HTR1_HALS3
ID HTR1_HALS3 Reviewed; 536 AA.
AC B0R632; P33741; P33955; Q9HPF6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Sensory rhodopsin I transducer;
DE AltName: Full=HTR-I;
DE AltName: Full=Methyl-accepting phototaxis protein I;
DE Short=MPP-I;
GN Name=htr1; Synonyms=htr, htrI; OrderedLocusNames=OE_3347F;
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 [GENOMIC DNA].
RC STRAIN=R1 / S9 / L33;
RX PubMed=8344242; DOI=10.1002/j.1460-2075.1993.tb05968.x;
RA Ferrando-May E., Krah M., Marwan W., Oesterhelt D.;
RT "The methyl-accepting transducer protein HtrI is functionally associated
RT with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium
RT salinarium.";
RL EMBO J. 12:2999-3005(1993).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=8187768; DOI=10.1002/j.1460-2075.1994.tb06491.x;
RA Krah M., Marwan W., Vermeglio A., Oesterhelt D.;
RT "Phototaxis of Halobacterium salinarium requires a signalling complex of
RT sensory rhodopsin I and its methyl-accepting transducer HtrI.";
RL EMBO J. 13:2150-2155(1994).
RN [4]
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 I (SR-I) to the flagellar motor. Responds to light changes
CC through the variation of the level of methylation.
CC {ECO:0000269|PubMed:8187768}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; X68591; CAA48578.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP14201.1; -; Genomic_DNA.
DR PIR; A47190; A47190.
DR RefSeq; WP_010903210.1; NC_010364.1.
DR AlphaFoldDB; B0R632; -.
DR SMR; B0R632; -.
DR EnsemblBacteria; CAP14201; CAP14201; OE_3347F.
DR GeneID; 5953066; -.
DR KEGG; hsl:OE_3347F; -.
DR HOGENOM; CLU_000445_107_18_2; -.
DR OMA; NKLEMIS; -.
DR PhylomeDB; B0R632; -.
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: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 InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
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 PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Chromophore; Membrane; Methylation; Photoreceptor protein;
KW Receptor; Repeat; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..536
FT /note="Sensory rhodopsin I transducer"
FT /id="PRO_0000429075"
FT TOPO_DOM 2..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..107
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 149..202
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 221..459
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 116..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT MOD_RES 473
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="D -> E (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="A -> G (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..60
FT /note="AS -> GR (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> G (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="A -> S (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..126
FT /note="AEAETA -> TESETT (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> S (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> S (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..158
FT /note="TAKRY -> SSNRD (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="AA -> SS (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> F (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="H -> P (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> F (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="A -> P (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> P (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="Q -> H (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="Q -> H (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..419
FT /note="RD -> LH (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> S (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="A -> P (in Ref. 1; CAA48578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 56675 MW; 24B6413266A9D085 CRC64;
MTIAWARRRY GVKLGLGYIA TAGLLVGVGV TTNDVPSTIV AGIAGLLTLG SINAAETVAS
IKEIAAQTER VANGNLEQEV TSTRTDEFGS LADSIEQMRQ SLRGRLNEME RTRADLEETQ
AEAETAREEA EQAKQEAQAA EREARELAAT YQDTAKRYGE TMEAAATGDL TQRVDVDTDH
EAMETVGTAF NQMMDDLQAT VRTVTTVADE IEAKTERMSE TSADIEASAG DTVEAVSKIE
SQANDQRTEL DSAADDVQQV SASAEEIAAT IDDLASRSED VATASDAARD SSKSALDEMS
SIETEVDDAV GQVEQLRDQV AEITDIVDVI TDIGEQTNML ALNASIEAAR AGGNADGDGF
SVVADEVKDL AEETQDRANE IAAVVEKVTA QTEDVTASIQ QTRTRVESGS ETVESTLRDI
RTIADSIAEV SNSIDEIQRT TSEQAETVQS TATSVERVAG LSDDTTALAS DAESAVIGQR
ESAEEIAASL EQFQNTAVEQ LQSRVASFTV ATEDSETAGG SVEQPVMRAG ADGGGA
