COST_HALS3
ID COST_HALS3 Reviewed; 810 AA.
AC B0R6A7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Transducer protein CosT;
DE AltName: Full=Compatible solute transducer protein;
GN Name=cosT; Synonyms=htr5; OrderedLocusNames=OE_3474R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/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).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, METHYLATION, AND GENE NAME.
RC STRAIN=R1 / S9;
RX PubMed=12006484; DOI=10.1093/emboj/21.10.2312;
RA Kokoeva M.V., Storch K.F., Klein C., Oesterhelt D.;
RT "A novel mode of sensory transduction in archaea: binding protein-mediated
RT chemotaxis towards osmoprotectants and amino acids.";
RL EMBO J. 21:2312-2322(2002).
RN [3]
RP METHYLATION AT GLU-556 AND GLU-739.
RC STRAIN=R1 / S9;
RX PubMed=18514223; DOI=10.1016/j.jmb.2008.04.063;
RA Koch M.K., Staudinger W.F., Siedler F., Oesterhelt D.;
RT "Physiological sites of deamidation and methyl esterification in sensory
RT transducers of Halobacterium salinarum.";
RL J. Mol. Biol. 380:285-302(2008).
RN [4]
RP INTERACTION WITH CHEA; CHEY; CHEW1 AND CHEW2.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=23171228; DOI=10.1186/1471-2180-12-272;
RA Schlesner M., Miller A., Besir H., Aivaliotis M., Streif J., Scheffer B.,
RA Siedler F., Oesterhelt D.;
RT "The protein interaction network of a taxis signal transduction system in a
RT halophilic archaeon.";
RL BMC Microbiol. 12:272-272(2012).
CC -!- FUNCTION: Mediates chemotaxis towards compatible osmolytes. Probably
CC transduces the signal from the substrate-binding protein CosB to the
CC histidine kinase CheA. {ECO:0000269|PubMed:12006484}.
CC -!- SUBUNIT: Interacts with CheA, CheY, CheW1 and CheW2.
CC {ECO:0000269|PubMed:23171228}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12006484};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12006484}.
CC -!- PTM: Methylated by CheR. {ECO:0000269|PubMed:12006484,
CC ECO:0000269|PubMed:18514223}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM774415; CAP14276.1; -; Genomic_DNA.
DR RefSeq; WP_010903284.1; NC_010364.1.
DR AlphaFoldDB; B0R6A7; -.
DR SMR; B0R6A7; -.
DR EnsemblBacteria; CAP14276; CAP14276; OE_3474R.
DR GeneID; 5953905; -.
DR KEGG; hsl:OE_3474R; -.
DR HOGENOM; CLU_000445_107_19_2; -.
DR OMA; WERTIVD; -.
DR PhylomeDB; B0R6A7; -.
DR Proteomes; UP000001321; 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: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; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 3.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Membrane; Methylation; Repeat; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..810
FT /note="Transducer protein CosT"
FT /id="PRO_0000428991"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 345..397
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 439..493
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 512..748
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 403..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 556
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
FT MOD_RES 739
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
SQ SEQUENCE 810 AA; 85219 MW; 4BF36E4B7D22BD80 CRC64;
MSEPTADAGD NSPSSTDTAP LDRVKAIALL PLRSYLVKFA VALLVILVII AAGGFWVQAD
ATATLEANTE QQLEQEAVSD ATEIGDWLER NEQSVLIASN NPRLGFNTTA ADKQAYVTQL
VAAELDADRI ADVHVADPTV GGASDARIVA STDEDARGTR VSADTHPWVD RTRSIGRDTV
VSTNPYRTAG GQRVVSSMSV AADLTHVLVV EYTAGDLSDQ FGAGIDGTFT QVVRPTSDAT
AVLFSDAGTD AVGQPYIPDR SQSEIPALDS ATEQGQFTNT PTKDSVLDRE YVAAYTTVPG
KNWVVVKHAP SESAFALSNQ IRTGILGFIL VALVGVVLVG GTIGRNTAAA VQSLSAAAAE
IEAGNYDVDV ASSRRDEIGQ LFASIGSMRD ALVTQIDEAE AAREQATEAQ QDAEAERERA
EDARERAEDA KADAEALAAE LEAQAERYSD VMAACADGDL TRRMPADDTD NEAMAAIAAS
FNEMLAQWEH TIIDIQEFAD AVATASEEAE VGAADAERAS GQVSESVQEI AGAADEQRNM
LDTVSGEMTD LSAAIEEVAA SADSVAEHSH QTAEIARDGE QTAEDAIERS LTVQEAIDAT
VQNVEALDDQ MAEISEIVDL ISDIAEQTNM LALNANIEAA RADKSGDGFA VVADEVKDLA
EETQESAGDI ERRITEVQSQ TTATVAEARA AEESMDAGID AVEEVVDAFT AVSDHADETD
TGVQEISDTT DDQAASTEEA VSMTEEVADL SDSTAGEAQS VSAAAEEQAA SMSEISDSVE
SLSGQAEQLK ALLSEFEVDA DRDVTPTQTD
