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Database: UniProt
Entry: B0R3S6_HALS3
LinkDB: B0R3S6_HALS3
Original site: B0R3S6_HALS3 
ID   B0R3S6_HALS3            Unreviewed;       792 AA.
AC   B0R3S6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Transducer protein Htr16 {ECO:0000313|EMBL:CAP13390.1};
GN   Name=htr16 {ECO:0000313|EMBL:CAP13390.1};
GN   OrderedLocusNames=OE_1929R {ECO:0000313|EMBL:CAP13390.1};
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=478009 {ECO:0000313|EMBL:CAP13390.1, ECO:0000313|Proteomes:UP000001321};
RN   [1] {ECO:0000313|EMBL:CAP13390.1, ECO:0000313|Proteomes:UP000001321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1 {ECO:0000313|Proteomes:UP000001321};
RX   PubMed=18313895; DOI=.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).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; AM774415; CAP13390.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0R3S6; -.
DR   EnsemblBacteria; CAP13390; CAP13390; OE_1929R.
DR   KEGG; hsl:OE_1929R; -.
DR   HOGENOM; CLU_000445_107_19_2; -.
DR   PhylomeDB; B0R3S6; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0016020; C:membrane; 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   CDD; cd06225; HAMP; 2.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 6.10.340.10; -; 1.
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; 2.
DR   SMART; SM00283; MA; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          313..366
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          433..486
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          505..741
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          740..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          393..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        745..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  84906 MW;  2D363E2B7B1CEB44 CRC64;
     MSRVTLEDTL PDWVRRSYVR KFSVLAAVLI VSIVVTGVVT QTAVSNQLTD QQQATLLTNA
     DQEAGSLEQW VQSQRSTVRT LSKHRGLTAD SNAAVRQTLA TEREFLPPEV AHLHYVGRQN
     GSIRASTDRQ LEGAGIAATN IVWPQEQAFS DVSFETPDAV VQTWMYTDDG TPSVAYASPV
     PEEDALLIAV VRTSERAQRF TSAINGTKTT AVGDTTGDVL FDRNESAFLT QYQSIGGSGV
     IETIESQDRG TVVTEDTIIA FAAVQDDATN WVVVKETPKS DALAIANNVQ TNIWVLLGLT
     LVGLVGFVAV VRAGLIGSLR EITTQTAAIA DGNLDQEIQD NGRIDEIGRV RSGFRDIKSY
     LQTVEGQAIA LSQQDFDNDV LDDEVPGTLG ESLTAMQTDL ETFIEDLTDA REEAERSQRD
     AEQSREEAQA LADSLERQAE RFSTQMQQAA DGDLTQRLDT DVDRESLAQI ATAFNDMLVQ
     LEALVDRIQA TANAVDDRTH AMSASTDEIE QSSMSVAKSI EQISAGAENQ NEKLTAAAGE
     MTDLSATVEE IASSSNNVAQ QAEDAAAMGQ DGQAAATDAI AEMDAIESKA TQTVEEMQSL
     QEEVGRISDI VTMIDDIASQ TDMLAINASI EAENASTSGD GFAVVADEVK SLAEDTATAT
     DEVESLIAEV EASTSALAED MYEMRDRVGD GQDTITDTAA LLEDIVDRVE DANAGIQSIN
     DATEDQAASV QEATRMVEEV ASVSDQTAGE ASNVSAAAEE QTSAIQEISQ SAQSLQTQAT
     ELLDRAEQFD TS
//
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