ID   KEFC_ESCF3              Reviewed;         620 AA.
AC   B7LVT8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=EFER_0055;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ87641.1; -; Genomic_DNA.
DR   RefSeq; WP_000377102.1; NC_011740.1.
DR   AlphaFoldDB; B7LVT8; -.
DR   SMR; B7LVT8; -.
DR   EnsemblBacteria; CAQ87641; CAQ87641; EFER_0055.
DR   GeneID; 60903259; -.
DR   KEGG; efe:EFER_0055; -.
DR   HOGENOM; CLU_005126_9_3_6; -.
DR   OMA; PYLWFAK; -.
DR   OrthoDB; 941006at2; -.
DR   BioCyc; EFER585054:EFER_RS00525-MON; -.
DR   Proteomes; UP000000745; 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_1000145543"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
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;  67737 MW;  89C8D8CE394B28F9 CRC64;
     MDSHTLIQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
     IGVVLMLFII GLELDPQRLW KLRAAVFGGG ALQMVICGGL LGLFCMFLGL RWQVAELIGM
     TLALSSTAIA MQAMNERNLM VTQMGRSAFA VLLFQDIAAI PLVAMIPLLA ASSASTTMGA
     FALSALKVAG ALVLVVLLGR YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS
     MAMGAFLAGV LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLL ENPLRIVILL
     LGFLIIKIAM LWLIARPLQV PNKQRRWFAV LLGQGSEFAF VVFGAAQMAN VLEPEWAKSL
     TLAVALSMAA TPILLVILNR LEQSSTEQAR EADEIDEEQP RVIIAGFGRY GQITGRLLLS
     SGVKMVVLDH DPDHIETLRK FGMKVFYGDA TRMDLLESAG AAKAEVLINA IDDPQTNLQL
     TEMVKEHFPH LQIIARARDV DHYIRLRQAG VEKPERETFE GALKTGRLAL ESLGLGPYEA
     RERADVFRRF NIQMVEEMAV VENDTKARAA VYKRTSAMLS EIITEDREHL SLIQRHGWQG
     TEEGKHTGNM ADEPETKPSS