HTR2_NATPH
ID HTR2_NATPH Reviewed; 534 AA.
AC P42259;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sensory rhodopsin II transducer;
DE AltName: Full=HTR-II;
DE AltName: Full=Methyl-accepting phototaxis protein II;
DE Short=MPP-II;
GN Name=htr2; Synonyms=htrII;
OS Natronomonas pharaonis (Natronobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=2257;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SP-1 / 28;
RX PubMed=7708770; DOI=10.1073/pnas.92.7.3036;
RA Seidel R., Scharf B., Gautel M., Kleine K., Oesterhelt D., Engelhard M.;
RT "The primary structure of sensory rhodopsin II: a member of an additional
RT retinal protein subgroup is coexpressed with its transducer, the
RT halobacterial transducer of rhodopsin II.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3036-3040(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-82.
RX PubMed=12368857; DOI=10.1038/nature01109;
RA Gordeliy V.I., Labahn J., Moukhametzianov R., Efremov R., Granzin J.,
RA Schlesinger R., Bueldt G., Savopol T., Scheidig A.J., Klare J.P.,
RA Engelhard M.;
RT "Molecular basis of transmembrane signalling by sensory rhodopsin II-
RT transducer complex.";
RL Nature 419:484-487(2002).
CC -!- FUNCTION: Transduces signals from the phototaxis receptor sensory
CC rhodopsin II (SR-II) to the flagellar motor. Responds to light changes
CC through the variation of the level of methylation. Also acts as a
CC chemotransducer.
CC -!- INTERACTION:
CC P42259; P42259: htr2; NbExp=3; IntAct=EBI-1034515, EBI-1034515;
CC P42259; P42196: sop2; NbExp=5; IntAct=EBI-1034515, EBI-1034509;
CC P42259; A0A1U7EZ03: sopII; Xeno; NbExp=2; IntAct=EBI-1034515, EBI-7339190;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; Z35086; CAA84468.1; -; Genomic_DNA.
DR PIR; S55299; S55299.
DR PDB; 1H2S; X-ray; 1.93 A; B=23-82.
DR PDB; 2F93; X-ray; 2.00 A; B=3-114.
DR PDB; 2F95; X-ray; 2.20 A; B=5-157.
DR PDB; 2RM8; NMR; -; A=100-159.
DR PDB; 4GYC; X-ray; 2.05 A; B=1-135.
DR PDB; 5JJE; X-ray; 1.90 A; B=5-157.
DR PDB; 5JJF; X-ray; 1.90 A; B=5-157.
DR PDB; 5JJJ; X-ray; 2.50 A; B=5-137.
DR PDB; 5JJN; X-ray; 2.25 A; B/D=5-137.
DR PDBsum; 1H2S; -.
DR PDBsum; 2F93; -.
DR PDBsum; 2F95; -.
DR PDBsum; 2RM8; -.
DR PDBsum; 4GYC; -.
DR PDBsum; 5JJE; -.
DR PDBsum; 5JJF; -.
DR PDBsum; 5JJJ; -.
DR PDBsum; 5JJN; -.
DR AlphaFoldDB; P42259; -.
DR BMRB; P42259; -.
DR SASBDB; P42259; -.
DR SMR; P42259; -.
DR DIP; DIP-35283N; -.
DR IntAct; P42259; 2.
DR MINT; P42259; -.
DR EvolutionaryTrace; P42259; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR040913; Htr2.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF17909; Htr2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Chromophore; Membrane;
KW Methylation; Photoreceptor protein; Receptor; Repeat; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Sensory rhodopsin II transducer"
FT /id="PRO_0000110555"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT TOPO_DOM 44..59
FT /note="Extracellular"
FT TRANSMEM 60..81
FT /note="Helical; Name=2"
FT TOPO_DOM 82..534
FT /note="Cytoplasmic"
FT DOMAIN 84..136
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 157..210
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 229..465
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 463..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 23..48
FT /evidence="ECO:0007829|PDB:5JJE"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2F93"
FT HELIX 53..82
FT /evidence="ECO:0007829|PDB:5JJE"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2RM8"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2RM8"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2RM8"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2RM8"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:2RM8"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2RM8"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2RM8"
SQ SEQUENCE 534 AA; 56622 MW; CBE8012CC5F278E8 CRC64;
MSLNVSRLLL PSRVRHSYTG KMGAVFIFVG ALTVLFGAIA YGEVTAAAAT GDAAAVQEAA
VSAILGLIIL LGINLGLVAA TLGGDTAASL STLAAKASRM GDGDLDVELE TRREDEIGDL
YAAFDEMRQS VRTSLEDAKN AREDAEQAQK RAEEINTELQ AEAERFGEVM DRCADGDFTQ
RLDAETDNEA MQSIEGSFNE MMDGIEALVG RIERFADAVS EDAEAVRANA ESVMEASEDV
NRAVQNISDA AGDQTETVQQ IALEMDDVSA TTEEVAASAD DIAKTARQAA ETGEAGRETA
ETAITEMNEV ESRTEQAVAS MEELNEDVRE IGEVSEMIAD IAEQTNILAL NASIEAARAD
GNSEGFAVVA DEVKALAEET KAATEEIDDL IGTVQDRTQT TVDDIRETSD QVSEGVETVE
DTVDALERIV DSVERTNDGI QEINQSTDAQ ADAAQKATTM VEDMAATSEQ TASDAETAAE
TTETQAESVK EVFDLIDGLS EQADSLSETL SRTDTEEASA ADLDDQPTLA AGDD
