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 08-NOV-2023, entry version 71.
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 PaxDb; 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 6.10.340.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR Pfam; PF00672; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 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
//
