ID   HTR1_HALMA              Reviewed;         528 AA.
AC   Q5UXM8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   08-NOV-2023, entry version 93.
DE   RecName: Full=Sensory rhodopsin I transducer;
DE   AltName: Full=MCP domain signal transducer 1;
DE            Short=HmHtrI;
GN   Name=htr1; OrderedLocusNames=rrnAC3281;
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   INDUCTION, AND IDENTIFICATION.
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).
RN   [3]
RP   SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH SOP1.
RX   PubMed=23474528; DOI=10.1016/j.jphotobiol.2013.02.002;
RA   Fu H.Y., Lu Y.H., Yi H.P., Yang C.S.;
RT   "A transducer for microbial sensory rhodopsin that adopts GTG as a start
RT   codon is identified in Haloarcula marismortui.";
RL   J. Photochem. Photobiol. B 121:15-22(2013).
CC   -!- FUNCTION: Transduces signals from the phototaxis receptor sensory
CC       rhodopsin I (Sop1). {ECO:0000269|PubMed:23474528}.
CC   -!- SUBUNIT: Interacts with Sop1. {ECO:0000269|PubMed:23474528}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23474528};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:23474528}.
CC   -!- INDUCTION: Expressed constitutively throughout the growth phases, both
CC       in presence and absence of white light. {ECO:0000269|PubMed:20802037}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV47975.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY596297; AAV47975.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049939098.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXM8; -.
DR   SMR; Q5UXM8; -.
DR   STRING; 272569.rrnAC3281; -.
DR   PaxDb; 272569-rrnAC3281; -.
DR   EnsemblBacteria; AAV47975; AAV47975; rrnAC3281.
DR   GeneID; 40154077; -.
DR   KEGG; hma:rrnAC3281; -.
DR   PATRIC; fig|272569.17.peg.3812; -.
DR   eggNOG; arCOG06364; Archaea.
DR   HOGENOM; CLU_000445_107_18_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 2.
DR   Gene3D; 6.10.340.10; -; 2.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 2.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 3.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Methylation; Reference proteome; Repeat;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..528
FT                   /note="Sensory rhodopsin I transducer"
FT                   /id="PRO_0000428857"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          55..107
FT                   /note="HAMP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          142..195
FT                   /note="HAMP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          214..455
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT   MOD_RES         259
FT                   /note="Glutamate methyl ester (Glu)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   528 AA;  55853 MW;  EF53B3B6C053C55E CRC64;
     MTISSVKQSY GAKLGVGYIA TATLLITVGV VTQDVASTVV AGIAGLLTLG SINAAETVAS
     ITELSAQTQR VADGDLDIEI DSTRTDEFGD LADSIEQMRV SLRDRLSEME AARADLEQAQ
     TDANEAQAEA EAAEEEAKEL ATAYQDIATE YGTVMAAAAD GDLTQRVDVA TEYDAMETVG
     QSFNRMMDEL QETIETVTAV SKRITTETDE ITETSRRVQQ EVDAAVETVA DIQTQATDQQ
     TKLESAAVDI QDVSASAEEI AATIDDLADR SSEVEEASSD ARTASETALT EMDQIQADAA
     DAVTQVETLQ QRMAEITDIA DIISEIAEQT NMLALNASIE AARAGGQGSG ADGNGFSVVA
     DEVKSLAEET QSRADEIATV IAEVSEQTEE VTDSIQATET RVETGTETVE SALSEIATIA
     EAVDDISASI EEMRETTSEQ ADTVQATADS IADVTEASAE TATTAEEMST QIRRQRDVVK
     SISDSLDSFR ETAVDDLESR VRLFTINTDT TAASQTRAVG SPSIGGDD
//