(data stored in ACNUC7421 zone)

SWISSPROT: KEFC_ECO57

ID   KEFC_ECO57              Reviewed;         620 AA.
AC   Q8XA20;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 109.
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=Z0053, ECs0050;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54350.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33473.1; -; Genomic_DNA.
DR   PIR; B85486; B85486.
DR   PIR; B90635; B90635.
DR   RefSeq; NP_308077.1; NC_002695.1.
DR   RefSeq; WP_000377184.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q8XA20; -.
DR   SMR; Q8XA20; -.
DR   STRING; 155864.Z0053; -.
DR   EnsemblBacteria; AAG54350; AAG54350; Z0053.
DR   EnsemblBacteria; BAB33473; BAB33473; BAB33473.
DR   GeneID; 913449; -.
DR   KEGG; ece:Z0053; -.
DR   KEGG; ecs:ECs0050; -.
DR   PATRIC; fig|386585.9.peg.149; -.
DR   eggNOG; ENOG4105CKD; Bacteria.
DR   eggNOG; COG0475; LUCA.
DR   eggNOG; COG1226; LUCA.
DR   HOGENOM; HOG000179076; -.
DR   KO; K11745; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; Q8XA20.
DR   SWISS-2DPAGE; Q8XA20.
KW   Antiport; Cell inner membrane; Cell membrane; Complete proteome;
KW   Ion transport; Membrane; Potassium; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    620       Glutathione-regulated potassium-efflux
FT                                system protein KefC.
FT                                /FTId=PRO_0000196608.
FT   TOPO_DOM      1      3       Periplasmic. {ECO:0000255}.
FT   TRANSMEM      4     24       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM     25     25       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     26     46       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM     47     53       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     54     74       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM     75     89       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     90    110       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    111    113       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    114    134       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    135    148       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    149    169       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    170    177       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    178    198       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    199    213       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    214    233       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    234    236       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    237    254       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    255    269       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    270    290       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    291    293       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    294    314       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    315    326       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    327    347       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    348    358       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    359    379       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
FT   TOPO_DOM    380    620       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      401    523       RCK N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01413}.
SQ   SEQUENCE   620 AA;  67653 MW;  D49FA7D368D277B9 CRC64;
     MDSHTLVQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
     IGVVLMLFII GLELDPQRLW KLRAAVFGGG ALQMVICGGL LGLFCMLLGL RWQVAELIGM
     TLALSSTAIA MQAMNERNLM VTQMGRSAFA VLLFQDIAAI PLVAMIPLLA ASSASTTMGA
     FALSALKVAG ALVLVVLLGR 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 DHYICLRQAG VEKPERETFE GALKTGRLAL ESLGLGPYEA
     RERADVFRRF NIQMVEEMAM VENDTKARAA VYKRTSAMLS EIITEDREHL SLIQRHGWQG
     TEEGKHTGNM ADEPETKPSS
//

If you have problems or comments...

PBIL Back to PBIL home page