ID   BASB_HALS3              Reviewed;         413 AA.
AC   B0R6I5; F2Z6C3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Chemotactic signal transduction system substrate-binding protein BasB;
DE   AltName: Full=Amino acid binding protein;
DE   Flags: Precursor;
GN   Name=basB; OrderedLocusNames=OE_3612R;
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 IN CHEMOTAXIS, SUBCELLULAR
RP   LOCATION, DISRUPTION PHENOTYPE, 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   [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).
CC   -!- FUNCTION: Mediates chemotaxis towards five attractant amino acids
CC       (leucine, isoleucine, valine, methionine and cysteine). May function as
CC       a receptor that binds the amino acids and transduces a signal to BasT.
CC       Has probably no additional role in transport.
CC       {ECO:0000269|PubMed:12006484}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12006484};
CC       Peripheral membrane protein {ECO:0000305|PubMed:12006484};
CC       Extracellular side {ECO:0000305|PubMed:12006484}. Note=Probably
CC       anchored to the membrane by lipids.
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:12006484}.
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DR   EMBL; AJ438168; CAD27274.1; -; Genomic_DNA.
DR   EMBL; AM774415; CAP14354.1; -; Genomic_DNA.
DR   PIR; A84337; A84337.
DR   RefSeq; WP_010903360.1; NC_010364.1.
DR   AlphaFoldDB; B0R6I5; -.
DR   SMR; B0R6I5; -.
DR   EnsemblBacteria; CAP14354; CAP14354; OE_3612R.
DR   GeneID; 5953582; -.
DR   KEGG; hsl:OE_3612R; -.
DR   HOGENOM; CLU_027128_5_0_2; -.
DR   OMA; LWPETGS; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   InterPro; IPR028081; Leu-bd.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF13458; Peripla_BP_6; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chemotaxis; Membrane; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..413
FT                   /note="Chemotactic signal transduction system substrate-
FT                   binding protein BasB"
FT                   /id="PRO_0000428987"
SQ   SEQUENCE   413 AA;  41210 MW;  009949A93E45FA80 CRC64;
     MHSTTRREWL GAIGATAATG LAGCAGVGGA GQPVTVGSLL PLSGPGSLGA LAADHQRAID
     TAVEHANRGG GINGRDVVHV SKDTEADPSV AADRYATLAA DESPLAIVGP VLSGVTTALT
     EQAAADAQLL VSPSTTAPAI ATAGRSDGQK FVARTCPNDS QQAAVMAKIV DDDMYAAADT
     ATILYVDNAF GAALADVLAD RLGADLLASV PYQGGTDTPG GPVDDALAPD PDAVAFIGSP
     GSSSGVIDEL VGREYGGEIA LSSALASASS PPSWNGAYTA TVNSASTVGT KRLRRALSDA
     TPLQPYTENA YDAAALALLA ASYSGDPTPR AVAGALQSVS GGVGHSITVG DFGRATDLID
     AGRELNYNGA TGNVDLTAAL EPVTGYLIQQ LTDAGIETRE LLKSGYFTDG GDA