KEFC_ECO45
ID KEFC_ECO45 Reviewed; 620 AA.
AC B7MAH0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=ECS88_0050;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
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; CU928161; CAR01416.1; -; Genomic_DNA.
DR RefSeq; WP_000377122.1; NC_011742.1.
DR AlphaFoldDB; B7MAH0; -.
DR SMR; B7MAH0; -.
DR EnsemblBacteria; CAR01416; CAR01416; ECS88_0050.
DR KEGG; ecz:ECS88_0050; -.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; PYLWFAK; -.
DR Proteomes; UP000000747; 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_1000145535"
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; 67720 MW; AA8E359F5E74FD9A 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 GMSIDFGTLI 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
