KEFB_SALEP
ID KEFB_SALEP Reviewed; 601 AA.
AC B5R2A8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=SEN3285;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM933172; CAR34860.1; -; Genomic_DNA.
DR RefSeq; WP_000398135.1; NC_011294.1.
DR AlphaFoldDB; B5R2A8; -.
DR SMR; B5R2A8; -.
DR KEGG; set:SEN3285; -.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; IRPFHDV; -.
DR Proteomes; UP000000613; 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_1000145527"
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; 66460 MW; 12194DAD57F45007 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
LVVIKMLTLY LLARLYGIRS SERMQFASVL SQGGEFAFVL FSTASSQRLF QGDQMALLLV
TVTLSMMTTP LLMKGIDKWL SRRLNGPEEN DEKPWVEDDK PQVIVVGFGR FGQVIARLLM
ANKMRITVLE RDIGAVNLMR KYGYKVYYGD ATQVELLRSA GAEAAESIVI TCNEPEDTMK
LVELCQQHFP HLHILARARG RVEAHELLQA GVTQFSRETF SSALELGRKT LVSLGMHPHQ
AQRAQLHFRR LDMRMLRELI PEHSDMVQIS RAREARRELE EIFQREMQQE RRQLDGWDEF
E
