HTR2_HALSA
ID HTR2_HALSA Reviewed; 764 AA.
AC Q9HP81; P71410;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
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; OrderedLocusNames=VNG_1765G;
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].
RC STRAIN=Flx15;
RX PubMed=8710852; DOI=10.1073/pnas.93.16.8230;
RA Zhang W., Brooun A., Mueller M.M., Alam M.;
RT "The primary structures of the Archaeon Halobacterium salinarium blue light
RT receptor sensory rhodopsin II and its transducer, a methyl-accepting
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8230-8235(1996).
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).
RN [3]
RP FUNCTION.
RX PubMed=9515936; DOI=10.1128/jb.180.6.1600-1602.1998;
RA Hou S., Brooun A., Yu H.S., Freitas T., Alam M.;
RT "Sensory rhodopsin II transducer HtrII is also responsible for serine
RT chemotaxis in the archaeon Halobacterium salinarum.";
RL J. Bacteriol. 180:1600-1602(1998).
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. {ECO:0000269|PubMed:9515936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Methylated by CheR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; U62676; AAC44369.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19989.1; -; Genomic_DNA.
DR PIR; A84328; A84328.
DR PIR; T44946; T44946.
DR RefSeq; WP_010903287.1; NC_002607.1.
DR AlphaFoldDB; Q9HP81; -.
DR SMR; Q9HP81; -.
DR STRING; 64091.VNG_1765G; -.
DR PaxDb; Q9HP81; -.
DR EnsemblBacteria; AAG19989; AAG19989; VNG_1765G.
DR GeneID; 5954313; -.
DR KEGG; hal:VNG_1765G; -.
DR PATRIC; fig|64091.14.peg.1344; -.
DR HOGENOM; CLU_000445_107_19_2; -.
DR InParanoid; Q9HP81; -.
DR OMA; VEQTNML; -.
DR OrthoDB; 10018at2157; -.
DR PhylomeDB; Q9HP81; -.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 2.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 3: Inferred from homology;
KW Cell membrane; Chemotaxis; Chromophore; Membrane; Methylation;
KW Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..764
FT /note="Sensory rhodopsin II transducer"
FT /id="PRO_0000110549"
FT TOPO_DOM 2..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 303..355
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 397..450
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 469..705
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 347..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 107..110
FT /note="VVAA -> RWFAG (in Ref. 1; AAC44369)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="E -> Q (in Ref. 1; AAC44369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 79042 MW; D5EB26F706576996 CRC64;
MGSGLVARIR GSYGTKLTLA LVVVVVLSVG VGTFVYQQTT TQLETDVRAD LTGSADARAD
HLDAWLSNAR GQTQLASRHP VLASGNDTAI TRYLEGLAAS DERPDGVVAA HVYNTSTTTI
EASSADAFTG VNPREQGAPF ATDPPSFATT SDVVVAAPFT VPAADFPVLS VLSPIPGTTD
KALIYMVNVN TLTDDFGQNV AGSTTTVVSA DGTYVSHPDQ DRVLTGHDGP SRLLNQSRTQ
PAYIDANGTV TAAAPVDGAP WSVLVRAPHD RAFALGDFVA SSLVGLVLIT IVSLSLIGVT
VGSTTVTALR QFSRRADEMA AGDLDTDIDT SRNDEFGTLA ESFRSMRDSL SESLTDAERA
TARAEDARED AEQQRADAEA AREDAEAARK DAQETARALE SAAADYEEAL TAVADGDLTR
RVDASRDHDA MARIGHALND MLDDIETSVA AATAFSDHVS DAAQRVEADA GDAIDAGTDV
STAVDEISDG ATEQTDRLHE VAGEVDDLSA SAEEVAETVA SLADTAGQAA SAVDDGRQAT
EDAVETMDDV ADDAEAAADA MDALDSEMAD IGEIVDVIAD IADQTNMLAL NASIEAARTG
ADGDGFAVVA DEVKTLAEES RDAAEDIESR LLALQGQVSD VADEMRATSD TVSDGRATVG
DAATALDDVV SFVADTDTAA GEIRAATDRQ AHAASRVASA VDEVAGISQE TAAQATAVAD
SAATQTDTLS SVDDAAADLA DRAAALDDLL AEFDAHDDTE PEDY
