ID   TRKA_ECOL6              Reviewed;         458 AA.
AC   P0AGI9; P23868; P77041;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Trk system potassium uptake protein TrkA;
DE            Short=K(+)-uptake protein TrkA;
GN   Name=trkA; OrderedLocusNames=c4050;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the constitutive potassium transport systems TrkG and
CC       TrkH. May regulate the transport activity of TrkG and TrkH systems.
CC       Binds to NAD(+) and NADH (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Note=Peripherally bound to the inner side of the inner membrane via the
CC       TrkG and TrkH proteins. {ECO:0000250}.
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}.
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DR   EMBL; AE014075; AAN82488.1; -; Genomic_DNA.
DR   RefSeq; WP_000691382.1; NC_004431.1.
DR   AlphaFoldDB; P0AGI9; -.
DR   SMR; P0AGI9; -.
DR   STRING; 199310.c4050; -.
DR   PRIDE; P0AGI9; -.
DR   EnsemblBacteria; AAN82488; AAN82488; c4050.
DR   GeneID; 67415330; -.
DR   KEGG; ecc:c4050; -.
DR   eggNOG; COG0569; Bacteria.
DR   HOGENOM; CLU_046525_0_2_6; -.
DR   OMA; IACQVAY; -.
DR   BioCyc; ECOL199310:C4050-MON; -.
DR   Proteomes; UP000001410; Chromosome.
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_0000148714"
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;  50368 MW;  1FF01BC23F4DC40F CRC64;
     MKIIILGAGQ VGGTLAENLV GENNDITVVD TNGERLRTLQ DKFDLRVVQG HGSHPRVLRE
     AGADDADMLV AVTSSDETNM VACQVAYSLF NTPNRIARIR SPDYVRDADK LFHSDAVPID
     HLIAPEQLVI DNIYRLIEYP GALQVVNFAE GKVSLAVVKA YYGGPLIGNA LSTMREHMPH
     IDTRVAAIFR HDRPIRPQGS TIVEAGDEVF FIAASQHIRA VMSELQRLEK PYKRIMLVGG
     GNIGAGLARR LEKDYSVKLI ERNQQRAAEL AEKLQNTIVF FGDASDQELL AEEHIDQVDL
     FIAVTNDDEA NIMSAMLAKR MGAKKVMVLI QRRAYVDLVQ GSVIDIAISP QQATISALLS
     HVRKADIVGV SSLRRGVAEA IEAVAHGDES TSRVVGRVID EIKLPPGTII GAVVRGNDVM
     IANDNLRIEQ GDHVIMFLTD KKFITDVERL FQPSPFFL