ID   KEFB_SALSV              Reviewed;         601 AA.
AC   B4TXF9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Glutathione-regulated potassium-efflux system protein KefB {ECO:0000255|HAMAP-Rule:MF_01412};
DE   AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01412};
GN   Name=kefB {ECO:0000255|HAMAP-Rule:MF_01412}; OrderedLocusNames=SeSA_A3653;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
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_01412}.
CC   -!- SUBUNIT: Interacts with the regulatory subunit KefG.
CC       {ECO:0000255|HAMAP-Rule:MF_01412}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01412}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01412}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. KefB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01412}.
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DR   EMBL; CP001127; ACF91291.1; -; Genomic_DNA.
DR   RefSeq; WP_000398129.1; NC_011094.1.
DR   AlphaFoldDB; B4TXF9; -.
DR   SMR; B4TXF9; -.
DR   EnsemblBacteria; ACF91291; ACF91291; SeSA_A3653.
DR   KEGG; sew:SeSA_A3653; -.
DR   HOGENOM; CLU_005126_9_3_6; -.
DR   OMA; IRPFHDV; -.
DR   Proteomes; UP000001865; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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   Gene3D; 1.20.1530.20; -; 1.
DR   HAMAP; MF_01412; K_H_efflux_KefB; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR004771; K/H_exchanger.
DR   InterPro; IPR020884; K_H_efflux_KefB.
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   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..601
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   protein KefB"
FT                   /id="PRO_1000145531"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT   DOMAIN          402..524
FT                   /note="RCK N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
SQ   SEQUENCE   601 AA;  66374 MW;  70CC0E18D9D84E84 CRC64;
     MEGADLLTAG VLFLFAAVAA VPLAARLGIG AVLGYLLAGI AIGPWGLGFI SDVDEILHFS
     ELGVVFLMFI IGLELNPSRL WQLRRSIFGV GAAQVLLSAA VLAGLLMLAD FLWQAAVVGG
     IGLAMSSTAM ALQLMREKGM NRSESGQLGF SVLLFQDLAV IPALALVPLL AGSADEHFDW
     FKVAMKVLAF AVMLIGGRYL LRPVFRFIAA SGVREVFTAA TLLLVLSAAL FMDALGLSMA
     LGTFIAGVLL AESEYRHELE NAIDPFKGLL LGLFFISVGM SLNLGVLYTH LLWVAASVVI
     LVAIKMLTLY LLARLYGIRS SERMQFASVL SQGGEFAFVL FSTASSQRLF QGDQMALLLV
     TVTLSMMTTP LLMKGIDKWL SRRLNGPEEN DEKPWVEDDK PQVIVVGFGR FGQVIARLLM
     ANKMRITVLE RDIGAVNLMR KYGYKVYYGD ATQVELLRSA GAEAAESIVI TCNEPEDTMK
     LVALCQQHFP HLHILARARG RVEAHELLQA GVTQFSRETF SSALELGRKT LVSLGMHPHQ
     AQRAQLHFRR LDMRMLRELI PEHSDMVQIS RAREARRELE EIFQREMQQE RRQLDGWDEF
     E