ISCS_ECOLI
ID ISCS_ECOLI Reviewed; 404 AA.
AC P0A6B7; P39171; P76581; P76992; Q8XA86;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000303|PubMed:8663056};
DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:8663056};
DE AltName: Full=NifS protein homolog {ECO:0000303|PubMed:8663056};
DE AltName: Full=ThiI transpersulfidase {ECO:0000303|PubMed:10600118};
DE AltName: Full=TusA transpersulfidase {ECO:0000303|PubMed:16387657};
GN Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331}; Synonyms=nuvC, yfhO, yzzO;
GN OrderedLocusNames=b2530, JW2514;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339 AND
RP 382-391, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=8663056; DOI=10.1016/s0021-9258(18)48580-8;
RA Flint D.H.;
RT "Escherichia coli contains a protein that is homologous in function and N-
RT terminal sequence to the protein encoded by the nifS gene of Azotobacter
RT vinelandii and that can participate in the synthesis of the Fe-S cluster of
RT dihydroxy-acid dehydratase.";
RL J. Biol. Chem. 271:16068-16074(1996).
RN [5]
RP PROTEIN SEQUENCE OF 1-16, FUNCTION, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=10600118; DOI=10.1021/bi991119r;
RA Kambampati R., Lauhon C.T.;
RT "IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine
RT in Escherichia coli tRNA.";
RL Biochemistry 38:16561-16568(1999).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-9, AND MUTAGENESIS OF CYS-328.
RC STRAIN=K12;
RX PubMed=10739946; DOI=10.1093/oxfordjournals.jbchem.a022641;
RA Mihara H., Kurihara T., Yoshimura T., Esaki N.;
RT "Kinetic and mutational studies of three NifS homologs from Escherichia
RT coli: mechanistic difference between L-cysteine desulfurase and L-
RT selenocysteine lyase reactions.";
RL J. Biochem. 127:559-567(2000).
RN [8]
RP FUNCTION, AND PATHWAY.
RC STRAIN=C41(DE3);
RX PubMed=10544286; DOI=10.1093/oxfordjournals.jbchem.a022535;
RA Takahashi Y., Nakamura M.;
RT "Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene
RT cluster involved in the assembly of Fe-S clusters in Escherichia coli.";
RL J. Biochem. 126:917-926(1999).
RN [9]
RP FUNCTION.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=10781558; DOI=10.1128/jb.182.10.2879-2885.2000;
RA Kiyasu T., Asakura A., Nagahashi Y., Hoshino T.;
RT "Contribution of cysteine desulfurase (NifS protein) to the biotin synthase
RT reaction of Escherichia coli.";
RL J. Bacteriol. 182:2879-2885(2000).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10781607; DOI=10.1074/jbc.m002680200;
RA Lauhon C.T., Kambampati R.;
RT "The iscS gene in Escherichia coli is required for the biosynthesis of 4-
RT thiouridine, thiamine, and NAD.";
RL J. Biol. Chem. 275:20096-20103(2000).
RN [11]
RP FUNCTION IN SELENIUM DELIVERY.
RC STRAIN=MBO8;
RX PubMed=10829016; DOI=10.1074/jbc.m000926200;
RA Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.;
RT "Escherichia coli NifS-like proteins provide selenium in the pathway for
RT the biosynthesis of selenophosphate.";
RL J. Biol. Chem. 275:23769-23773(2000).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10908675; DOI=10.1073/pnas.160261497;
RA Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J.;
RT "The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster
RT formation in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9009-9014(2000).
RN [13]
RP FUNCTION IN SULFUR TRANSFER, INTERACTION WITH ISCU, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 376-SER--HIS-404.
RC STRAIN=K12;
RX PubMed=11577100; DOI=10.1074/jbc.m106907200;
RA Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E.;
RT "Transfer of sulfur from IscS to IscU during Fe/S cluster assembly.";
RL J. Biol. Chem. 276:44521-44526(2001).
RN [14]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=16387657; DOI=10.1016/j.molcel.2005.11.001;
RA Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.;
RT "Mechanistic insights into sulfur relay by multiple sulfur mediators
RT involved in thiouridine biosynthesis at tRNA wobble positions.";
RL Mol. Cell 21:97-108(2006).
RN [15]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22203963; DOI=10.1073/pnas.1114372109;
RA Kim J.H., Tonelli M., Markley J.L.;
RT "Disordered form of the scaffold protein IscU is the substrate for iron-
RT sulfur cluster assembly on cysteine desulfurase.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:454-459(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP PYRIDOXAL PHOSPHATE AT LYS-206, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=12860127; DOI=10.1016/s0022-2836(03)00690-9;
RA Cupp-Vickery J.R., Urbina H., Vickery L.E.;
RT "Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.";
RL J. Mol. Biol. 330:1049-1059(2003).
CC -!- FUNCTION: Master enzyme that delivers sulfur to a number of partners
CC involved in Fe-S cluster assembly, tRNA modification or cofactor
CC biosynthesis. Catalyzes the removal of elemental sulfur from cysteine
CC to produce alanine. Functions as a sulfur delivery protein for Fe-S
CC cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well
CC as other S acceptor proteins. Preferentially binds to disordered IscU
CC on which the Fe-S is assembled, IscU converts to the structured state
CC and then dissociates from IscS to transfer the Fe-S to an acceptor
CC protein. Also functions as a selenium delivery protein in the pathway
CC for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys-
CC 456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation
CC reactions. {ECO:0000269|PubMed:10544286, ECO:0000269|PubMed:10600118,
CC ECO:0000269|PubMed:10781558, ECO:0000269|PubMed:10781607,
CC ECO:0000269|PubMed:10829016, ECO:0000269|PubMed:10908675,
CC ECO:0000269|PubMed:11577100, ECO:0000269|PubMed:16387657,
CC ECO:0000269|PubMed:22203963, ECO:0000269|PubMed:8663056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00331, ECO:0000269|PubMed:8663056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000269|PubMed:10600118, ECO:0000269|PubMed:12860127};
CC -!- ACTIVITY REGULATION: Treatment with N-ethylmaleimide inhibits sulfur
CC transfer. Activated by ThiI and TusA. {ECO:0000269|PubMed:10600118,
CC ECO:0000269|PubMed:11577100, ECO:0000269|PubMed:16387657}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for L-cysteine {ECO:0000269|PubMed:11577100};
CC Note=kcat is 8.5 min(-1). {ECO:0000269|PubMed:11577100};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|PubMed:10544286}.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with IscU and TusA, other S
CC acceptors. Each subunit of the IscS dimer contacts a IscU monomer.
CC {ECO:0000269|PubMed:11577100, ECO:0000269|PubMed:12860127,
CC ECO:0000269|PubMed:16387657, ECO:0000269|PubMed:22203963}.
CC -!- INTERACTION:
CC P0A6B7; P27838: cyaY; NbExp=2; IntAct=EBI-550055, EBI-9146621;
CC P0A6B7; P0A9R4: fdx; NbExp=2; IntAct=EBI-550055, EBI-767037;
CC P0A6B7; P0ACD4: iscU; NbExp=12; IntAct=EBI-550055, EBI-561646;
CC P0A6B7; P0A890: tusA; NbExp=7; IntAct=EBI-550055, EBI-561780;
CC P0A6B7; P52197: rhdA; Xeno; NbExp=2; IntAct=EBI-550055, EBI-7906952;
CC P0A6B7; Q1R8K8: yfhJ; Xeno; NbExp=2; IntAct=EBI-550055, EBI-15582429;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000305}.
CC -!- DOMAIN: The C-terminus (residues 376-404) is important for interaction
CC with IscU. {ECO:0000269|PubMed:11577100}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose sulfurtransferase
CC activity and require thiamine and nicotinic acid for growth. Under
CC aerobic conditions the deletion of IscS causes an auxotrophy for
CC thiamine and nicotinic acid, whereas under anaerobic conditions, only
CC nicotinic acid s required. {ECO:0000269|PubMed:10781607,
CC ECO:0000269|PubMed:10908675}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00331}.
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DR EMBL; U00096; AAT48142.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16424.1; -; Genomic_DNA.
DR RefSeq; WP_001295373.1; NZ_STEB01000011.1.
DR RefSeq; YP_026169.1; NC_000913.3.
DR PDB; 1P3W; X-ray; 2.10 A; A/B=1-404.
DR PDBsum; 1P3W; -.
DR AlphaFoldDB; P0A6B7; -.
DR SASBDB; P0A6B7; -.
DR SMR; P0A6B7; -.
DR BioGRID; 4263511; 579.
DR BioGRID; 851343; 3.
DR ComplexPortal; CPX-2136; L-cysteine desulfurase complex.
DR ComplexPortal; CPX-2139; iscS-tusA cysteine desulfurase complex.
DR ComplexPortal; CPX-2140; iscS-thiI sulfurtransferase complex.
DR ComplexPortal; CPX-2141; iscS-iscU iron-sulfur cluster assembly complex.
DR DIP; DIP-29109N; -.
DR IntAct; P0A6B7; 47.
DR MINT; P0A6B7; -.
DR STRING; 511145.b2530; -.
DR jPOST; P0A6B7; -.
DR PaxDb; P0A6B7; -.
DR PRIDE; P0A6B7; -.
DR EnsemblBacteria; AAT48142; AAT48142; b2530.
DR EnsemblBacteria; BAA16424; BAA16424; BAA16424.
DR GeneID; 67416914; -.
DR GeneID; 947004; -.
DR KEGG; ecj:JW2514; -.
DR KEGG; eco:b2530; -.
DR PATRIC; fig|1411691.4.peg.4204; -.
DR EchoBASE; EB2542; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_6; -.
DR InParanoid; P0A6B7; -.
DR OMA; KGLYWAR; -.
DR PhylomeDB; P0A6B7; -.
DR BioCyc; EcoCyc:G7325-MON; -.
DR BioCyc; MetaCyc:G7325-MON; -.
DR SABIO-RK; P0A6B7; -.
DR UniPathway; UPA00266; -.
DR EvolutionaryTrace; P0A6B7; -.
DR PRO; PR:P0A6B7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990330; C:IscS-IscU complex; IPI:ComplexPortal.
DR GO; GO:1990329; C:IscS-TusA complex; IPI:ComplexPortal.
DR GO; GO:1990221; C:L-cysteine desulfurase complex; IPI:ComplexPortal.
DR GO; GO:1990228; C:sulfurtransferase complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009000; F:selenocysteine lyase activity; IDA:EcoCyc.
DR GO; GO:0097163; F:sulfur carrier activity; EXP:EcoCyc.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0009589; P:detection of UV; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:EcoCyc.
DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:ComplexPortal.
DR GO; GO:0018131; P:oxazole or thiazole biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016261; P:selenocysteine catabolic process; IDA:ComplexPortal.
DR GO; GO:0072348; P:sulfur compound transport; IDA:ComplexPortal.
DR GO; GO:0009228; P:thiamine biosynthetic process; IC:ComplexPortal.
DR GO; GO:0002937; P:tRNA 4-thiouridine biosynthesis; IMP:EcoCyc.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IDA:ComplexPortal.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02006; IscS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; Pyridoxal phosphate; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..404
FT /note="Cysteine desulfurase IscS"
FT /id="PRO_0000150264"
FT ACT_SITE 328
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:12860127, ECO:0000269|PubMed:8663056"
FT BINDING 75..76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT BINDING 155
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:12860127"
FT BINDING 203..205
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:12860127"
FT BINDING 243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:12860127"
FT BINDING 328
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscU"
FT /note="via persulfide group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:12860127"
FT MUTAGEN 328
FT /note="C->A: Loss of cysteine desulfurization."
FT /evidence="ECO:0000269|PubMed:10739946"
FT MUTAGEN 376..404
FT /note="Missing: Normal cysteine desulfurase activity,
FT decreased binding to IscU, decreased sulfur transfer to
FT IscU, decreased Fe-S cluster assembly."
FT /evidence="ECO:0000269|PubMed:11577100"
FT CONFLICT 31
FT /note="G -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="G -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37..38
FT /note="AS -> NA (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="P -> M (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..327
FT /note="SA -> YL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 246..279
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1P3W"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:1P3W"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 363..382
FT /evidence="ECO:0007829|PDB:1P3W"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:1P3W"
SQ SEQUENCE 404 AA; 45090 MW; 1E4F2E6F9CD266B0 CRC64;
MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA VDIARNQIAD
LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS KTEHKAVLDT CRQLEREGFE
VTYLAPQRNG IIDLKELEAA MRDDTILVSI MHVNNEIGVV QDIAAIGEMC RARGIIYHVD
ATQSVGKLPI DLSQLKVDLM SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR
SGTLPVHQIV GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFSLGRF
TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE WAHH
