KEFC_ECOL6
ID KEFC_ECOL6 Reviewed; 620 AA.
AC Q8FLA1;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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}; OrderedLocusNames=c0057;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN78553.1; -; Genomic_DNA.
DR RefSeq; WP_000377123.1; NC_004431.1.
DR AlphaFoldDB; Q8FLA1; -.
DR SMR; Q8FLA1; -.
DR STRING; 199310.c0057; -.
DR DNASU; 1035128; -.
DR EnsemblBacteria; AAN78553; AAN78553; c0057.
DR KEGG; ecc:c0057; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; PYLWFAK; -.
DR BioCyc; ECOL199310:C0057-MON; -.
DR Proteomes; UP000001410; 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_0000196607"
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 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 67720 MW; A918D19CEF20FF2B CRC64;
MDSHTLIQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
IGVVLMLFII GLELDPQRLW KLRAAVFGGG ALQMVICGGL LGLFCMLLGL RWQVAELIGM
TLALSSTAIA MQAMNERNLM VTQMGRSAFA VLLFQDIAAI PLVAMIPLLA ASSASTTMGA
FVLSALKVAG ALALVVLLGR YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS
MAMGAFLAGV LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLL ENPLRIVILL
LGFLIIKIAM LWLIARPLQV PNKQRRWFAV LLGQGSEFAF VVFGAAQMAN VLEPEWAKSL
TLAVALSMAA TPILLVILNR LEQSSTEEAR EADEIDEEQP RVIIAGFGRF GQITGRLLLS
SGVKMVVLDH DPDHIETLRK FGMKVFYGDA TRMDLLESAG AAKAEVLINA IDDPQTNLQL
TEMVKEHFPH LQIIARARDV DHYIRLRQAG VEKPERETFE GALKTGRLAL ESLGLGPYEA
RERADVFRRF NIQMVEEMAM VENDTKARAA VYKRTSAMLS EIITEDREHL SLIQRHGWQG
TEEGKHTGNM ADEPETKPSS
