KEFB_ECOLI
ID KEFB_ECOLI Reviewed; 601 AA.
AC P45522; Q2M716;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
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};
DE AltName: Full=NEM-activable K(+)/H(+) antiporter;
GN Name=kefB {ECO:0000255|HAMAP-Rule:MF_01412}; Synonyms=trkB;
GN OrderedLocusNames=b3350, JW3313;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION.
RX PubMed=3301813; DOI=10.1128/jb.169.8.3743-3749.1987;
RA Bakker E.P., Booth I.R., Dinnbier U., Epstein W., Gajewska A.;
RT "Evidence for multiple K+ export systems in Escherichia coli.";
RL J. Bacteriol. 169:3743-3749(1987).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=9023177; DOI=10.1128/jb.179.4.1007-1012.1997;
RA Ferguson G.P., Nikolaev Y., McLaggan D., Maclean M., Booth I.R.;
RT "Survival during exposure to the electrophilic reagent N-ethylmaleimide in
RT Escherichia coli: role of KefB and KefC potassium channels.";
RL J. Bacteriol. 179:1007-1012(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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, ECO:0000269|PubMed:3301813,
CC ECO:0000269|PubMed:9023177}.
CC -!- ACTIVITY REGULATION: Activated by adducts between glutathione and
CC electrophiles. {ECO:0000269|PubMed:9023177}.
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, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01412, ECO:0000269|PubMed:15919996}.
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; U18997; AAA58147.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76375.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77940.1; -; Genomic_DNA.
DR PIR; A65129; A65129.
DR RefSeq; NP_417809.1; NC_000913.3.
DR RefSeq; WP_000399147.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P45522; -.
DR SMR; P45522; -.
DR BioGRID; 4262061; 18.
DR ComplexPortal; CPX-3090; Glutathione-regulated potassium-efflux system KefB-KefG complex.
DR STRING; 511145.b3350; -.
DR TCDB; 2.A.37.1.2; the monovalent cation:proton antiporter-2 (cpa2) family.
DR PaxDb; P45522; -.
DR PRIDE; P45522; -.
DR EnsemblBacteria; AAC76375; AAC76375; b3350.
DR EnsemblBacteria; BAE77940; BAE77940; BAE77940.
DR GeneID; 947858; -.
DR KEGG; ecj:JW3313; -.
DR KEGG; eco:b3350; -.
DR PATRIC; fig|1411691.4.peg.3380; -.
DR EchoBASE; EB4144; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR InParanoid; P45522; -.
DR OMA; IRPFHDV; -.
DR PhylomeDB; P45522; -.
DR BioCyc; EcoCyc:KEFB-MON; -.
DR BioCyc; MetaCyc:KEFB-MON; -.
DR PRO; PR:P45522; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IC:ComplexPortal.
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:0006813; P:potassium ion transport; IGI:EcoliWiki.
DR GO; GO:0051453; P:regulation of intracellular pH; IC:ComplexPortal.
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..601
FT /note="Glutathione-regulated potassium-efflux system
FT protein KefB"
FT /id="PRO_0000196596"
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 601 AA; 66411 MW; B7534C7F4541497E CRC64;
MEGSDFLLAG VLFLFAAVAA VPLASRLGIG AVLGYLLAGI AIGPWGLGFI SDVDEILHFS
ELGVVFLMFI IGLELNPSKL WQLRRSIFGV GAAQVLLSAA LLAGLLMLTD FAWQAAVVGG
IGLAMSSTAM ALQLMREKGM NRSESGQLGF SVLLFQDLAV IPALALVPLL AGSADEHFDW
MKVGMKVLAF 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 RRQLDGWDEF
E
