TRKA_ECOLI
ID TRKA_ECOLI Reviewed; 458 AA.
AC P0AGI8; P23868; P77041; Q2M6V4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Trk system potassium uptake protein TrkA;
DE Short=K(+)-uptake protein TrkA;
GN Name=trkA; OrderedLocusNames=b3290, JW3251;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32, AND FUNCTION.
RX PubMed=8412700; DOI=10.1111/j.1365-2958.1993.tb01714.x;
RA Schloesser A., Hamann A., Bossemeyer D., Schneider E., Bakker E.P.;
RT "NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence
RT similarity between TrkA and domains of a family of dehydrogenases suggest a
RT role for NAD+ in bacterial transport.";
RL Mol. Microbiol. 9:533-543(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / K37;
RX PubMed=7961514; DOI=10.1128/jb.176.23.7387-7390.1994;
RA Meinnel T., Blanquet S.;
RT "Characterization of the Thermus thermophilus locus encoding peptide
RT deformylase and methionyl-tRNA(fMet) formyltransferase.";
RL J. Bacteriol. 176:7387-7390(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835;
RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.;
RT "A survey of polypeptide deformylase function throughout the eubacterial
RT lineage.";
RL J. Mol. Biol. 266:939-949(1997).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=2674131; DOI=10.1016/s0021-9258(19)84721-x;
RA Bossemeyer D., Borchard A., Dosch D.C., Helmer G.C., Epstein W.,
RA Booth I.R., Bakker E.P.;
RT "K+-transport protein TrkA of Escherichia coli is a peripheral membrane
RT protein that requires other trk gene products for attachment to the
RT cytoplasmic membrane.";
RL J. Biol. Chem. 264:16403-16410(1989).
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. {ECO:0000269|PubMed:2674131,
CC ECO:0000269|PubMed:8412700}.
CC -!- INTERACTION:
CC P0AGI8; P69829: ptsN; NbExp=3; IntAct=EBI-1132371, EBI-547017;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2674131};
CC Peripheral membrane protein {ECO:0000269|PubMed:2674131}; Cytoplasmic
CC side {ECO:0000269|PubMed:2674131}. Note=Peripherally bound to the inner
CC side of the inner membrane via the TrkG and TrkH proteins.
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; X52114; CAA36359.1; -; Genomic_DNA.
DR EMBL; X77091; CAA54371.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58087.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76315.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78002.1; -; Genomic_DNA.
DR EMBL; Y10307; CAA71360.1; -; Genomic_DNA.
DR PIR; S36252; S36252.
DR RefSeq; NP_417748.1; NC_000913.3.
DR RefSeq; WP_000691382.1; NZ_STEB01000038.1.
DR AlphaFoldDB; P0AGI8; -.
DR SMR; P0AGI8; -.
DR BioGRID; 4263438; 20.
DR DIP; DIP-35971N; -.
DR IntAct; P0AGI8; 5.
DR STRING; 511145.b3290; -.
DR TCDB; 2.A.38.1.1; the k(+) transporter (trk) family.
DR jPOST; P0AGI8; -.
DR PaxDb; P0AGI8; -.
DR PRIDE; P0AGI8; -.
DR EnsemblBacteria; AAC76315; AAC76315; b3290.
DR EnsemblBacteria; BAE78002; BAE78002; BAE78002.
DR GeneID; 67415330; -.
DR GeneID; 947788; -.
DR KEGG; ecj:JW3251; -.
DR KEGG; eco:b3290; -.
DR PATRIC; fig|1411691.4.peg.3442; -.
DR EchoBASE; EB1012; -.
DR eggNOG; COG0569; Bacteria.
DR HOGENOM; CLU_046525_0_2_6; -.
DR InParanoid; P0AGI8; -.
DR OMA; IACQVAY; -.
DR PhylomeDB; P0AGI8; -.
DR BioCyc; EcoCyc:TRKA-MON; -.
DR PRO; PR:P0AGI8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IDA:EcoCyc.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Membrane; NAD; Potassium; Potassium transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..458
FT /note="Trk system potassium uptake protein TrkA"
FT /id="PRO_0000148712"
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
