(data stored in ACNUC7421 zone)

SWISSPROT: KEFC_ECODH

ID   KEFC_ECODH              Reviewed;         620 AA.
AC   B1XC48;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 71.
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=ECDH10B_0048;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Pore-forming subunit of a potassium efflux system that
CC       confers protection against electrophiles. Catalyzes K(+)/H(+)
CC       antiport. {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
CC       (CPA2) transporter (TC 2.A.37) family. KefC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01413}.
DR   EMBL; CP000948; ACB01252.1; -; Genomic_DNA.
DR   RefSeq; WP_000377098.1; NC_010473.1.
DR   ProteinModelPortal; B1XC48; -.
DR   SMR; B1XC48; -.
DR   EnsemblBacteria; ACB01252; ACB01252; ECDH10B_0048.
DR   KEGG; ecd:ECDH10B_0048; -.
DR   eggNOG; ENOG4105CKD; Bacteria.
DR   eggNOG; COG0475; LUCA.
DR   eggNOG; COG1226; LUCA.
DR   HOGENOM; HOG000179076; -.
DR   KO; K11745; -.
DR   OMA; RPIGQTI; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IEA:InterPro.
DR   GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IEA:InterPro.
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   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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
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; B1XC48.
DR   SWISS-2DPAGE; B1XC48.
KW   Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    620       Glutathione-regulated potassium-efflux
FT                                system protein KefC.
FT                                /FTId=PRO_1000145539.
FT   TRANSMEM      4     24       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM     26     46       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM     54     74       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM     90    110       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    114    134       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    149    169       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    178    198       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    218    238       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    270    290       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    294    314       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    327    347       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TRANSMEM    359    379       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   DOMAIN      401    523       RCK N-terminal. {ECO:0000255|HAMAP-
FT                                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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