KUP_SHIBS
ID KUP_SHIBS Reviewed; 622 AA.
AC Q31UM6;
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=SBO_3761;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
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; CP000036; ABB68232.1; -; Genomic_DNA.
DR RefSeq; WP_000102317.1; NC_007613.1.
DR AlphaFoldDB; Q31UM6; -.
DR EnsemblBacteria; ABB68232; ABB68232; SBO_3761.
DR KEGG; sbo:SBO_3761; -.
DR HOGENOM; CLU_008142_4_2_6; -.
DR OMA; AADQFEI; -.
DR Proteomes; UP000007067; 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; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..622
FT /note="Low affinity potassium transport system protein kup"
FT /id="PRO_0000279828"
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..362
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 384..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 417..418
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TOPO_DOM 440..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69310 MW; F402390763864CF9 CRC64;
MSTDNKQSLP AITLAAIGVV YGDIGTSPLY TLRECLSGQF GFGVERDAVF GFLSLIFWLL
IFVVSIKYLT FVMRADNAGE GGILTLMSLA GRNTSARTTS MLVIMGLIGG SFFYGEVVIT
PAISVMSAIE GLEIVAPQLD TWIVPLSIIV LTLLFMIQKH GTAMVGKLFA PIMLTWFLIL
AGLGLRSIIA NPEVLHALNP MWAVHFFLEY KTVSFIALGA VVLSITGVEA LYADMGHFGK
FPIRLAWFTV VLPSLTLNYF GQGALLLKNP EAIKNPFFLL APDWALIPLL IIAALATVIA
SQAVISGVFS LTRQAVRLGY LSPMRIIHTS EMESGQIYIP FVNWMLYVAV VIVIVSFEHS
SNLAAAYGIA VTGTMVLTSI LSTTVARQNW HWNKYFVALI LIAFLCVDIP LFTANLDKLL
SGGWLPLSLG TVMFIVMTTW KSERFRLLRR MHEHGNSLEA MIASLEKSPP VRVPGTAVYM
SRAINVIPFA LMHNLKHNKV LHERVILLTL RTEDAPYVHN VRRVQIEQLS LTFWRVVASY
GWRETPNVEE VFHRCGLEGL SCRMMETSFF MSHESLILGK RPWYLRLRGK LYLLLQRNAL
RAPDQFEIPP NRVIELGTQV EI
