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KEFC_KLEAE
ID   KEFC_KLEAE              Reviewed;         621 AA.
AC   Q9X756;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 97.
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};
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11053405; DOI=10.1128/jb.182.22.6536-6540.2000;
RA   Miller S., Ness L.S., Wood C.M., Fox B.C., Booth I.R.;
RT   "Identification of an ancillary protein, YabF, required for activity of the
RT   KefC glutathione-gated potassium efflux system in Escherichia coli.";
RL   J. Bacteriol. 182:6536-6540(2000).
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; AJ242913; CAB44437.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X756; -.
DR   SMR; Q9X756; -.
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..621
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   protein KefC"
FT                   /id="PRO_0000196609"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        30..50
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        232..252
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        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT   TRANSMEM        326..346
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          598..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  67353 MW;  94EA20456227327E CRC64;
     MDSHTLIQAL IYLGAAALIV PIASVLGLGS VLGYLIAGCI IGPWALRLVN DAEAILHFAE
     IGVVLMLVAM GLELDPQRLW KLRASVFDGG ALQMVACGVL IGLFCMLLGL RWQVAELIGM
     TLALSSTAIA MQAMNERNLT VSQMGRSAFA VLLFQDIAAI PLVAMIPLLA ASGGATSLMA
     FALSALKVAA ALALVVVLGR YLTRPLLRFV ARSGLREVFS AVACSWSSAL GLLLEEVGLS
     MAMGAFLAGV LLASSEYRHA LENDIEPVKG LLLGLFFIGV GMSIDFAPWS PNPLRIVILL
     VGFPAIKMLM LWLIAQPLGV PRAQHRWFAV LLGQGSEFAF VVFGPARMAD VLDGEWPKAL
     TLAVALSMAT TPILLVLLTR LEKSSSGQAR DADEIDEEQP RVIVAGFGRF GQIAGRLLLS
     SGVKMVILDH DPDHVDTLRK FDMKVFYGDA TRVDLLESAG AEKAEVLINA IDDPHVSLEL
     VARVKEHFPH LQIISRARDV DHYIQLRQAG VEAPERETFE AALKSGRMTL EALGLGAYEA
     RERPDLFRRF NLQMVEEMVA MAENDPRRGV AVFKRTSDML TGIINEDRHH LSLVQRHGWQ
     GTEEGRHTGD IADEPENKPS A
 
 
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