TRKH_SHIFL
ID TRKH_SHIFL Reviewed; 483 AA.
AC P0AFZ9; P21166; P76769;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Trk system potassium uptake protein TrkH;
GN Name=trkH; OrderedLocusNames=SF3925, S3827;
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: Low-affinity potassium transport system. Interacts with Trk
CC system potassium uptake protein TrkA and requires TrkE for transport
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45360.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18838.1; -; Genomic_DNA.
DR RefSeq; NP_709653.1; NC_004337.2.
DR RefSeq; WP_000545677.1; NZ_WPGW01000036.1.
DR AlphaFoldDB; P0AFZ9; -.
DR SMR; P0AFZ9; -.
DR STRING; 198214.SF3925; -.
DR PRIDE; P0AFZ9; -.
DR EnsemblBacteria; AAN45360; AAN45360; SF3925.
DR EnsemblBacteria; AAP18838; AAP18838; S3827.
DR GeneID; 1023595; -.
DR GeneID; 66672245; -.
DR KEGG; sfl:SF3925; -.
DR KEGG; sfx:S3827; -.
DR PATRIC; fig|198214.7.peg.4625; -.
DR HOGENOM; CLU_030708_0_2_6; -.
DR OMA; LQWMGGM; -.
DR OrthoDB; 756220at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004772; TrkH.
DR Pfam; PF02386; TrkH; 1.
DR PIRSF; PIRSF006247; TrkH; 1.
DR TIGRFAMs; TIGR00933; 2a38; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion channel; Ion transport; Membrane;
KW Metal-binding; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..483
FT /note="Trk system potassium uptake protein TrkH"
FT /id="PRO_0000070479"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 3..29
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 30..35
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 58..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 66..90
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..?
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM ?..97
FT /evidence="ECO:0000250"
FT INTRAMEM 98..109
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 110..115
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..124
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 125..150
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..202
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 203..205
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 206
FT /evidence="ECO:0000250"
FT INTRAMEM 207..218
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 219..224
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..234
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 235..250
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 251..?
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 295..?
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM ?..300
FT /evidence="ECO:0000250"
FT INTRAMEM 301..316
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 317..322
FT /evidence="ECO:0000250"
FT TOPO_DOM 323..330
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 331..342
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 343..355
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 356..?
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 390..417
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 418..419
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 420..421
FT /evidence="ECO:0000250"
FT INTRAMEM 422..432
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 433..439
FT /evidence="ECO:0000250"
FT TOPO_DOM 440..451
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 452..463
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 464..?
FT /evidence="ECO:0000250"
FT TOPO_DOM ?..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 110..115
FT /note="Selectivity filter part 1"
FT /evidence="ECO:0000250"
FT REGION 219..224
FT /note="Selectivity filter part 2"
FT /evidence="ECO:0000250"
FT REGION 317..322
FT /note="Selectivity filter part 3"
FT /evidence="ECO:0000250"
FT REGION 434..439
FT /note="Selectivity filter part 4"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 112
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 220
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 318
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 319
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 435
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
FT BINDING 436
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q87TN7"
SQ SEQUENCE 483 AA; 52960 MW; 1AA9CC2F83EB509A CRC64;
MHFRAITRIV GLLVILFSGT MIIPGLVALI YRDGAGRAFT QTFFVALAIG SMLWWPNRKE
KGELKSREGF LIVVLFWTVL GSVGALPFIF SESPNLTITD AFFESFSGLT TTGATTLVGL
DSLPHAILFY RQMLQWFGGM GIIVLAVAIL PILGVGGMQL YRAEMPGPLK DNKMRPRIAE
TAKTLWLIYV LLTVACALAL WFAGMDAFDA IGHSFATIAI GGFSTHDASI GYFDSPTINT
IIAIFLLISG CNYGLHFSLL SGRSLKVYWR DPEFRMFIGV QFTLVVICTL VLWFHNVYSS
ALMTINQAFF QVVSMATTAG FTTDSIARWP LFLPVLLLCS AFIGGCAGST GGGLKVIRIL
LLFKQGNREL KRLVHPNAVY SIKLGNRALP ERILEAVWGF FSAYALVFIV SMLAIIATGV
DDFSAFASVV ATLNNLGPGL GVVADNFTSM NPVAKWILIA NMLFGRLEVF TLLVLFTPTF
WRE
