB; B0R6B1; -.
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:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   Pfam; PF00672; HAMP; 2.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 2.
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; Chromophore; Membrane; Methylation;
KW   Photoreceptor protein; Receptor; Repeat; Sensory transduction; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..764
FT                   /note="Sensory rhodopsin II transducer"
FT                   /id="PRO_0000429078"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..764
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          303..355
FT                   /note="HAMP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          397..450
FT                   /note="HAMP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          469..705
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   REGION          347..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  79042 MW;  D5EB26F706576996 CRC64;
     MGSGLVARIR GSYGTKLTLA LVVVVVLSVG VGTFVYQQTT TQLETDVRAD LTGSADARAD
     HLDAWLSNAR GQTQLASRHP VLASGNDTAI TRYLEGLAAS DERPDGVVAA HVYNTSTTTI
     EASSADAFTG VNPREQGAPF ATDPPSFATT SDVVVAAPFT VPAADFPVLS VLSPIPGTTD
     KALIYMVNVN TLTDDFGQNV AGSTTTVVSA DGTYVSHPDQ DRVLTGHDGP SRLLNQSRTQ
     PAYIDANGTV TAAAPVDGAP WSVLVRAPHD RAFALGDFVA SSLVGLVLIT IVSLSLIGVT
     VGSTTVTALR QFSRRADEMA AGDLDTDIDT SRNDEFGTLA ESFRSMRDSL SESLTDAERA
     TARAEDARED AEQQRADAEA AREDAEAARK DAQETARALE SAAADYEEAL TAVADGDLTR
     RVDASRDHDA MARIGHALND MLDDIETSVA AATAFSDHVS DAAQRVEADA GDAIDAGTDV
     STAVDEISDG ATEQTDRLHE VAGEVDDLSA SAEEVAETVA SLADTAGQAA SAVDDGRQAT
     EDAVETMDDV ADDAEAAADA MDALDSEMAD IGEIVDVIAD IADQTNMLAL NASIEAARTG
     ADGDGFAVVA DEVKTLAEES RDAAEDIESR LLALQGQVSD VADEMRATSD TVSDGRATVG
     DAATALDDVV SFVADTDTAA GEIRAATDRQ AHAASRVASA VDEVAGISQE TAAQATAVAD
     SAATQTDTLS SVDDAAADLA DRAAALDDLL AEFDAHDDTE PEDY