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Database: UniProt
Entry: B0R5I3_HALS3
LinkDB: B0R5I3_HALS3
Original site: B0R5I3_HALS3 
ID   B0R5I3_HALS3            Unreviewed;       481 AA.
AC   B0R5I3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Transducer protein Htr9 {ECO:0000313|EMBL:CAP14000.1};
GN   Name=htr9 {ECO:0000313|EMBL:CAP14000.1};
GN   Synonyms=htpIII:htA {ECO:0000313|EMBL:CAP14000.1};
GN   OrderedLocusNames=OE_2996R {ECO:0000313|EMBL:CAP14000.1};
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:CAP14000.1, ECO:0000313|Proteomes:UP000001321};
RN   [1] {ECO:0000313|EMBL:CAP14000.1, 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; CAP14000.1; -; Genomic_DNA.
DR   RefSeq; WP_010903014.1; NC_010364.1.
DR   AlphaFoldDB; B0R5I3; -.
DR   SMR; B0R5I3; -.
DR   EnsemblBacteria; CAP14000; CAP14000; OE_2996R.
DR   GeneID; 68694125; -.
DR   KEGG; hsl:OE_2996R; -.
DR   HOGENOM; CLU_000445_116_0_2; -.
DR   PhylomeDB; B0R5I3; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000014; PAS.
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; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          10..65
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          208..444
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   481 AA;  50774 MW;  B333B55DBFE206D1 CRC64;
     MSKNKHELGS PFTVPLLLNT LDVPAFAVDA DGAVVAWDDQ IAALLETAPE DAIGVTDIGE
     RLNDDGSRAL ANKVADTPID AHHEYDGVGL ADESYALLTG DYVYEDTTVA GNTDLWFIAT
     PVYHTGEFRG VIEIVQDRSS SARYQSELQA LFGELVDTLD AYDAGRFDAT VDIAAEDTLL
     DDEYIQIGRN LTEFGDTLAA HITEVHNDVE RLEAASQAVS ESSAEIDELS TAQSTNVSTV
     ATEVETLSAT VQEIASTADE VVDTSATAER LADDGSAAAS DAADMMADVA TAADSVTSDV
     EALQNRIEDI DEVVDVITGI AEQTNMLALN ASIEAARAGE EGEGFAVVAE EVKALAEDAQ
     SNAGHIESLV SEIQRDTADT VTDLVTTTDR IEDAVAQVED AMASFEEIVT AVEATAEGIE
     QVSDATNEQA ASAEEIAAMV DETADLADDI TTAVADIVSQ TEAQSAMLHD LDESVSELHD
     Q
//
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