ID   TRKA_VIBAL              Reviewed;         458 AA.
AC   P39448;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Trk system potassium uptake protein TrkA;
DE            Short=K(+)-uptake protein TrkA;
GN   Name=trkA;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=138-2;
RX   PubMed=7948029; DOI=10.1016/0167-4781(94)90231-3;
RA   Nakamura T., Matsuba Y., Yamamuro N., Booth I.R., Unemoto T.;
RT   "Cloning and sequencing of a K+ transport gene (trk A) from the marine
RT   bacterium Vibrio alginolyticus.";
RL   Biochim. Biophys. Acta 1219:701-705(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=138-2;
RX   PubMed=9720051; DOI=10.1099/00221287-144-8-2281;
RA   Nakamura T., Yamamuro N., Stumpe S., Unemoto T., Bakker E.P.;
RT   "Cloning of the trkAH gene cluster and characterization of the Trk K+-
RT   uptake system of Vibrio alginolyticus.";
RL   Microbiology 144:2281-2289(1998).
CC   -!- FUNCTION: Part of a potassium transport system.
CC       {ECO:0000269|PubMed:9720051}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9720051};
CC       Peripheral membrane protein {ECO:0000269|PubMed:9720051}; Cytoplasmic
CC       side {ECO:0000269|PubMed:9720051}.
CC   -!- DOMAIN: The RCK N-terminal domain binds NAD and possibly other
CC       effectors. This is expected to cause a conformation change that
CC       regulates potassium transport (By similarity). {ECO:0000250}.
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; D28477; BAA05838.1; -; Genomic_DNA.
DR   EMBL; D86411; BAA31228.1; -; Genomic_DNA.
DR   PIR; S50220; S50220.
DR   AlphaFoldDB; P39448; -.
DR   SMR; P39448; -.
DR   STRING; 663.BAU10_14925; -.
DR   eggNOG; COG0569; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 3.30.70.1450; -; 2.
DR   InterPro; IPR006036; K_uptake_TrkA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006037; RCK_C.
DR   InterPro; IPR036721; RCK_C_sf.
DR   InterPro; IPR003148; RCK_N.
DR   Pfam; PF02080; TrkA_C; 2.
DR   Pfam; PF02254; TrkA_N; 2.
DR   PRINTS; PR00335; KUPTAKETRKA.
DR   SUPFAM; SSF116726; SSF116726; 2.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   PROSITE; PS51202; RCK_C; 2.
DR   PROSITE; PS51201; RCK_N; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; NAD;
KW   Potassium; Potassium transport; Repeat; Transport.
FT   CHAIN           1..458
FT                   /note="Trk system potassium uptake protein TrkA"
FT                   /id="PRO_0000148719"
FT   DOMAIN          2..131
FT                   /note="RCK N-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   DOMAIN          143..227
FT                   /note="RCK C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   DOMAIN          234..356
FT                   /note="RCK N-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   DOMAIN          368..453
FT                   /note="RCK C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT   BINDING         7..11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         234..262
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   458 AA;  50125 MW;  309B2AC490C03472 CRC64;
     MKIIILGAGQ VGGTLAENLV GENNDITIVD NNADRLRELQ DKYDLRVVNG HASHPDVLHE
     AGAQDADMLV AVTNTDETNM AACQVAFTLF NTPNRVARIR SPEYLAEKEA LFKSGAIPVD
     HLIAPEELVT SYIERLIQYP GALQVVSFAE QKVSLVAVKA YYGGPLVGNA LSALREHMPH
     IDTRVAAIFR QGRPIRPQGT TIIEADDEVF FVAASNHIRS VMSELQRLEK PYRRIMIVGG
     GNIGASLAKR LEQNYSVKLI ERNYQRAEKL SEELENTIVF CGDAADQELL SEENIDQVDV
     FIALTNEDET NIMSAMLAKR MGAKKVMVLI QRGAYVDLVQ GGVIDVAISP QQATISALLT
     HVRRADIVNV SSLRRGAAEA IEAVAHGDES TSKVVGRAIG DIKLPPGTTI GAIVRGEEVL
     IAHDRTVIEQ DDHVVMFLVN KKYVSDVEAL FQPSPFFL