TRKA_SHIFL
ID TRKA_SHIFL Reviewed; 458 AA.
AC P0AGJ1; P23868; P77041;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Trk system potassium uptake protein TrkA;
DE Short=K(+)-uptake protein TrkA;
GN Name=trkA; OrderedLocusNames=SF3321, S3546;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44784.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18593.1; -; Genomic_DNA.
DR RefSeq; NP_709077.1; NC_004337.2.
DR RefSeq; WP_000691382.1; NZ_WPGW01000137.1.
DR AlphaFoldDB; P0AGJ1; -.
DR SMR; P0AGJ1; -.
DR STRING; 198214.SF3321; -.
DR EnsemblBacteria; AAN44784; AAN44784; SF3321.
DR EnsemblBacteria; AAP18593; AAP18593; S3546.
DR GeneID; 1027048; -.
DR GeneID; 67415330; -.
DR KEGG; sfl:SF3321; -.
DR KEGG; sfx:S3546; -.
DR PATRIC; fig|198214.7.peg.3930; -.
DR HOGENOM; CLU_046525_0_2_6; -.
DR OMA; IACQVAY; -.
DR OrthoDB; 1768241at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..458
FT /note="Trk system potassium uptake protein TrkA"
FT /id="PRO_0000148718"
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
