TRKA_HALED
ID TRKA_HALED Reviewed; 457 AA.
AC E1V6C6; Q6T3V8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Trk system potassium uptake protein TrkA;
DE Short=K(+)-uptake protein TrkA;
GN Name=trkA; OrderedLocusNames=HELO_1372;
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND GENE
RP NAME.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=15659681; DOI=10.1128/jb.187.3.1036-1043.2005;
RA Kraegeloh A., Amendt B., Kunte H.J.;
RT "Potassium transport in a halophilic member of the bacteria domain:
RT identification and characterization of the K+ uptake systems TrkH and TrkI
RT from Halomonas elongata DSM 2581T.";
RL J. Bacteriol. 187:1036-1043(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
CC -!- FUNCTION: Part of a potassium transport system. Required for the
CC activity of the TrkH and TrkI transport systems.
CC {ECO:0000269|PubMed:15659681}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {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}.
CC -!- DISRUPTION PHENOTYPE: Deletion abolishes any K(+) uptake activity via
CC TkrH and TkrI. {ECO:0000269|PubMed:15659681}.
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DR EMBL; AY437838; AAR91791.1; -; Genomic_DNA.
DR EMBL; FN869568; CBV41255.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V6C6; -.
DR SMR; E1V6C6; -.
DR STRING; 768066.HELO_1372; -.
DR EnsemblBacteria; CBV41255; CBV41255; HELO_1372.
DR KEGG; hel:HELO_1372; -.
DR eggNOG; COG0569; Bacteria.
DR HOGENOM; CLU_046525_0_2_6; -.
DR OMA; IACQVAY; -.
DR Proteomes; UP000008707; 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; Reference proteome; Repeat; Transport.
FT CHAIN 1..457
FT /note="Trk system potassium uptake protein TrkA"
FT /id="PRO_0000430040"
FT DOMAIN 2..130
FT /note="RCK N-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT DOMAIN 142..226
FT /note="RCK C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00544"
FT DOMAIN 233..353
FT /note="RCK N-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT DOMAIN 367..452
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 233..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 50420 MW; 6214AAE0CB462C5B CRC64;
MKIIILGAGQ VGGTLAEHLA REENDITVVD TDADRLRELH TRLDIRTVAG AGSYPMVLRQ
AGCEDADMLI AVTNTDEVNM IACQVAHTLF RTPTKIARVR ATAYLTRKGL FAHEAVPIDV
LISPEQVVTD HIRRLIEHPG ALQVLEFTGG LVQLVAVKAY YGGPLVGQEL GFLRRHMPSV
DTRVAAIYRR NRPIIPRGDT VIEADDEVFF IAARRDIRAV MSELRRLERD FRRVVIVGGG
NIGERLAEHL EHSHQVKIVE HNLERCTQLS ERLDRTVVLH GSATSKRLLE EENIEDCDIF
CALTNDDEVN IMSSMLAKRM GAKKVLTLIN NAAYVDLVQG GEIDIAISPQ QATIGSLLTH
VRRGDIVNVH SLRRGAAEAI EAIAHGDTQS SKVVGRAIGD IDLPSGTTIG AVVRGKEVLI
AHDDVVVESG DHVILFVIDK RRIRDVERLF QVGLTFF
