BAST_HALS3
ID BAST_HALS3 Reviewed; 805 AA.
AC B0R6I4; Q9P9J0;
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 BasT;
DE AltName: Full=Branched chain and sulfur-containing amino acids transducer protein;
GN Name=basT; Synonyms=htr3; OrderedLocusNames=OE_3611R;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP METHYLATION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=R1 / S9;
RX PubMed=10672186; DOI=10.1046/j.1365-2958.2000.01735.x;
RA Kokoeva M.V., Oesterhelt D.;
RT "BasT, a membrane-bound transducer protein for amino acid detection in
RT Halobacterium salinarum.";
RL Mol. Microbiol. 35:647-656(2000).
RN [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [4]
RP METHYLATION AT GLU-554; GLU-736 AND GLU-763.
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 [5]
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 five attractant amino acids
CC (leucine, isoleucine, valine, methionine and cysteine). Probably
CC transduces the signal from the substrate-binding protein BasB to the
CC histidine kinase CheA. {ECO:0000269|PubMed:10672186,
CC 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:10672186};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10672186}.
CC -!- PTM: Methylated by CheR. {ECO:0000269|PubMed:10672186,
CC ECO:0000269|PubMed:18514223}.
CC -!- DISRUPTION PHENOTYPE: Mutants completely lose the chemotactic response
CC towards leucine, isoleucine, valine, methionine and cysteine, but they
CC still respond to arginine. {ECO:0000269|PubMed:10672186,
CC ECO:0000269|PubMed:12006484}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AJ245950; CAB82572.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP14353.1; -; Genomic_DNA.
DR PIR; T48840; T48840.
DR RefSeq; WP_012289396.1; NC_010364.1.
DR AlphaFoldDB; B0R6I4; -.
DR SMR; B0R6I4; -.
DR EnsemblBacteria; CAP14353; CAP14353; OE_3611R.
DR GeneID; 5953137; -.
DR KEGG; hsl:OE_3611R; -.
DR HOGENOM; CLU_000445_107_19_2; -.
DR OMA; WLEQKLI; -.
DR PhylomeDB; B0R6I4; -.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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..805
FT /note="Transducer protein BasT"
FT /id="PRO_0000428989"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 317..370
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 437..490
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 509..745
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 513..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 554
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
FT MOD_RES 736
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
FT MOD_RES 763
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:18514223"
SQ SEQUENCE 805 AA; 84831 MW; 089CA734D3F9DE3D CRC64;
MSDIDRGLFE RVLPARIRGS YAAKFNVLLL VVVIIVAAAG GYIHLQTQST VGENTERRVS
GIAEQQAATL HDWLTQKEST TTFLASNIGG DAVRTSDVKP QLERQLATLQ QDVRAIHVVS
TSQDTVVAST DDARSGTTLQ AGDAPWLSTI EDGTTDVSVS DPYEVDDSPV VAMTAPTDKP
GWVLVMTMSL AQHSQSFNSP IATGDVKVVN GDGVITLDNR NRALLEQYTD TAGNVPAAVA
TARSGQTVYN TEPERTGMDD GRYATAYTPV AGTDWVLTYH VPRGQAYALQ SEVTQNLAGL
VVVALVGLLL VGLTVGRRTS SALDELAGVA AAIADGDLDT TIPDTDRTDE LGQLVGAFGE
MQTYLTTAAS QADALADQNF DADVLDEDLP GAFGASLSQM HTRLEALITD LDEAREDAEQ
TRKDAEEARA ASERLNERLE RRAAEYSDEM AAAAAGDLTR RLDEDVDSEP MQDIAEAFND
MMGDVEATLA QVRSIADAVD AASTDVSTSA AEIRSASDQV SESVQDISAD ADQQRDRLGT
VGDEVTSLSA TVEEIAASAD DVAETVNQAA TESERGQELG EDAVAELERI EATADSAVER
VTALEEAVDA IGDVTGVITD IAEQTNMLAL NANIEAARAD KSGDGFAVVA DEVKDLADEV
KESATEIETL VDDVQADVAD TVADMSELGD RVDAGSETIE AALAALDDIG DQVEAANGSV
QSISDATDEQ AASTEEVVTM IDEVTDLSDR TATESQQVSA AAEEQAASVS EVAGRADDLD
DQVSTLNDLL DQFDARAASA DTDEN
