KEFC_SALA4
ID KEFC_SALA4 Reviewed; 620 AA.
AC B5F767;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, 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=SeAg_B0095;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH52204.1; -; Genomic_DNA.
DR RefSeq; WP_000377166.1; NC_011149.1.
DR AlphaFoldDB; B5F767; -.
DR SMR; B5F767; -.
DR EnsemblBacteria; ACH52204; ACH52204; SeAg_B0095.
DR KEGG; sea:SeAg_B0095; -.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; PYLWFAK; -.
DR Proteomes; UP000008819; 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_1000145545"
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 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 67110 MW; CC071DC4F0E5EDC3 CRC64;
MDSHTLLQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
IGVVLMLFVI GLELDPQRLW KLRASVFGGG ALQMVVCGGL IGLFCMFLGL RWQVAELIGM
TLALSSTAIA MQAMNERNLT VSQVGRSAFA VLLFQDIAAI PLVAMIPLLA ASGASTTLGA
FALSALKVAG ALALVVLLGR YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS
MAMGAFLAGV LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLV ENPLRILLLL
AGFLAIKIVM LWLVARPLGV PAKQRRWFAV LLGQGSEFAF VVFGAAQMAD VLEPEWAKAL
TLAVALSMAA TPIFLVLLTR MEKTATGEAR EADEIDEEQP RVIVAGFGRF GQIAGRLLLS
SGVKMVVLDH DPDHIETLRK FGMKVFYGDA TRMDLLESAG AAKAEVLINA IDDPQTNLQL
SELVKTHFPH LQIIARARDV DHYIRLRQAG VAMPERETFE GALKSGRQAL EALGLGRYEA
RERADLFRHF NTRMVEEMAK GENDPLSRAA AYKRTSAMLS EIITEDREHL SLIQRHGWQG
TAEGKHSGEV ADEPEVKPSI
