(data stored in SCRATCH3701 zone)

SWISSPROT: KEFC_ECOBW

ID   KEFC_ECOBW              Reviewed;         620 AA.
AC   C4ZPX3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 68.
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=BWG_0045;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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}.
DR   EMBL; CP001396; ACR64087.1; -; Genomic_DNA.
DR   RefSeq; WP_000377098.1; NC_012759.1.
DR   SMR; C4ZPX3; -.
DR   EnsemblBacteria; ACR64087; ACR64087; BWG_0045.
DR   KEGG; ebw:BWG_0045; -.
DR   HOGENOM; HOG000179076; -.
DR   KO; K11745; -.
DR   OMA; DVIFVRI; -.
DR   BioCyc; ECOL595496:BWG_RS00245-MONOMER; -.
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;
DR   PRODOM; C4ZPX3.
DR   SWISS-2DPAGE; C4ZPX3.
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_1000215224"
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"
SQ   SEQUENCE   620 AA;  67796 MW;  9995B2E8E3C1DCE3 CRC64;
     MDSHTLIQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
     IGVVLMLFII GLELDPQRLW KLRAAVFGCG ALQMVICGGL LGLFCMLLGL RWQVAELIGM
     TLALSSTAIA MQAMNERNLM VTQMGRSAFA VLLFQDIAAI PLVAMIPLLA TSSASTTMGA
     FALSALKVAG ALVLVVLLGR 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
//

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