KEFC_SALTI
ID KEFC_SALTI Reviewed; 620 AA.
AC Q8Z9K0;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Glutathione-regulated potassium-efflux system protein KefC {ECO:0000255|HAMAP-Rule:MF_01413};
DE AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01413};
GN Name=kefC {ECO:0000255|HAMAP-Rule:MF_01413};
GN OrderedLocusNames=STY0101, t0089;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Pore-forming subunit of a potassium efflux system that
CC confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
CC {ECO:0000255|HAMAP-Rule:MF_01413}.
CC -!- SUBUNIT: Homodimer. Interacts with the regulatory subunit KefF.
CC {ECO:0000255|HAMAP-Rule:MF_01413}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01413}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01413}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. KefC subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01413}.
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DR EMBL; AL513382; CAD01242.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67822.1; -; Genomic_DNA.
DR RefSeq; NP_454698.1; NC_003198.1.
DR RefSeq; WP_000377172.1; NZ_WSUR01000028.1.
DR AlphaFoldDB; Q8Z9K0; -.
DR SMR; Q8Z9K0; -.
DR STRING; 220341.16501371; -.
DR EnsemblBacteria; AAO67822; AAO67822; t0089.
DR KEGG; stt:t0089; -.
DR KEGG; sty:STY0101; -.
DR PATRIC; fig|220341.7.peg.100; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; PYLWFAK; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:InterPro.
DR GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; IEA:InterPro.
DR GO; GO:0051595; P:response to methylglyoxal; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR HAMAP; MF_01413; K_H_efflux_KefC; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR023941; K_H_efflux_KefC.
DR InterPro; IPR006036; K_uptake_TrkA.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR PANTHER; PTHR46157:SF3; PTHR46157:SF3; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR PRINTS; PR00335; KUPTAKETRKA.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00932; 2a37; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..620
FT /note="Glutathione-regulated potassium-efflux system
FT protein KefC"
FT /id="PRO_0000196611"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 47..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 75..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 111..113
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 135..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 170..177
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 199..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 234..236
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 255..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 291..293
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 315..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 348..358
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 380..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 401..523
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 67032 MW; B4AAAD52999D5806 CRC64;
MDSHTLLQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
IGVVLMLFVI GLELDPQRLW KLRASVFGGG ALQMVVCGGL IGLFCMFLGL RWQVAELIGM
TLALSSTAIA MQAMNERNLT VSQVGRSAFA VLLFQDIAAI PLVAMIPLLA ASGASTTLGA
FALSALKVAG ALALVVLLGR YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS
MAMGAFLAGV LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLV ENPLRILLLL
AGFLAIKIVM LWLVARTLGV PAKQRRWFAV LLGQGSEFAF VVFGAAQMAD VLEPEWAKAL
TLAVALSMAA TPIFLVLLTR MEKTATGEAR EADEIDEEQP RVIVAGFGRF GQIAGRLLLS
SGVKMVVLDH DPDHIETLRK FGMKVFYGDA TRMDLLESAG AAKAEVLINA IDDPQTNLQL
SELVKTHFPH LQIIARARDV DHYIRLRQAG VAMPERETFE GALKSGRQAL EALGLGRYEA
RERADLFCHF NTRMVEEMAK GENDPLSRAA AYKRTSAMLS EIITEDREHL SLIQRHGWQG
TAEGKHSGKA ADEPEVKPSI
