KEFC_ECOLI
ID KEFC_ECOLI Reviewed; 620 AA.
AC P03819;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glutathione-regulated potassium-efflux system protein KefC {ECO:0000255|HAMAP-Rule:MF_01413};
DE AltName: Full=K(+)/H(+) antiporter {ECO:0000255|HAMAP-Rule:MF_01413};
GN Name=kefC {ECO:0000255|HAMAP-Rule:MF_01413}; Synonyms=trkC;
GN OrderedLocusNames=b0047, JW0046;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / CS520;
RX PubMed=2046548; DOI=10.1111/j.1365-2958.1991.tb00731.x;
RA Munro A.W., Ritchie G.Y., Lamb A.J., Douglas R.M., Booth I.R.;
RT "The cloning and DNA sequence of the gene for the glutathione-regulated
RT potassium-efflux system KefC of Escherichia coli.";
RL Mol. Microbiol. 5:607-616(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-620.
RC STRAIN=K12;
RX PubMed=6159575; DOI=10.1093/nar/8.10.2255;
RA Smith D.R., Calvo J.M.;
RT "Nucleotide sequence of the E coli gene coding for dihydrofolate
RT reductase.";
RL Nucleic Acids Res. 8:2255-2274(1980).
RN [6]
RP SIMILARITY TO NAPA.
RX PubMed=1325937; DOI=10.1016/0378-1097(92)90601-j;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "The putative Na+/H+ antiporter (NapA) of Enterococcus hirae is homologous
RT to the putative K+/H+ antiporter (KefC) of Escherichia coli.";
RL FEMS Microbiol. Lett. 73:161-163(1992).
RN [7]
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 [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=17679694; DOI=10.1073/pnas.0703709104;
RA Fujisawa M., Ito M., Krulwich T.A.;
RT "Three two-component transporters with channel-like properties have
RT monovalent cation/proton antiport activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13289-13294(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 401-620 IN COMPLEX WITH KEFF AND
RP AMP, SUBUNIT, INTERACTION WITH KEFF, MUTAGENESIS OF ASP-264; ARG-416;
RP GLU-520; ALA-522; GLY-526 AND ASN-551, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19523906; DOI=10.1016/j.str.2009.03.018;
RA Roosild T.P., Castronovo S., Miller S., Li C., Rasmussen T., Bartlett W.,
RA Gunasekera B., Choe S., Booth I.R.;
RT "KTN (RCK) domains regulate K+ channels and transporters by controlling the
RT dimer-hinge conformation.";
RL Structure 17:893-903(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 401-620 IN COMPLEXES WITH KEFF;
RP AMP AND GLUTATHIONE, FUNCTION, SUBUNIT, INTERACTION WITH KEFF, ACTIVITY
RP REGULATION, DOMAIN, AND MUTAGENESIS OF GLN-412; ARG-416; PHE-441; ASP-499;
RP ARG-516 AND ASN-551.
RX PubMed=21041667; DOI=10.1073/pnas.1012716107;
RA Roosild T.P., Castronovo S., Healy J., Miller S., Pliotas C., Rasmussen T.,
RA Bartlett W., Conway S.J., Booth I.R.;
RT "Mechanism of ligand-gated potassium efflux in bacterial pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19784-19789(2010).
CC -!- FUNCTION: Pore-forming subunit of a potassium efflux system that
CC confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
CC Can also export rubidium, lithium and sodium. {ECO:0000255|HAMAP-
CC Rule:MF_01413, ECO:0000269|PubMed:17679694,
CC ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}.
CC -!- ACTIVITY REGULATION: Inhibited by glutathione. This inhibition is
CC increased by NADH. Activated by adducts between glutathione and
CC electrophiles. {ECO:0000269|PubMed:17679694,
CC ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}.
CC -!- SUBUNIT: Homodimer. Interacts with the regulatory subunit KefF, forming
CC a heterotetramer with 2:2 stoichiometry. Interaction with KefF is
CC required for optimal activity. The active antiporter may be formed by
CC the heterotetramer, or by an octamer. {ECO:0000255|HAMAP-Rule:MF_01413,
CC ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:19523906,
CC ECO:0000269|PubMed:21041667}.
CC -!- INTERACTION:
CC P03819; P0A754: kefF; NbExp=2; IntAct=EBI-547193, EBI-562116;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01413, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2046548}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2046548}.
CC -!- DOMAIN: The cytoplasmic RCK N-terminal domain regulates channel
CC activity. It binds glutathione, resulting in inhibition of potassium
CC efflux. In contrast, binding of the adducts formed between glutathione
CC and electrophiles leads to activation of potassium efflux. Is expected
CC to bind NADH, but X-ray crystallography shows bound AMP, and it would
CC be difficult to accommodate NADH in this binding site
CC (PubMed:21041667). {ECO:0000269|PubMed:21041667}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. KefC subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01413}.
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DR EMBL; X56742; CAA40066.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73158.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96615.1; -; Genomic_DNA.
DR EMBL; J01609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S40568; QQECRD.
DR RefSeq; NP_414589.1; NC_000913.3.
DR RefSeq; WP_000377098.1; NZ_STEB01000010.1.
DR PDB; 3EYW; X-ray; 2.40 A; A/B=401-620.
DR PDB; 3L9W; X-ray; 1.75 A; A/B=401-620.
DR PDB; 3L9X; X-ray; 2.10 A; A/B=401-620.
DR PDBsum; 3EYW; -.
DR PDBsum; 3L9W; -.
DR PDBsum; 3L9X; -.
DR AlphaFoldDB; P03819; -.
DR SMR; P03819; -.
DR BioGRID; 4262200; 8.
DR ComplexPortal; CPX-2543; Glutathione-regulated potassium-efflux system KefC-KefF complex.
DR DIP; DIP-10072N; -.
DR IntAct; P03819; 3.
DR STRING; 511145.b0047; -.
DR TCDB; 2.A.37.1.1; the monovalent cation:proton antiporter-2 (cpa2) family.
DR jPOST; P03819; -.
DR PaxDb; P03819; -.
DR PRIDE; P03819; -.
DR EnsemblBacteria; AAC73158; AAC73158; b0047.
DR EnsemblBacteria; BAB96615; BAB96615; BAB96615.
DR GeneID; 944773; -.
DR KEGG; ecj:JW0046; -.
DR KEGG; eco:b0047; -.
DR PATRIC; fig|1411691.4.peg.2236; -.
DR EchoBASE; EB0516; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR InParanoid; P03819; -.
DR OMA; PYLWFAK; -.
DR PhylomeDB; P03819; -.
DR BioCyc; EcoCyc:KEFC-MON; -.
DR BioCyc; MetaCyc:KEFC-MON; -.
DR EvolutionaryTrace; P03819; -.
DR PRO; PR:P03819; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0019899; F:enzyme binding; IMP:EcoCyc.
DR GO; GO:0015503; F:glutathione-regulated potassium exporter activity; IMP:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; IDA:EcoCyc.
DR GO; GO:0051454; P:intracellular pH elevation; IC:ComplexPortal.
DR GO; GO:0006813; P:potassium ion transport; IDA:EcoliWiki.
DR GO; GO:0051453; P:regulation of intracellular pH; IC:ComplexPortal.
DR GO; GO:0006885; P:regulation of pH; IDA:EcoliWiki.
DR GO; GO:0051595; P:response to methylglyoxal; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR Gene3D; 1.20.1530.20; -; 1.
DR HAMAP; MF_01413; K_H_efflux_KefC; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR023941; K_H_efflux_KefC.
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 PANTHER; PTHR46157:SF3; PTHR46157:SF3; 1.
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 1: Evidence at protein level;
KW 3D-structure; Antiport; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Nucleotide-binding; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Glutathione-regulated potassium-efflux system
FT protein KefC"
FT /id="PRO_0000196606"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 47..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 75..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 111..113
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 135..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 170..177
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 199..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 234..236
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 255..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 291..293
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 315..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 348..358
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT TOPO_DOM 380..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT DOMAIN 401..523
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01413"
FT REGION 259..267
FT /note="Important for the regulation of potassium
FT conductance"
FT REGION 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..410
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 412
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 429..430
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 434
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 449..450
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 472
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 496
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:19523906"
FT BINDING 498..500
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT BINDING 516
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT MUTAGEN 262
FT /note="E->K: Increases potassium efflux in the absence of
FT glutathione, but not in the presence of glutathione.
FT Increases constitutive potassium efflux; when associated
FT with D-551."
FT MUTAGEN 264
FT /note="D->A: Increases constitutive potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906"
FT MUTAGEN 412
FT /note="Q->A: Increases constitutive potassium efflux and
FT reduces glutathione-mediated inhibition of potassium
FT efflux."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 412
FT /note="Q->K: Increases constitutive potassium efflux and
FT abolishes regulation of potassium efflux by glutathione and
FT glutathione adducts."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 416
FT /note="R->A: Increases constitutive potassium efflux and
FT abolishes regulation of potassium efflux by glutathione and
FT glutathione adducts; when associated with A-516 and A-551."
FT /evidence="ECO:0000269|PubMed:19523906,
FT ECO:0000269|PubMed:21041667"
FT MUTAGEN 416
FT /note="R->S: Increased constitutive potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906,
FT ECO:0000269|PubMed:21041667"
FT MUTAGEN 441
FT /note="F->D,L: Reduced activation of potassium efflux by
FT glutathione adducts."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 441
FT /note="F->W,Y: No effect on activation of potassium efflux
FT by glutathione adducts."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 499
FT /note="D->A: Strongly reduced activation of potassium
FT efflux by glutathione adducts."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 499
FT /note="D->G: Mildly reduced activation of potassium efflux
FT by glutathione adducts."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 499
FT /note="D->S: No effect on potassium efflux."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 516
FT /note="R->A: Increases constitutive potassium efflux and
FT abolishes regulation of potassium efflux by glutathione and
FT glutathione adducts; when associated with A-416 and A-551."
FT /evidence="ECO:0000269|PubMed:21041667"
FT MUTAGEN 520
FT /note="E->G: Strongly reduced potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906"
FT MUTAGEN 522
FT /note="A->V: Strongly reduced potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906"
FT MUTAGEN 526
FT /note="G->V: Strongly reduced potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906"
FT MUTAGEN 551
FT /note="N->A: Increases constitutive potassium efflux and
FT abolishes regulation of potassium efflux by glutathione and
FT glutathione adducts; when associated with A-416 and A-516."
FT /evidence="ECO:0000269|PubMed:19523906,
FT ECO:0000269|PubMed:21041667"
FT MUTAGEN 551
FT /note="N->D: Increases constitutive potassium efflux; when
FT associated with K-262."
FT /evidence="ECO:0000269|PubMed:19523906,
FT ECO:0000269|PubMed:21041667"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:3L9W"
FT TURN 459..463
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 474..487
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 492..499
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 500..508
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 519..532
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 537..560
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 565..579
FT /evidence="ECO:0007829|PDB:3L9W"
SQ 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
