KEFB_ECO57
ID KEFB_ECO57 Reviewed; 592 AA.
AC Q8X878;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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};
GN OrderedLocusNames=Z4710, ECs4201;
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT 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(+) 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; AE005174; AAG58458.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37624.1; -; Genomic_DNA.
DR PIR; A91154; A91154.
DR PIR; F85999; F85999.
DR RefSeq; NP_312228.1; NC_002695.1.
DR RefSeq; WP_000399120.1; NZ_SEKU01000003.1.
DR AlphaFoldDB; Q8X878; -.
DR SMR; Q8X878; -.
DR STRING; 155864.EDL933_4554; -.
DR EnsemblBacteria; AAG58458; AAG58458; Z4710.
DR EnsemblBacteria; BAB37624; BAB37624; ECs_4201.
DR GeneID; 915944; -.
DR KEGG; ece:Z4710; -.
DR KEGG; ecs:ECs_4201; -.
DR PATRIC; fig|386585.9.peg.4385; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OMA; IRPFHDV; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 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 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..592
FT /note="Glutathione-regulated potassium-efflux system
FT protein KefB"
FT /id="PRO_0000196598"
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 115..135
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 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01412"
FT TRANSMEM 291..311
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 592 AA; 65305 MW; C2FACCE6C048A5F0 CRC64;
MEGSDFLLAG VLFLFAAVAA VPLASRLGIG AVLGYLLAGI AIGPWGLGFI SDVDEILHFS
ELGVVFLMFI IGLELNPSKL WQLRRSIFGV GAAQVLLSAA LLAGLLMLTD FAWQAAVVGG
IGLAMSSTAM ALQLMREKGM NRSESGQLGF SVLLFQDLAV IPALALVPLL AGSADEHFDW
MKIGMKVLAF VGMLIGGRYL LRPVFRFIAA SGVREVFTAA TLLLVLGSAL FMDALGLSMA
LGTFIAGVLL AESEYRHELE TAIDPFKGLL LGLFFISVGM SLNLGVLYTH LLWVVISVVV
LVAVKILVLY LLARLYGVRS SERMQFAGVL SQGGEFAFVL FSTASSQRLF QGDQMALLLV
TVTLSMMTTP LLMKLVDKWL SRQFNGPEEE DEKPWVNDDK PQVIVVGFGR FGQVIGRLLM
ANKMRITVLE RDISAVNLMR KYGYKVYYGD ATQVDLLRSA GAEAAESIVI TCNEPEDTMK
LVEICQQHFP HLHILARARG RVEAHELLQA GVTQFSRETF SSALELGRKT LVTLGMHPHQ
AQRAQLHFRR LDMRMLRELI PMHADTVQIS RAREARRELE EIFQREMQQE RR
