HTR1_HALSA
ID HTR1_HALSA Reviewed; 536 AA.
AC P0DMI3; P33741; P33955; Q9HPF6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=VNG_1659G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11; 351-378 AND
RP 458-477, AND FUNCTION.
RC STRAIN=Flx5R;
RX PubMed=1465418; DOI=10.1073/pnas.89.24.11915;
RA Yao V.J., Spudich J.L.;
RT "Primary structure of an archaebacterial transducer, a methyl-accepting
RT protein associated with sensory rhodopsin I.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11915-11919(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:1465418}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Methylated by CheR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {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; L05603; AAA72315.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19913.1; -; Genomic_DNA.
DR PIR; A47190; A47190.
DR PIR; E84318; E84318.
DR RefSeq; WP_010903210.1; NC_002607.1.
DR AlphaFoldDB; P0DMI3; -.
DR SMR; P0DMI3; -.
DR STRING; 64091.VNG_1659G; -.
DR PaxDb; P0DMI3; -.
DR EnsemblBacteria; AAG19913; AAG19913; VNG_1659G.
DR GeneID; 5953066; -.
DR KEGG; hal:VNG_1659G; -.
DR PATRIC; fig|64091.14.peg.1264; -.
DR HOGENOM; CLU_000445_107_18_2; -.
DR OMA; NKLEMIS; -.
DR OrthoDB; 28514at2157; -.
DR PhylomeDB; P0DMI3; -.
DR Proteomes; UP000000554; 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; Direct protein sequencing; Membrane;
KW Methylation; Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1465418"
FT CHAIN 2..536
FT /note="Sensory rhodopsin I transducer"
FT /id="PRO_0000110548"
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"
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
