ID B0R688_HALS3 Unreviewed; 536 AA.
AC B0R688;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Transducer protein Htr17 {ECO:0000313|EMBL:CAP14257.1};
GN Name=htr17 {ECO:0000313|EMBL:CAP14257.1};
GN OrderedLocusNames=OE_3436R {ECO:0000313|EMBL:CAP14257.1};
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:CAP14257.1, ECO:0000313|Proteomes:UP000001321};
RN [1] {ECO:0000313|EMBL:CAP14257.1, 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; CAP14257.1; -; Genomic_DNA.
DR RefSeq; WP_010903266.1; NC_010364.1.
DR AlphaFoldDB; B0R688; -.
DR EnsemblBacteria; CAP14257; CAP14257; OE_3436R.
DR GeneID; 68694385; -.
DR KEGG; hsl:OE_3436R; -.
DR HOGENOM; CLU_000445_107_18_2; -.
DR PhylomeDB; B0R688; -.
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; cd11386; MCP_signal; 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; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 3.
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; 1.
PE 3: Inferred from homology;
KW 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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..206
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 225..461
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 100..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 56816 MW; 3B33D2FD8701EE04 CRC64;
MNHLIVLFDV IAVAAYVAAI GVGIQTYRDT TDIAGFWVNY TYICGLGFLW TGVVALEWIG
VAGPVMDAFS TSLLAVLIGV VAISSTGTIS IVEDLKTSNA RAHRRRKDAE QAKRRADEQR
AQAQEAKAEA QDAREEAETL AAKLQERAAE RDAQLSKKAS EYSSVMEKAA SGDLTVRANS
SSDSDAMTEV GQAFNEMIAA FEEMVARTRE FAGDVADNSR DIHASVDEIE AASEQVAESV
QEISAGTDRE HTRLADATDE LQSLSGAVEE VAASASQVAD VSDQAADRGR QGSDDAAAAV
TQMTDIQSET EAVVSEANAL AAEAQEIRRV VDLINDITDQ THLLALNASI EAARADQDGD
GFAVVAAEVK ELAEETNEAT DEIETLVDNL LSSTQSVVDD SEQMAATVSS GTETVENALT
ALEEIGDHVT DVNEAVQQID DATDAQAASA DTTVSMIEEI EDISEQNSSE AASVSAAAQQ
QTASLSDVTD GVTRLVDRAD TLQDVLTGFT VDSDDYELDV DTSRPATTNP ELEADD
//
