TRKA_SALTY
ID TRKA_SALTY Reviewed; 458 AA.
AC P0A2J9; P39445;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Trk system potassium uptake protein TrkA;
DE Short=K(+)-uptake protein TrkA;
GN Name=trkA; Synonyms=sapG; OrderedLocusNames=STM3409;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8076592; DOI=10.1002/j.1460-2075.1994.tb06712.x;
RA Parra-Lopez C., Lin R., Aspedon A., Groisman E.A.;
RT "A Salmonella protein that is required for resistance to antimicrobial
RT peptides and transport of potassium.";
RL EMBO J. 13:3964-3972(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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. In Salmonella it is required for resistance
CC to antimicrobial peptides.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Peripherally bound to the inner side of the
CC 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}.
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; X80501; CAA56663.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22272.1; -; Genomic_DNA.
DR PIR; S48001; S48001.
DR RefSeq; NP_462313.1; NC_003197.2.
DR RefSeq; WP_000691374.1; NC_003197.2.
DR AlphaFoldDB; P0A2J9; -.
DR SMR; P0A2J9; -.
DR STRING; 99287.STM3409; -.
DR PaxDb; P0A2J9; -.
DR EnsemblBacteria; AAL22272; AAL22272; STM3409.
DR GeneID; 1254932; -.
DR GeneID; 66757744; -.
DR KEGG; stm:STM3409; -.
DR PATRIC; fig|99287.12.peg.3607; -.
DR HOGENOM; CLU_046525_0_2_6; -.
DR OMA; IACQVAY; -.
DR PhylomeDB; P0A2J9; -.
DR BioCyc; SENT99287:STM3409-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
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 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..458
FT /note="Trk system potassium uptake protein TrkA"
FT /id="PRO_0000148717"
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; 50369 MW; 75127E09DAE8EB3E CRC64;
MKIIILGAGQ VGGTLAENLV GENNDITVVD TNGERLRSLQ DKFDLRVVQG HGSHPRVLRE
AGADDADMLV AVTSSDETNM VACQVAYSLF NTPNRIARIR SPDYVRDADK LFHSEAVPID
HLIAPEQLVI DNIYRLIEYP GALQVVNFAE GKVSLAVVKA YYGGPLIGNA LSTMREHMPH
IDTRVAAIFR HDRPIRPQGS TIVEAGDEVF FIAASQHIRA VMSELQRLEK PYKRIMLVGG
GNIGAGLARR LEKDYSVKLI ERDQQRAAEL AEKLQNTIVF FGDASDQELL AEEHIDQVDL
FIAVTNDDEA NIMSAMLAKR MGAKKVMVLI QRRAYVDLVQ GSVIDIAISP QQATISALLS
HVRKADIVGV SSLRRGVAEA IEAVAHGDES TSRVVGRVID EIKLPPGTII GAVVRGNDVM
IANDNLRIEQ GDHVIMFLTD KKFITDVERL FQPSPFFL
