ID   HTRM_HALMA              Reviewed;         184 AA.
AC   Q5V4H8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Probable sensory rhodopsin transducer;
DE            Short=HmHtrM;
GN   Name=htrM; OrderedLocusNames=rrnAC0558;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
RN   [2]
RP   FUNCTION, INDUCTION, AND INTERACTION WITH XOP2/SRM.
RX   PubMed=20802037; DOI=10.1128/jb.00642-10;
RA   Fu H.Y., Lin Y.C., Chang Y.N., Tseng H., Huang C.C., Liu K.C., Huang C.S.,
RA   Su C.W., Weng R.R., Lee Y.Y., Ng W.V., Yang C.S.;
RT   "A novel six-rhodopsin system in a single archaeon.";
RL   J. Bacteriol. 192:5866-5873(2010).
CC   -!- FUNCTION: The HtrM-Xop2/SRM complex may interact with CheB or CheR and
CC       modulate their availability to Sop1 or Sop2.
CC       {ECO:0000269|PubMed:20802037}.
CC   -!- SUBUNIT: Interacts with Xop2/SRM. {ECO:0000269|PubMed:20802037}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed constitutively throughout the growth phases, both
CC       in presence and absence of white light. {ECO:0000269|PubMed:20802037}.
CC   -!- MISCELLANEOUS: Is lacking a methyl-accepting transducer domain found in
CC       all other photosensory transducers. {ECO:0000305|PubMed:20802037}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY596297; AAV45574.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5V4H8; -.
DR   SMR; Q5V4H8; -.
DR   STRING; 272569.rrnAC0558; -.
DR   EnsemblBacteria; AAV45574; AAV45574; rrnAC0558.
DR   KEGG; hma:rrnAC0558; -.
DR   PATRIC; fig|272569.17.peg.1322; -.
DR   eggNOG; arCOG02320; Archaea.
DR   HOGENOM; CLU_1465058_0_0_2; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003660; HAMP_dom.
DR   Pfam; PF00672; HAMP; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..184
FT                   /note="Probable sensory rhodopsin transducer"
FT                   /id="PRO_0000428856"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          73..125
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
SQ   SEQUENCE   184 AA;  19903 MW;  9F346987D39E59AA CRC64;
     MSAVTKRSGS YGRTLGVGAV LVLVLATLAV VNVYTNLAPE MSGSQQSMLL SGLVSILLIV
     AVALLFVATI IGRERTAAVE TLAAQARQIE QGELDVDLAT NRTDDVGDIY RALAVLRDSE
     QLDRQHGVSA EVVAQYCETA VEISNGNDDS RLEENVDDPQ LAELAMRFNE ILDQRKRDAE
     IDSR