TRKA_METJA
ID TRKA_METJA Reviewed; 218 AA.
AC Q58505;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Trk system potassium uptake protein TrkA homolog;
DE Short=K(+)-uptake protein TrkA homolog;
GN Name=trkA; OrderedLocusNames=MJ1105;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-136 IN COMPLEX WITH NAD,
RP DOMAIN, AND SUBUNIT.
RX PubMed=12086676; DOI=10.1016/s0092-8674(02)00768-7;
RA Roosild T.P., Miller S., Booth I.R., Choe S.;
RT "A mechanism of regulating transmembrane potassium flux through a ligand-
RT mediated conformational switch.";
RL Cell 109:781-791(2002).
CC -!- FUNCTION: Part of a potassium transport system. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:12086676}.
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. {ECO:0000269|PubMed:12086676}.
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DR EMBL; L77117; AAB99108.1; -; Genomic_DNA.
DR PIR; H64437; H64437.
DR RefSeq; WP_010870617.1; NC_000909.1.
DR PDB; 1LSS; X-ray; 2.30 A; A/B/C/D=1-136.
DR PDBsum; 1LSS; -.
DR AlphaFoldDB; Q58505; -.
DR SMR; Q58505; -.
DR STRING; 243232.MJ_1105; -.
DR EnsemblBacteria; AAB99108; AAB99108; MJ_1105.
DR GeneID; 1452002; -.
DR KEGG; mja:MJ_1105; -.
DR eggNOG; arCOG01957; Archaea.
DR HOGENOM; CLU_046525_2_3_2; -.
DR InParanoid; Q58505; -.
DR OMA; QRCNVVI; -.
DR OrthoDB; 116057at2157; -.
DR PhylomeDB; Q58505; -.
DR EvolutionaryTrace; Q58505; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.30.70.1450; -; 1.
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; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR PRINTS; PR00335; KUPTAKETRKA.
DR SUPFAM; SSF116726; SSF116726; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51202; RCK_C; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; NAD; Potassium; Potassium transport;
KW Reference proteome; Transport.
FT CHAIN 1..218
FT /note="Trk system potassium uptake protein TrkA homolog"
FT /id="PRO_0000148725"
FT DOMAIN 2..124
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT DOMAIN 136..217
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT BINDING 7..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12086676"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12086676"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12086676"
FT BINDING 73..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12086676"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:12086676"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:1LSS"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1LSS"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1LSS"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:1LSS"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1LSS"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1LSS"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1LSS"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:1LSS"
SQ SEQUENCE 218 AA; 23996 MW; 28CFD33E8791E0CC CRC64;
MYIIIAGIGR VGYTLAKSLS EKGHDIVLID IDKDICKKAS AEIDALVING DCTKIKTLED
AGIEDADMYI AVTGKEEVNL MSSLLAKSYG INKTIARISE IEYKDVFERL GVDVVVSPEL
IAANYIEKLI ERPGILDLAI VGRGEAEILE FIIPEKAKVV NKKIKELGRP QDYLIIAIYD
GDELKIPSGD TELKSGDRVL VLVKKDAADA IRKMFLEE
