KUP_STRPG
ID KUP_STRPG Reviewed; 666 AA.
AC A2RDW5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Probable potassium transport system protein kup {ECO:0000255|HAMAP-Rule:MF_01522};
GN Name=kup {ECO:0000255|HAMAP-Rule:MF_01522}; OrderedLocusNames=SpyM50707;
OS Streptococcus pyogenes serotype M5 (strain Manfredo).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=160491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Manfredo;
RX PubMed=17012393; DOI=10.1128/jb.01227-06;
RA Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT "Complete genome of acute rheumatic fever-associated serotype M5
RT Streptococcus pyogenes strain Manfredo.";
RL J. Bacteriol. 189:1473-1477(2007).
CC -!- FUNCTION: Transport of potassium into the cell. {ECO:0000255|HAMAP-
CC Rule:MF_01522}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01522};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; AM295007; CAM30040.1; -; Genomic_DNA.
DR RefSeq; WP_011888791.1; NC_009332.1.
DR AlphaFoldDB; A2RDW5; -.
DR KEGG; spf:SpyM50707; -.
DR HOGENOM; CLU_008142_4_1_9; -.
DR OMA; AADQFEI; -.
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 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.
PE 3: Inferred from homology;
KW Cell membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..666
FT /note="Probable potassium transport system protein kup"
FT /id="PRO_0000296769"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01522"
SQ SEQUENCE 666 AA; 74836 MW; 270DA2D0B12B8521 CRC64;
MSDSHLTAFD KASKAGFIIA LGIVYGDIGT SPLYTMQSLV ENQGGVNQVS ESFILGSISL
IIWTLTLITT IKYVLIALKA DNHHEGGIFS LFTLVRKMSP WLIIPAMIGG ATLLSDGALT
PAVTVTSAIE GLKAVPGLSH IYQNQTNVII TTLVILIVLF GIQRFGTGFI GKIFGPVMFI
WFSFLGVSGF FNTLGHLEIF KAINPYYALH LLFSPENHRG IFILGSIFLA TTGAEALYSD
LGHVGRGNIY VSWPFVKMCI VLSYCGQAAW ILANKHSGIE LNPFFASVPS QLTVYVVILA
TLAAIIASQA LISGSFTLVS EAMRLKIFPL FRVTYPGANL GQLYIPVINW ILFAVTSCTV
LYFRTSAHME AAYGLAITIT MLMTTILLNY YLIKEGVKPF LAHLVMTFFA LVEFIFFWAS
AVKFMHGGYV VVILALAIVF VMFIWHAGTR IVFKYVKSLN LNDYKEQIKQ LRDDVCFDLY
QTNVVYLSNR MQDYMIDRSI LYSILDKRPK RARVYWFVNV QVTDEPYTAK YKVDMMGTDY
MVRVNLYLGF RMPQTVPRYL RTIVQDLMES GRLPKQEQEY TITPGRDVGD FRFVLIEERV
SNARQLSNFE RFIMQTKASI KHVTASPMRW FGLQYSEVTL EVVPLILSDV LKLPIKELVP
VEDSEA