ID NARK_ECOLI Reviewed; 463 AA.
AC P10903;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Nitrate/nitrite antiporter NarK {ECO:0000303|PubMed:25959928};
DE AltName: Full=Nitrate/nitrite exchanger {ECO:0000303|PubMed:23665960};
DE AltName: Full=Nitrite extrusion protein 1;
DE AltName: Full=Nitrite facilitator 1;
GN Name=narK {ECO:0000303|PubMed:2668029}; OrderedLocusNames=b1223, JW1214;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2668029; DOI=10.1016/0014-5793(89)80906-8;
RA Noji S., Nohno T., Saito T., Taniguchi S.;
RT "The narK gene product participates in nitrate transport induced in
RT Escherichia coli nitrate-respiring cells.";
RL FEBS Lett. 252:139-143(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 1-31.
RC STRAIN=K12;
RX PubMed=2657652; DOI=10.1093/nar/17.8.2947;
RA Nohno T., Noji S., Taniguchi S., Saito T.;
RT "The narX and narL genes encoding the nitrate-sensing regulators of
RT Escherichia coli are homologous to a family of prokaryotic two-component
RT regulatory genes.";
RL Nucleic Acids Res. 17:2947-2957(1989).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11967075; DOI=10.1046/j.1365-2958.2002.02858.x;
RA Clegg S., Yu F., Griffiths L., Cole J.A.;
RT "The roles of the polytopic membrane proteins NarK, NarU and NirC in
RT Escherichia coli K-12: two nitrate and three nitrite transporters.";
RL Mol. Microbiol. 44:143-155(2002).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15667293; DOI=10.1042/bst0330159;
RA Jia W., Cole J.A.;
RT "Nitrate and nitrite transport in Escherichia coli.";
RL Biochem. Soc. Trans. 33:159-161(2005).
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, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=16804183; DOI=10.1099/mic.0.28688-0;
RA Clegg S.J., Jia W., Cole J.A.;
RT "Role of the Escherichia coli nitrate transport protein, NarU, in survival
RT during severe nutrient starvation and slow growth.";
RL Microbiology 152:2091-2100(2006).
RN [10]
RP TOPOLOGY.
RX PubMed=18691156; DOI=10.1042/bj20080746;
RA Jia W., Tovell N., Clegg S., Trimmer M., Cole J.;
RT "A single channel for nitrate uptake, nitrite export and nitrite uptake by
RT Escherichia coli NarU and a role for NirC in nitrite export and uptake.";
RL Biochem. J. 417:297-304(2009).
RN [11] {ECO:0007744|PDB:4JR9, ECO:0007744|PDB:4JRE}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH NITRITE, FUNCTION AS
RP AN EXCHANGER, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN,
RP AND SUBSTRATE-BINDING SITES.
RC STRAIN=K12;
RX PubMed=23665960; DOI=10.1038/nature12139;
RA Zheng H., Wisedchaisri G., Gonen T.;
RT "Crystal structure of a nitrate/nitrite exchanger.";
RL Nature 497:647-651(2013).
RN [12] {ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V, ECO:0007744|PDB:4U4W}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH NITRATE IN THREE
RP DIFFERENT STATES, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ARG-89; PHE-147; TYR-263; PHE-267;
RP GLY-268; ARG-305; GLY-363; GLY-365; GLY-367; GLY-408 AND GLY-418.
RX PubMed=25959928; DOI=10.1038/ncomms8097;
RA Fukuda M., Takeda H., Kato H.E., Doki S., Ito K., Maturana A.D.,
RA Ishitani R., Nureki O.;
RT "Structural basis for dynamic mechanism of nitrate/nitrite antiport by
RT NarK.";
RL Nat. Commun. 6:7097-7097(2015).
CC -!- FUNCTION: Catalyzes nitrate uptake, nitrite uptake and nitrite export
CC across the cytoplasmic membrane (PubMed:2668029, PubMed:11967075,
CC PubMed:15667293, PubMed:16804183, PubMed:23665960, PubMed:25959928).
CC Functions as a nitrate/nitrite exchanger, and protons are unlikely to
CC be co-transported (PubMed:2668029, PubMed:15667293, PubMed:23665960,
CC PubMed:25959928). {ECO:0000269|PubMed:11967075,
CC ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:16804183,
CC ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:25959928,
CC ECO:0000269|PubMed:2668029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nitrate(in) + nitrite(out) = nitrate(out) + nitrite(in);
CC Xref=Rhea:RHEA:28743, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632;
CC Evidence={ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:23665960,
CC ECO:0000269|PubMed:25959928, ECO:0000305|PubMed:2668029};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:25959928}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:23665960,
CC ECO:0000269|PubMed:25959928}.
CC -!- INDUCTION: Highly expressed during anaerobic growth in the presence of
CC nitrate. {ECO:0000269|PubMed:16804183, ECO:0000269|PubMed:2668029}.
CC -!- DOMAIN: Each molecule contains 12 transmembrane helices, forming the N
CC bundle (TM1-6) and the C bundle (TM7-12) (PubMed:25959928). These N and
CC C bundles are connected with a linker loop between TM6 and TM7
CC (PubMed:25959928). The substrate-binding pocket is located at the
CC interface between the N and C bundles (PubMed:23665960,
CC PubMed:25959928). Substrate recognition is coupled to the transport
CC cycle by the concomitant movement of the transmembrane helices and the
CC key tyrosine and arginine residues in the substrate-binding site
CC (PubMed:25959928). {ECO:0000269|PubMed:23665960,
CC ECO:0000269|PubMed:25959928}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant, under conditions for the
CC induction of nitrate respiration, is unable to perform nitrate
CC transport (PubMed:2668029). The narK-narU double mutant is defective in
CC nitrate-dependent growth unless nitrate transport is facilitated by the
CC nitrate ionophore, reduced benzyl viologen (BV) (PubMed:11967075).
CC Deletion of both NarK and NirC also decreases nitrite uptake
CC (PubMed:11967075). {ECO:0000269|PubMed:11967075,
CC ECO:0000269|PubMed:2668029}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nitrate/nitrite porter (TC 2.A.1.8) family. {ECO:0000305}.
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DR EMBL; X15996; CAA34126.1; -; Genomic_DNA.
DR EMBL; X69189; CAA48933.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74307.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36091.1; -; Genomic_DNA.
DR EMBL; X13360; CAA31740.1; -; Genomic_DNA.
DR PIR; S05239; GRECNK.
DR RefSeq; NP_415741.1; NC_000913.3.
DR RefSeq; WP_000019827.1; NZ_STEB01000023.1.
DR PDB; 4JR9; X-ray; 2.60 A; A=1-463.
DR PDB; 4JRE; X-ray; 2.80 A; A/D=1-463.
DR PDB; 4U4T; X-ray; 2.40 A; A=1-463.
DR PDB; 4U4V; X-ray; 2.35 A; A=1-463.
DR PDB; 4U4W; X-ray; 2.40 A; A/B=1-463.
DR PDBsum; 4JR9; -.
DR PDBsum; 4JRE; -.
DR PDBsum; 4U4T; -.
DR PDBsum; 4U4V; -.
DR PDBsum; 4U4W; -.
DR AlphaFoldDB; P10903; -.
DR SMR; P10903; -.
DR BioGRID; 4261633; 21.
DR STRING; 511145.b1223; -.
DR TCDB; 2.A.1.8.1; the major facilitator superfamily (mfs).
DR jPOST; P10903; -.
DR PaxDb; 511145-b1223; -.
DR ABCD; P10903; 1 sequenced antibody.
DR EnsemblBacteria; AAC74307; AAC74307; b1223.
DR GeneID; 75171336; -.
DR GeneID; 945783; -.
DR KEGG; ecj:JW1214; -.
DR KEGG; eco:b1223; -.
DR PATRIC; fig|1411691.4.peg.1058; -.
DR EchoBASE; EB0636; -.
DR eggNOG; COG2223; Bacteria.
DR HOGENOM; CLU_033198_1_0_6; -.
DR InParanoid; P10903; -.
DR OMA; WWYYARR; -.
DR OrthoDB; 9771451at2; -.
DR PhylomeDB; P10903; -.
DR BioCyc; EcoCyc:NARK-MONOMER; -.
DR BioCyc; MetaCyc:NARK-MONOMER; -.
DR PRO; PR:P10903; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015113; F:nitrite transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IDA:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0043602; P:nitrate catabolic process; IMP:EcoCyc.
DR GO; GO:0015706; P:nitrate transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015707; P:nitrite transport; IMP:EcoCyc.
DR CDD; cd17341; MFS_NRT2_like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044772; NO3_transporter.
DR InterPro; IPR004737; NO3_transporter_NarK/NarU-like.
DR NCBIfam; TIGR00886; 2A0108; 1.
DR PANTHER; PTHR23515; HIGH-AFFINITY NITRATE TRANSPORTER 2.3; 1.
DR PANTHER; PTHR23515:SF6; NITRATE_NITRITE ANTIPORTER NARK; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Nitrate assimilation; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="Nitrate/nitrite antiporter NarK"
FT /id="PRO_0000096728"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 60..73
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 96..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 123..130
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 152..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 190..211
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 234..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 254..281
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 282..289
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 313..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 339..347
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 348..373
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 374..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 428..435
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TRANSMEM 436..458
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V"
FT TOPO_DOM 459..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T,
FT ECO:0007744|PDB:4U4V"
FT BINDING 89
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4W"
FT BINDING 89
FT /ligand="nitrite"
FT /ligand_id="ChEBI:CHEBI:16301"
FT /evidence="ECO:0000269|PubMed:23665960,
FT ECO:0007744|PDB:4JRE"
FT BINDING 175
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4W"
FT BINDING 263
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4W"
FT BINDING 263
FT /ligand="nitrite"
FT /ligand_id="ChEBI:CHEBI:16301"
FT /evidence="ECO:0000269|PubMed:23665960,
FT ECO:0007744|PDB:4JRE"
FT BINDING 411
FT /ligand="nitrate"
FT /ligand_id="ChEBI:CHEBI:17632"
FT /evidence="ECO:0000269|PubMed:25959928,
FT ECO:0007744|PDB:4U4T"
FT SITE 305
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:23665960,
FT ECO:0000305|PubMed:25959928"
FT MUTAGEN 89
FT /note="R->K: Decreases nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 147
FT /note="F->A: Decreases nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 263
FT /note="Y->F: Abolishes nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 267
FT /note="F->A: Decreases nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 268
FT /note="G->A: Abolishes nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 305
FT /note="R->K: Abolishes nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 363
FT /note="G->A: Abolishes nitrate uptake activity; when
FT associated with A-365 and A-367."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 365
FT /note="G->A: Abolishes nitrate uptake activity; when
FT associated with A-363 and A-367."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 367
FT /note="G->A: Abolishes nitrate uptake activity; when
FT associated with A-363 and A-365."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 408
FT /note="G->A: Abolishes nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT MUTAGEN 418
FT /note="G->A: Abolishes nitrate uptake activity."
FT /evidence="ECO:0000269|PubMed:25959928"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:4U4W"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 30..52
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:4U4V"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4U4V"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4JRE"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 254..284
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4U4V"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 296..315
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 317..334
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4U4V"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4U4T"
FT HELIX 348..387
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 392..414
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 417..432
FT /evidence="ECO:0007829|PDB:4U4V"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:4U4T"
FT HELIX 436..459
FT /evidence="ECO:0007829|PDB:4U4V"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:4U4T"
SQ SEQUENCE 463 AA; 49693 MW; AF1DD67CAD40FE8A CRC64;
MSHSSAPERA TGAVITDWRP EDPAFWQQRG QRIASRNLWI SVPCLLLAFC VWMLFSAVAV
NLPKVGFNFT TDQLFMLTAL PSVSGALLRV PYSFMVPIFG GRRWTAFSTG ILIIPCVWLG
FAVQDTSTPY SVFIIISLLC GFAGANFASS MANISFFFPK QKQGGALGLN GGLGNMGVSV
MQLVAPLVVS LSIFAVFGSQ GVKQPDGTEL YLANASWIWV PFLAIFTIAA WFGMNDLATS
KASIKEQLPV LKRGHLWIMS LLYLATFGSF IGFSAGFAML SKTQFPDVQI LQYAFFGPFI
GALARSAGGA LSDRLGGTRV TLVNFILMAI FSGLLFLTLP TDGQGGSFMA FFAVFLALFL
TAGLGSGSTF QMISVIFRKL TMDRVKAEGG SDERAMREAA TDTAAALGFI SAIGAIGGFF
IPKAFGSSLA LTGSPVGAMK VFLIFYIACV VITWAVYGRH SKK
//
