KUP_SHIFL
ID KUP_SHIFL Reviewed; 622 AA.
AC Q83PJ2; Q7BZA7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Low affinity potassium transport system protein kup;
DE AltName: Full=Kup system potassium uptake protein;
GN Name=kup; OrderedLocusNames=SF3828, S3940;
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: Responsible for the low-affinity transport of potassium into
CC the cell, with the probable concomitant uptake of protons (symport
CC system). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45268.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18929.1; -; Genomic_DNA.
DR RefSeq; NP_709561.1; NC_004337.2.
DR RefSeq; WP_000102309.1; NZ_WPGW01000238.1.
DR AlphaFoldDB; Q83PJ2; -.
DR STRING; 198214.SF3828; -.
DR EnsemblBacteria; AAN45268; AAN45268; SF3828.
DR EnsemblBacteria; AAP18929; AAP18929; S3940.
DR GeneID; 1026053; -.
DR KEGG; sfl:SF3828; -.
DR KEGG; sft:NCTC1_04132; -.
DR KEGG; sfx:S3940; -.
DR PATRIC; fig|198214.7.peg.4516; -.
DR HOGENOM; CLU_008142_4_2_6; -.
DR OMA; AADQFEI; -.
DR OrthoDB; 589903at2; -.
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: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..622
FT /note="Low affinity potassium transport system protein kup"
FT /id="PRO_0000209058"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..133
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..209
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..286
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..362
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..418
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69270 MW; C4ED8956B2DA0037 CRC64;
MSTDNKQSLP AITLAAIGVV YGDIGTSPLY TLRECLSGQF GFGVERDAVF GFLSLIFWLL
IFVVSIKYLT FVMRADNAGE GGILTLMSLA GRNTSARTTS MLVIMGLIGG SFFYGEVVIT
PAISVMSAIE GLEIVAPQLD TWIVPLSIIV LTLLFMIQKH GTAMVGKLFA PIMLTWFLIL
AGLGLRSIIA NPEVLHALNP MWAVHFFLEY KTVSFIALGA VVLSITGGEV LYADMGHFGK
FSIRLAWFTV 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 PTFWRVVASY
GWRETPNVEE VFHRCGLEGL SCRMMETSFF MSHESLILGK RPWYLRLRGK LYLLLQRNAL
RAPDQFEIPP NRVIELGTQV EI
