KUP_SHIDS
ID KUP_SHIDS Reviewed; 624 AA.
AC Q329T6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Low affinity potassium transport system protein kup {ECO:0000255|HAMAP-Rule:MF_01522};
DE AltName: Full=Kup system potassium uptake protein {ECO:0000255|HAMAP-Rule:MF_01522};
GN Name=kup {ECO:0000255|HAMAP-Rule:MF_01522}; OrderedLocusNames=SDY_4001;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Responsible for the low-affinity transport of potassium into
CC the cell, with the probable concomitant uptake of protons (symport
CC system). {ECO:0000255|HAMAP-Rule:MF_01522}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01522}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01522}.
CC -!- SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family.
CC {ECO:0000255|HAMAP-Rule:MF_01522}.
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DR EMBL; CP000034; ABB63919.1; -; Genomic_DNA.
DR RefSeq; WP_000102298.1; NC_007606.1.
DR RefSeq; YP_405410.1; NC_007606.1.
DR AlphaFoldDB; Q329T6; -.
DR STRING; 300267.SDY_4001; -.
DR EnsemblBacteria; ABB63919; ABB63919; SDY_4001.
DR KEGG; sdy:SDY_4001; -.
DR PATRIC; fig|300267.13.peg.4713; -.
DR HOGENOM; CLU_008142_4_2_6; -.
DR OMA; AADQFEI; -.
DR Proteomes; UP000002716; 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:0015079; F:potassium ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01522; Kup; 1.
DR InterPro; IPR003855; K+_transporter.
DR InterPro; IPR023051; K+_uptake_low_affin.
DR PANTHER; PTHR30540; PTHR30540; 1.
DR Pfam; PF02705; K_trans; 1.
DR TIGRFAMs; TIGR00794; kup; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..624
FT /note="Low affinity potassium transport system protein kup"
FT /id="PRO_0000279829"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 30..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 124..136
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 158..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 186..212
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 234..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 268..286
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 310..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 358..364
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 386..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 419..420
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 442..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 624 AA; 69573 MW; 5B0DCA3916AEC3C6 CRC64;
MSTDNKQSLP AITLAAIGVV YGDIGTSPLY TLRECLSGQF GFGVERDAVF GFLSLIFWLL
IFVVSIKYLT FVIRADNAGE GGILTLMSLA GRNTSARTTS MLVIMGLIGG SFFYGEVVIT
PAISVMSAIE GLEIVAPQLD TWIVPLSIIV LTLLFMIQKH GTAMVGKLFA PIMLTWFLIL
AGLGLRSIIA NPEVLHALNP MWAVHFFLEY KTVSFIALGA VVLSITGVEA LYADMGHFGK
FPIRLAWFTV VLPSLTLNYF GQGALLLKNP EAIKNPFFLL APDWALIPLL IIAALATVIA
SQAVISGVFL LTRQAVRLGY LSPMRIIHTS EMESGQIYIP FVNWMLYVAV VIVIVIVSFE
HSSNLAAAYG IAVTGTMVLT SILSTTVARQ NWHWNKYFVA LILIAFLCVD IPLFTANLDK
LLSGGWLPLS LGTVMFIVMT TWKSERFRLL RRMHEHGNSL EAMIASLEKS PPVRVPGTEV
YMSRAINVIP FALMHNLKHN KVLHERVILL TLRTEDAPYV HNVRRVQIEQ LSPTFWRVVA
SYGWRETPNV EEVFHRCGLE GLSCRMMETS FFMSHESLIL GKRPWYLRLR GKLYLLLQRN
ALRAPDQFEI PPNRVIELGT QVEI
