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Glutathione-regulated potassium-efflux system protein KefC (K( )/H( ) antiporter)

 KEFC_ECOLI              Reviewed;         620 AA.
P03819;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
22-NOV-2017, entry version 170.
RecName: Full=Glutathione-regulated potassium-efflux system protein KefC {ECO:0000255|HAMAP-Rule:MF_01413};
AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01413};
Name=kefC {ECO:0000255|HAMAP-Rule:MF_01413}; Synonyms=trkC;
OrderedLocusNames=b0047, JW0046;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
STRAIN=K12 / CS520;
PubMed=2046548; DOI=10.1111/j.1365-2958.1991.tb00731.x;
Munro A.W., Ritchie G.Y., Lamb A.J., Douglas R.M., Booth I.R.;
"The cloning and DNA sequence of the gene for the glutathione-
regulated potassium-efflux system KefC of Escherichia coli.";
Mol. Microbiol. 5:607-616(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-620.
STRAIN=K12;
PubMed=6159575; DOI=10.1093/nar/8.10.2255;
Smith D.R., Calvo J.M.;
"Nucleotide sequence of the E coli gene coding for dihydrofolate
reductase.";
Nucleic Acids Res. 8:2255-2274(1980).
[6]
SIMILARITY TO NAPA.
PubMed=1325937; DOI=10.1016/0378-1097(92)90601-J;
Reizer J., Reizer A., Saier M.H. Jr.;
"The putative Na+/H+ antiporter (NapA) of Enterococcus hirae is
homologous to the putative K+/H+ antiporter (KefC) of Escherichia
coli.";
FEMS Microbiol. Lett. 73:161-163(1992).
[7]
FUNCTION, AND ENZYME REGULATION.
STRAIN=K12;
PubMed=9023177; DOI=10.1128/jb.179.4.1007-1012.1997;
Ferguson G.P., Nikolaev Y., McLaggan D., Maclean M., Booth I.R.;
"Survival during exposure to the electrophilic reagent N-
ethylmaleimide in Escherichia coli: role of KefB and KefC potassium
channels.";
J. Bacteriol. 179:1007-1012(1997).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[9]
FUNCTION, ENZYME REGULATION, AND SUBUNIT.
PubMed=17679694; DOI=10.1073/pnas.0703709104;
Fujisawa M., Ito M., Krulwich T.A.;
"Three two-component transporters with channel-like properties have
monovalent cation/proton antiport activity.";
Proc. Natl. Acad. Sci. U.S.A. 104:13289-13294(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 401-620 IN COMPLEX WITH KEFF
AND AMP, SUBUNIT, INTERACTION WITH KEFF, MUTAGENESIS OF ASP-264;
ARG-416; GLU-520; ALA-522; GLY-526 AND ASN-551, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=19523906; DOI=10.1016/j.str.2009.03.018;
Roosild T.P., Castronovo S., Miller S., Li C., Rasmussen T.,
Bartlett W., Gunasekera B., Choe S., Booth I.R.;
"KTN (RCK) domains regulate K+ channels and transporters by
controlling the dimer-hinge conformation.";
Structure 17:893-903(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 401-620 IN COMPLEXES WITH
KEFF; AMP AND GLUTATHIONE, FUNCTION, SUBUNIT, INTERACTION WITH KEFF,
ENZYME REGULATION, DOMAIN, AND MUTAGENESIS OF GLN-412; ARG-416;
PHE-441; ASP-499; ARG-516 AND ASN-551.
PubMed=21041667; DOI=10.1073/pnas.1012716107;
Roosild T.P., Castronovo S., Healy J., Miller S., Pliotas C.,
Rasmussen T., Bartlett W., Conway S.J., Booth I.R.;
"Mechanism of ligand-gated potassium efflux in bacterial pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 107:19784-19789(2010).
-!- FUNCTION: Pore-forming subunit of a potassium efflux system that
confers protection against electrophiles. Catalyzes K(+)/H(+)
antiport. Can also export rubidium, lithium and sodium.
{ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:17679694,
ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}.
-!- ENZYME REGULATION: Inhibited by glutathione. This inhibition is
increased by NADH. Activated by adducts between glutathione and
electrophiles. {ECO:0000269|PubMed:17679694,
ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}.
-!- SUBUNIT: Homodimer. Interacts with the regulatory subunit KefF,
forming a heterotetramer with 2:2 stoichiometry. Interaction with
KefF is required for optimal activity. The active antiporter may
be formed by the heterotetramer, or by an octamer.
{ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:17679694,
ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
Rule:MF_01413, ECO:0000269|PubMed:15919996,
ECO:0000269|PubMed:2046548}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996,
ECO:0000269|PubMed:2046548}.
-!- DOMAIN: The cytoplasmic RCK N-terminal domain regulates channel
activity. It binds glutathione, resulting in inhibition of
potassium efflux. In contrast, binding of the adducts formed
between glutathione and electrophiles leads to activation of
potassium efflux. Is expected to bind NADH, but X-ray
crystallography shows bound AMP, and it would be difficult to
accommodate NADH in this binding site (PubMed:21041667).
{ECO:0000269|PubMed:21041667}.
-!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2
(CPA2) transporter (TC 2.A.37) family. KefC subfamily.
{ECO:0000255|HAMAP-Rule:MF_01413}.
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EMBL; X56742; CAA40066.1; -; Genomic_DNA.
EMBL; U00096; AAC73158.1; -; Genomic_DNA.
EMBL; AP009048; BAB96615.1; -; Genomic_DNA.
EMBL; J01609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S40568; QQECRD.
RefSeq; NP_414589.1; NC_000913.3.
RefSeq; WP_000377098.1; NZ_LN832404.1.
PDB; 3EYW; X-ray; 2.40 A; A/B=401-620.
PDB; 3L9W; X-ray; 1.75 A; A/B=401-620.
PDB; 3L9X; X-ray; 2.10 A; A/B=401-620.
PDBsum; 3EYW; -.
PDBsum; 3L9W; -.
PDBsum; 3L9X; -.
ProteinModelPortal; P03819; -.
SMR; P03819; -.
BioGrid; 4262200; 7.
DIP; DIP-10072N; -.
IntAct; P03819; 2.
MINT; MINT-1257196; -.
STRING; 316385.ECDH10B_0048; -.
TCDB; 2.A.37.1.1; the monovalent cation:proton antiporter-2 (cpa2) family.
PaxDb; P03819; -.
PRIDE; P03819; -.
EnsemblBacteria; AAC73158; AAC73158; b0047.
EnsemblBacteria; BAB96615; BAB96615; BAB96615.
GeneID; 944773; -.
KEGG; ecj:JW0046; -.
KEGG; eco:b0047; -.
PATRIC; fig|1411691.4.peg.2236; -.
EchoBASE; EB0516; -.
EcoGene; EG10521; kefC.
eggNOG; ENOG4105CKD; Bacteria.
eggNOG; COG0475; LUCA.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000179076; -.
InParanoid; P03819; -.
KO; K11745; -.
PhylomeDB; P03819; -.
BioCyc; EcoCyc:KEFC-MONOMER; -.
BioCyc; MetaCyc:KEFC-MONOMER; -.
EvolutionaryTrace; P03819; -.
PRO; PR:P03819; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
GO; GO:0016020; C:membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0019899; F:enzyme binding; IMP:EcoCyc.
GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IMP:EcoCyc.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
GO; GO:0015643; F:toxic substance binding; IDA:EcoCyc.
GO; GO:0006813; P:potassium ion transport; IDA:EcoliWiki.
GO; GO:0006885; P:regulation of pH; IDA:EcoliWiki.
GO; GO:0051595; P:response to methylglyoxal; IMP:EcoCyc.
GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
HAMAP; MF_01413; K_H_efflux_KefC; 1.
InterPro; IPR006153; Cation/H_exchanger.
InterPro; IPR004771; K/H_exchanger.
InterPro; IPR023941; K_H_efflux_KefC.
InterPro; IPR006036; K_uptake_TrkA.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR003148; RCK_N.
PANTHER; PTHR16254:SF28; PTHR16254:SF28; 1.
Pfam; PF00999; Na_H_Exchanger; 1.
Pfam; PF02254; TrkA_N; 1.
PRINTS; PR00335; KUPTAKETRKA.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00932; 2a37; 1.
PROSITE; PS51201; RCK_N; 1.
1: Evidence at protein level;
3D-structure; Antiport; Cell inner membrane; Cell membrane;
Complete proteome; Ion transport; Membrane; Nucleotide-binding;
Potassium; Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 620 Glutathione-regulated potassium-efflux
system protein KefC.
/FTId=PRO_0000196606.
TOPO_DOM 1 3 Periplasmic. {ECO:0000255}.
TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 25 25 Cytoplasmic. {ECO:0000255}.
TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 47 53 Periplasmic. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 75 89 Cytoplasmic. {ECO:0000255}.
TRANSMEM 90 110 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 111 113 Periplasmic. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 135 148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 170 177 Periplasmic. {ECO:0000255}.
TRANSMEM 178 198 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 199 213 Cytoplasmic. {ECO:0000255}.
TRANSMEM 214 233 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 234 236 Periplasmic. {ECO:0000255}.
TRANSMEM 237 254 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 255 269 Cytoplasmic. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 291 293 Periplasmic. {ECO:0000255}.
TRANSMEM 294 314 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 315 326 Cytoplasmic. {ECO:0000255}.
TRANSMEM 327 347 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 348 358 Periplasmic. {ECO:0000255}.
TRANSMEM 359 379 Helical. {ECO:0000255|HAMAP-
Rule:MF_01413}.
TOPO_DOM 380 620 Cytoplasmic.
{ECO:0000305|PubMed:15919996}.
DOMAIN 401 523 RCK N-terminal. {ECO:0000255|HAMAP-
Rule:MF_01413}.
NP_BIND 408 410 AMP. {ECO:0000269|PubMed:19523906}.
NP_BIND 429 430 AMP. {ECO:0000269|PubMed:19523906}.
NP_BIND 449 450 AMP. {ECO:0000269|PubMed:19523906}.
REGION 259 267 Important for the regulation of potassium
conductance.
REGION 498 500 Glutathione binding.
BINDING 412 412 Glutathione; shared with dimeric partner.
BINDING 434 434 AMP. {ECO:0000269|PubMed:19523906}.
BINDING 472 472 AMP. {ECO:0000269|PubMed:19523906}.
BINDING 496 496 AMP. {ECO:0000269|PubMed:19523906}.
BINDING 516 516 Glutathione.
MUTAGEN 262 262 E->K: Increases potassium efflux in the
absence of glutathione, but not in the
presence of glutathione. Increases
constitutive potassium efflux; when
associated with D-551.
MUTAGEN 264 264 D->A: Increases constitutive potassium
efflux. {ECO:0000269|PubMed:19523906}.
MUTAGEN 412 412 Q->A: Increases constitutive potassium
efflux and reduces glutathione-mediated
inhibition of potassium efflux.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 412 412 Q->K: Increases constitutive potassium
efflux and abolishes regulation of
potassium efflux by glutathione and
glutathione adducts.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 416 416 R->A: Increases constitutive potassium
efflux and abolishes regulation of
potassium efflux by glutathione and
glutathione adducts; when associated with
A-516 and A-551.
{ECO:0000269|PubMed:19523906,
ECO:0000269|PubMed:21041667}.
MUTAGEN 416 416 R->S: Increased constitutive potassium
efflux. {ECO:0000269|PubMed:19523906,
ECO:0000269|PubMed:21041667}.
MUTAGEN 441 441 F->D,L: Reduced activation of potassium
efflux by glutathione adducts.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 441 441 F->W,Y: No effect on activation of
potassium efflux by glutathione adducts.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 499 499 D->A: Strongly reduced activation of
potassium efflux by glutathione adducts.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 499 499 D->G: Mildly reduced activation of
potassium efflux by glutathione adducts.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 499 499 D->S: No effect on potassium efflux.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 516 516 R->A: Increases constitutive potassium
efflux and abolishes regulation of
potassium efflux by glutathione and
glutathione adducts; when associated with
A-416 and A-551.
{ECO:0000269|PubMed:21041667}.
MUTAGEN 520 520 E->G: Strongly reduced potassium efflux.
{ECO:0000269|PubMed:19523906}.
MUTAGEN 522 522 A->V: Strongly reduced potassium efflux.
{ECO:0000269|PubMed:19523906}.
MUTAGEN 526 526 G->V: Strongly reduced potassium efflux.
{ECO:0000269|PubMed:19523906}.
MUTAGEN 551 551 N->A: Increases constitutive potassium
efflux and abolishes regulation of
potassium efflux by glutathione and
glutathione adducts; when associated with
A-416 and A-516.
{ECO:0000269|PubMed:19523906,
ECO:0000269|PubMed:21041667}.
MUTAGEN 551 551 N->D: Increases constitutive potassium
efflux; when associated with K-262.
{ECO:0000269|PubMed:19523906,
ECO:0000269|PubMed:21041667}.
STRAND 401 405 {ECO:0000244|PDB:3L9W}.
HELIX 409 420 {ECO:0000244|PDB:3L9W}.
STRAND 425 429 {ECO:0000244|PDB:3L9W}.
HELIX 432 440 {ECO:0000244|PDB:3L9W}.
STRAND 446 448 {ECO:0000244|PDB:3L9W}.
HELIX 453 458 {ECO:0000244|PDB:3L9W}.
TURN 459 463 {ECO:0000244|PDB:3L9W}.
STRAND 465 469 {ECO:0000244|PDB:3L9W}.
HELIX 474 487 {ECO:0000244|PDB:3L9W}.
STRAND 492 499 {ECO:0000244|PDB:3L9W}.
HELIX 500 508 {ECO:0000244|PDB:3L9W}.
HELIX 519 532 {ECO:0000244|PDB:3L9W}.
HELIX 537 560 {ECO:0000244|PDB:3L9W}.
HELIX 565 579 {ECO:0000244|PDB:3L9W}.
SEQUENCE 620 AA; 67796 MW; 9995B2E8E3C1DCE3 CRC64;
MDSHTLIQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT DAESILHFAE
IGVVLMLFII GLELDPQRLW KLRAAVFGCG ALQMVICGGL LGLFCMLLGL RWQVAELIGM
TLALSSTAIA MQAMNERNLM VTQMGRSAFA VLLFQDIAAI PLVAMIPLLA TSSASTTMGA
FALSALKVAG ALVLVVLLGR YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS
MAMGAFLAGV LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLL ENPLRIVILL
LGFLIIKIAM LWLIARPLQV PNKQRRWFAV LLGQGSEFAF VVFGAAQMAN VLEPEWAKSL
TLAVALSMAA TPILLVILNR LEQSSTEEAR EADEIDEEQP RVIIAGFGRF GQITGRLLLS
SGVKMVVLDH DPDHIETLRK FGMKVFYGDA TRMDLLESAG AAKAEVLINA IDDPQTNLQL
TEMVKEHFPH LQIIARARDV DHYIRLRQAG VEKPERETFE GALKTGRLAL ESLGLGPYEA
RERADVFRRF NIQMVEEMAM VENDTKARAA VYKRTSAMLS EIITEDREHL SLIQRHGWQG
TEEGKHTGNM ADEPETKPSS


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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