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Protein

Glutathione-regulated potassium-efflux system protein KefC

Gene

kefC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K+/H+ antiport. Can also export rubidium, lithium and sodium.UniRule annotation3 Publications

Enzyme regulationi

Inhibited by glutathione. This inhibition is increased by NADH. Activated by adducts between glutathione and electrophiles.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei412Glutathione; shared with dimeric partner1
Binding sitei434AMP1 Publication1
Binding sitei472AMP1 Publication1
Binding sitei496AMP1 Publication1
Binding sitei516Glutathione1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi408 – 410AMP1 Publication3
Nucleotide bindingi429 – 430AMP1 Publication2
Nucleotide bindingi449 – 450AMP1 Publication2

GO - Molecular functioni

  • enzyme binding Source: EcoCyc
  • glutathione-regulated potassium exporter activity Source: EcoCyc
  • nucleotide binding Source: UniProtKB-KW
  • solute:proton antiporter activity Source: InterPro
  • toxic substance binding Source: EcoCyc

GO - Biological processi

  • potassium ion transport Source: EcoliWiki
  • regulation of pH Source: EcoliWiki
  • response to methylglyoxal Source: EcoCyc
  • response to toxic substance Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Potassium transport, Transport

Keywords - Ligandi

Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:KEFC-MONOMER.
ECOL316407:JW0046-MONOMER.
MetaCyc:KEFC-MONOMER.

Protein family/group databases

TCDBi2.A.37.1.1. the monovalent cation:proton antiporter-2 (cpa2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione-regulated potassium-efflux system protein KefCUniRule annotation
Alternative name(s):
K(+)/H(+) antiporterUniRule annotation
Gene namesi
Name:kefCUniRule annotation
Synonyms:trkC
Ordered Locus Names:b0047, JW0046
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10521. kefC.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 3PeriplasmicSequence analysis3
Transmembranei4 – 24HelicalUniRule annotationAdd BLAST21
Topological domaini25CytoplasmicSequence analysis1
Transmembranei26 – 46HelicalUniRule annotationAdd BLAST21
Topological domaini47 – 53PeriplasmicSequence analysis7
Transmembranei54 – 74HelicalUniRule annotationAdd BLAST21
Topological domaini75 – 89CytoplasmicSequence analysisAdd BLAST15
Transmembranei90 – 110HelicalUniRule annotationAdd BLAST21
Topological domaini111 – 113PeriplasmicSequence analysis3
Transmembranei114 – 134HelicalUniRule annotationAdd BLAST21
Topological domaini135 – 148CytoplasmicSequence analysisAdd BLAST14
Transmembranei149 – 169HelicalUniRule annotationAdd BLAST21
Topological domaini170 – 177PeriplasmicSequence analysis8
Transmembranei178 – 198HelicalUniRule annotationAdd BLAST21
Topological domaini199 – 213CytoplasmicSequence analysisAdd BLAST15
Transmembranei214 – 233HelicalUniRule annotationAdd BLAST20
Topological domaini234 – 236PeriplasmicSequence analysis3
Transmembranei237 – 254HelicalUniRule annotationAdd BLAST18
Topological domaini255 – 269CytoplasmicSequence analysisAdd BLAST15
Transmembranei270 – 290HelicalUniRule annotationAdd BLAST21
Topological domaini291 – 293PeriplasmicSequence analysis3
Transmembranei294 – 314HelicalUniRule annotationAdd BLAST21
Topological domaini315 – 326CytoplasmicSequence analysisAdd BLAST12
Transmembranei327 – 347HelicalUniRule annotationAdd BLAST21
Topological domaini348 – 358PeriplasmicSequence analysisAdd BLAST11
Transmembranei359 – 379HelicalUniRule annotationAdd BLAST21
Topological domaini380 – 620Cytoplasmic1 PublicationAdd BLAST241

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoliWiki
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi262E → 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. 1
Mutagenesisi264D → A: Increases constitutive potassium efflux. 1 Publication1
Mutagenesisi412Q → A: Increases constitutive potassium efflux and reduces glutathione-mediated inhibition of potassium efflux. 1 Publication1
Mutagenesisi412Q → K: Increases constitutive potassium efflux and abolishes regulation of potassium efflux by glutathione and glutathione adducts. 1 Publication1
Mutagenesisi416R → A: Increases constitutive potassium efflux and abolishes regulation of potassium efflux by glutathione and glutathione adducts; when associated with A-516 and A-551. 2 Publications1
Mutagenesisi416R → S: Increased constitutive potassium efflux. 2 Publications1
Mutagenesisi441F → D or L: Reduced activation of potassium efflux by glutathione adducts. 1 Publication1
Mutagenesisi441F → W or Y: No effect on activation of potassium efflux by glutathione adducts. 1 Publication1
Mutagenesisi499D → A: Strongly reduced activation of potassium efflux by glutathione adducts. 1 Publication1
Mutagenesisi499D → G: Mildly reduced activation of potassium efflux by glutathione adducts. 1 Publication1
Mutagenesisi499D → S: No effect on potassium efflux. 1 Publication1
Mutagenesisi516R → A: Increases constitutive potassium efflux and abolishes regulation of potassium efflux by glutathione and glutathione adducts; when associated with A-416 and A-551. 1 Publication1
Mutagenesisi520E → G: Strongly reduced potassium efflux. 1 Publication1
Mutagenesisi522A → V: Strongly reduced potassium efflux. 1 Publication1
Mutagenesisi526G → V: Strongly reduced potassium efflux. 1 Publication1
Mutagenesisi551N → A: Increases constitutive potassium efflux and abolishes regulation of potassium efflux by glutathione and glutathione adducts; when associated with A-416 and A-516. 2 Publications1
Mutagenesisi551N → D: Increases constitutive potassium efflux; when associated with K-262. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001966061 – 620Glutathione-regulated potassium-efflux system protein KefCAdd BLAST620

Proteomic databases

PaxDbiP03819.
PRIDEiP03819.

Interactioni

Subunit structurei

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.UniRule annotation3 Publications

GO - Molecular functioni

  • enzyme binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262200. 7 interactors.
DIPiDIP-10072N.
IntActiP03819. 2 interactors.
MINTiMINT-1257196.
STRINGi511145.b0047.

Structurei

Secondary structure

1620
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi401 – 405Combined sources5
Helixi409 – 420Combined sources12
Beta strandi425 – 429Combined sources5
Helixi432 – 440Combined sources9
Beta strandi446 – 448Combined sources3
Helixi453 – 458Combined sources6
Turni459 – 463Combined sources5
Beta strandi465 – 469Combined sources5
Helixi474 – 487Combined sources14
Beta strandi492 – 499Combined sources8
Helixi500 – 508Combined sources9
Helixi519 – 532Combined sources14
Helixi537 – 560Combined sources24
Helixi565 – 579Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EYWX-ray2.40A/B401-620[»]
3L9WX-ray1.75A/B401-620[»]
3L9XX-ray2.10A/B401-620[»]
ProteinModelPortaliP03819.
SMRiP03819.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03819.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini401 – 523RCK N-terminalUniRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni259 – 267Important for the regulation of potassium conductance9
Regioni498 – 500Glutathione binding3

Domaini

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).1 Publication

Sequence similaritiesi

Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. KefC subfamily. [View classification]UniRule annotation
Contains 1 RCK N-terminal domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CKD. Bacteria.
COG0475. LUCA.
COG1226. LUCA.
HOGENOMiHOG000179076.
InParanoidiP03819.
KOiK11745.
OMAiRNRRHAY.
PhylomeDBiP03819.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01413. K_H_efflux_KefC. 1 hit.
InterProiIPR006153. Cation/H_exchanger.
IPR004771. K/H_exchanger.
IPR023941. K_H_efflux_KefC.
IPR006036. K_uptake_TrkA.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view]
PfamiPF00999. Na_H_Exchanger. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
PRINTSiPR00335. KUPTAKETRKA.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00932. 2a37. 1 hit.
PROSITEiPS51201. RCK_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSHTLIQAL IYLGSAALIV PIAVRLGLGS VLGYLIAGCI IGPWGLRLVT
60 70 80 90 100
DAESILHFAE IGVVLMLFII GLELDPQRLW KLRAAVFGCG ALQMVICGGL
110 120 130 140 150
LGLFCMLLGL RWQVAELIGM TLALSSTAIA MQAMNERNLM VTQMGRSAFA
160 170 180 190 200
VLLFQDIAAI PLVAMIPLLA TSSASTTMGA FALSALKVAG ALVLVVLLGR
210 220 230 240 250
YVTRPALRFV ARSGLREVFS AVALFLVFGF GLLLEEVGLS MAMGAFLAGV
260 270 280 290 300
LLASSEYRHA LESDIEPFKG LLLGLFFIGV GMSIDFGTLL ENPLRIVILL
310 320 330 340 350
LGFLIIKIAM LWLIARPLQV PNKQRRWFAV LLGQGSEFAF VVFGAAQMAN
360 370 380 390 400
VLEPEWAKSL TLAVALSMAA TPILLVILNR LEQSSTEEAR EADEIDEEQP
410 420 430 440 450
RVIIAGFGRF GQITGRLLLS SGVKMVVLDH DPDHIETLRK FGMKVFYGDA
460 470 480 490 500
TRMDLLESAG AAKAEVLINA IDDPQTNLQL TEMVKEHFPH LQIIARARDV
510 520 530 540 550
DHYIRLRQAG VEKPERETFE GALKTGRLAL ESLGLGPYEA RERADVFRRF
560 570 580 590 600
NIQMVEEMAM VENDTKARAA VYKRTSAMLS EIITEDREHL SLIQRHGWQG
610 620
TEEGKHTGNM ADEPETKPSS
Length:620
Mass (Da):67,796
Last modified:November 1, 1991 - v2
Checksum:i9995B2E8E3C1DCE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56742 Genomic DNA. Translation: CAA40066.1.
U00096 Genomic DNA. Translation: AAC73158.1.
AP009048 Genomic DNA. Translation: BAB96615.1.
J01609 Genomic DNA. No translation available.
PIRiS40568. QQECRD.
RefSeqiNP_414589.1. NC_000913.3.
WP_000377098.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73158; AAC73158; b0047.
BAB96615; BAB96615; BAB96615.
GeneIDi944773.
KEGGiecj:JW0046.
eco:b0047.
PATRICi32115193. VBIEscCol129921_0048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56742 Genomic DNA. Translation: CAA40066.1.
U00096 Genomic DNA. Translation: AAC73158.1.
AP009048 Genomic DNA. Translation: BAB96615.1.
J01609 Genomic DNA. No translation available.
PIRiS40568. QQECRD.
RefSeqiNP_414589.1. NC_000913.3.
WP_000377098.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EYWX-ray2.40A/B401-620[»]
3L9WX-ray1.75A/B401-620[»]
3L9XX-ray2.10A/B401-620[»]
ProteinModelPortaliP03819.
SMRiP03819.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262200. 7 interactors.
DIPiDIP-10072N.
IntActiP03819. 2 interactors.
MINTiMINT-1257196.
STRINGi511145.b0047.

Protein family/group databases

TCDBi2.A.37.1.1. the monovalent cation:proton antiporter-2 (cpa2) family.

Proteomic databases

PaxDbiP03819.
PRIDEiP03819.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73158; AAC73158; b0047.
BAB96615; BAB96615; BAB96615.
GeneIDi944773.
KEGGiecj:JW0046.
eco:b0047.
PATRICi32115193. VBIEscCol129921_0048.

Organism-specific databases

EchoBASEiEB0516.
EcoGeneiEG10521. kefC.

Phylogenomic databases

eggNOGiENOG4105CKD. Bacteria.
COG0475. LUCA.
COG1226. LUCA.
HOGENOMiHOG000179076.
InParanoidiP03819.
KOiK11745.
OMAiRNRRHAY.
PhylomeDBiP03819.

Enzyme and pathway databases

BioCyciEcoCyc:KEFC-MONOMER.
ECOL316407:JW0046-MONOMER.
MetaCyc:KEFC-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP03819.
PROiP03819.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01413. K_H_efflux_KefC. 1 hit.
InterProiIPR006153. Cation/H_exchanger.
IPR004771. K/H_exchanger.
IPR023941. K_H_efflux_KefC.
IPR006036. K_uptake_TrkA.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view]
PfamiPF00999. Na_H_Exchanger. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
PRINTSiPR00335. KUPTAKETRKA.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00932. 2a37. 1 hit.
PROSITEiPS51201. RCK_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKEFC_ECOLI
AccessioniPrimary (citable) accession number: P03819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.