ARAC_ECOLI
ID ARAC_ECOLI Reviewed; 292 AA.
AC P0A9E0; P03021; Q47056;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Arabinose operon regulatory protein {ECO:0000305};
DE AltName: Full=HTH-type transcriptional regulator AraC {ECO:0000305};
GN Name=araC {ECO:0000303|PubMed:4943786}; OrderedLocusNames=b0064, JW0063;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B/R;
RX PubMed=7019009; DOI=10.1016/0378-1119(80)90100-6;
RA Wallace R.G., Lee N., Fowler A.V.;
RT "The araC gene of Escherichia coli: transcriptional and translational
RT start-points and complete nucleotide sequence.";
RL Gene 12:179-190(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B/R;
RX PubMed=7008027; DOI=10.1093/nar/8.22.5267;
RA Miyada C.G., Horwitz A.H., Cass L.G., Timko J., Wilcox G.;
RT "DNA sequence of the araC regulatory gene from Escherichia coli B/r.";
RL Nucleic Acids Res. 8:5267-5274(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6283093; DOI=10.1016/s0022-2836(82)80020-x;
RA Stoner C.M., Schleif R.;
RT "Is the amino acid but not the nucleotide sequence of the Escherichia coli
RT araC gene conserved?";
RL J. Mol. Biol. 154:649-652(1982).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RC STRAIN=B/R;
RX PubMed=6160371; DOI=10.1007/bf00267373;
RA Cass L.G., Horwitz A.H., Miyada C.G., Greenfield L., Wilcox G.;
RT "The araC regulatory gene mRNA contains a leader sequence.";
RL Mol. Gen. Genet. 180:219-226(1980).
RN [8]
RP PURIFICATION, AND DNA-BINDING.
RX PubMed=4943786; DOI=10.1073/pnas.68.9.2145;
RA Wilcox G., Clemetson K.J., Santi D.V., Englesberg E.;
RT "Purification of the araC protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 68:2145-2148(1971).
RN [9]
RP FUNCTION.
RX PubMed=4362626; DOI=10.1073/pnas.71.3.634;
RA Lee N., Wilcox G., Gielow W., Arnold J., Cleary P., Englesberg E.;
RT "In vitro activation of the transcription of araBAD operon by araC
RT activator.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:634-638(1974).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=328165; DOI=10.1016/0092-8674(77)90072-1;
RA Hirsh J., Schleif R.;
RT "The araC promoter: transcription, mapping and interaction with the araBAD
RT promoter.";
RL Cell 11:545-550(1977).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=6251457; DOI=10.1073/pnas.77.6.3346;
RA Ogden S., Haggerty D., Stoner C.M., Kolodrubetz D., Schleif R.;
RT "The Escherichia coli L-arabinose operon: binding sites of the regulatory
RT proteins and a mechanism of positive and negative regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:3346-3350(1980).
RN [12]
RP FUNCTION.
RX PubMed=6319708; DOI=10.1016/0022-2836(83)90035-9;
RA Stoner C., Schleif R.F.;
RT "The araE low affinity L-arabinose transport promoter. Cloning, sequence,
RT transcription start site and DNA binding sites of regulatory proteins.";
RL J. Mol. Biol. 171:369-381(1983).
RN [13]
RP INDUCTION.
RX PubMed=6377308; DOI=10.1073/pnas.81.13.4120;
RA Miyada C.G., Stoltzfus L., Wilcox G.;
RT "Regulation of the araC gene of Escherichia coli: catabolite repression,
RT autoregulation, and effect on araBAD expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4120-4124(1984).
RN [14]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=2962192; DOI=10.1073/pnas.84.24.8814;
RA Lee N., Francklyn C., Hamilton E.P.;
RT "Arabinose-induced binding of AraC protein to araI2 activates the araBAD
RT operon promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8814-8818(1987).
RN [15]
RP ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=3279415; DOI=10.1073/pnas.85.6.1749;
RA Hamilton E.P., Lee N.;
RT "Three binding sites for AraC protein are required for autoregulation of
RT araC in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1749-1753(1988).
RN [16]
RP DNA-BINDING, HTH MOTIFS, AND MUTAGENESIS OF SER-209; HIS-213; ASP-257;
RP GLN-258 AND SER-262.
RX PubMed=2531226; DOI=10.1016/0022-2836(89)90598-6;
RA Brunelle A., Schleif R.;
RT "Determining residue-base interactions between AraC protein and araI DNA.";
RL J. Mol. Biol. 209:607-622(1989).
RN [17]
RP FUNCTION.
RX PubMed=2231717; DOI=10.1016/s0022-2836(05)80163-9;
RA Hendrickson W., Stoner C., Schleif R.;
RT "Characterization of the Escherichia coli araFGH and araJ promoters.";
RL J. Mol. Biol. 215:497-510(1990).
RN [18]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=1447222; DOI=10.1016/s0021-9258(18)35841-1;
RA Lu Y., Flaherty C., Hendrickson W.;
RT "AraC protein contacts asymmetric sites in the Escherichia coli araFGH
RT promoter.";
RL J. Biol. Chem. 267:24848-24857(1992).
RN [19]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [20]
RP DOMAIN.
RX PubMed=26800223; DOI=10.1002/prot.24990;
RA Malaga F., Mayberry O., Park D.J., Rodgers M.E., Toptygin D., Schleif R.F.;
RT "A genetic and physical study of the interdomain linker of E. Coli AraC
RT protein--a trans-subunit communication pathway.";
RL Proteins 84:448-460(2016).
RN [21] {ECO:0007744|PDB:2AAC}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-178 IN COMPLEX WITH D-FUCOSE,
RP SUBUNIT, DOMAIN, AND ACTIVITY REGULATION.
RX PubMed=9367758; DOI=10.1006/jmbi.1997.1314;
RA Soisson S.M., Macdougall-Shackleton B., Schleif R., Wolberger C.;
RT "The 1.6 A crystal structure of the AraC sugar-binding and dimerization
RT domain complexed with D-fucose.";
RL J. Mol. Biol. 273:226-237(1997).
RN [22] {ECO:0007744|PDB:2ARA, ECO:0007744|PDB:2ARC}
RP X-RAY CRYSTALLOGRAPHY (1.5 AND 2.8 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX
RP WITH ARABINOSE, SUBUNIT, AND DOMAIN.
RX PubMed=9103202; DOI=10.1126/science.276.5311.421;
RA Soisson S.M., Macdougall-Shackleton B., Schleif R., Wolberger C.;
RT "Structural basis for ligand-regulated oligomerization of AraC.";
RL Science 276:421-425(1997).
RN [23] {ECO:0007744|PDB:1XJA}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-178 OF MUTANT VAL-31, SUBUNIT,
RP AND MUTAGENESIS OF TYR-31.
RX PubMed=17173282; DOI=10.1002/prot.21267;
RA Weldon J.E., Rodgers M.E., Larkin C., Schleif R.F.;
RT "Structure and properties of a truely apo form of AraC dimerization
RT domain.";
RL Proteins 66:646-654(2007).
RN [24] {ECO:0007744|PDB:2K9S}
RP STRUCTURE BY NMR OF 175-281, AND DOMAIN.
RX PubMed=19422057; DOI=10.1002/prot.22431;
RA Rodgers M.E., Schleif R.;
RT "Solution structure of the DNA binding domain of AraC protein.";
RL Proteins 77:202-208(2009).
CC -!- FUNCTION: Transcription factor that regulates the expression of several
CC genes involved in the transport and metabolism of L-arabinose
CC (PubMed:4362626, PubMed:328165, PubMed:6251457, PubMed:2962192,
CC PubMed:6319708, PubMed:2231717, PubMed:1447222). Functions both as a
CC positive and a negative regulator (PubMed:328165, PubMed:6251457). In
CC the presence of arabinose, activates the expression of the araBAD,
CC araE, araFGH and araJ promoters (PubMed:4362626, PubMed:328165,
CC PubMed:6251457, PubMed:2962192, PubMed:6319708, PubMed:2231717,
CC PubMed:1447222). In the absence of arabinose, negatively regulates the
CC araBAD operon (PubMed:6251457). Represses its own transcription
CC (PubMed:328165). Acts by binding directly to DNA (PubMed:4943786,
CC PubMed:6251457, PubMed:2962192, PubMed:2531226, PubMed:1447222).
CC {ECO:0000269|PubMed:1447222, ECO:0000269|PubMed:2231717,
CC ECO:0000269|PubMed:2531226, ECO:0000269|PubMed:2962192,
CC ECO:0000269|PubMed:328165, ECO:0000269|PubMed:4362626,
CC ECO:0000269|PubMed:4943786, ECO:0000269|PubMed:6251457,
CC ECO:0000269|PubMed:6319708}.
CC -!- ACTIVITY REGULATION: Arabinose converts the repressor form of AraC to
CC the activator form to regulate the araBAD promoter (PubMed:2962192,
CC PubMed:3279415). In the absence of arabinose, AraC binds to the araO2
CC and araI1 half-sites in the promoter region of the araBAD operon,
CC leading to the formation of a DNA loop that blocks access of RNA
CC polymerase to the promoter. In the presence of arabinose and the cyclic
CC AMP receptor protein (CRP), it binds to the adjacent half-sites araI1
CC and araI2, leading to the binding of RNA polymerase to the promoter
CC region and transcription of the araBAD operon (PubMed:2962192,
CC PubMed:3279415). AraI1 acts as a switch mechanism allowing both the
CC repressor and the activator forms of AraC protein to regulate the
CC araBAD promoter (PubMed:2962192, PubMed:3279415). Inhibited by D-
CC fucose, which binds competitively to the same site on the protein
CC (PubMed:9367758). {ECO:0000269|PubMed:2962192,
CC ECO:0000269|PubMed:3279415, ECO:0000269|PubMed:9367758}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1447222,
CC ECO:0000269|PubMed:17173282, ECO:0000269|PubMed:9103202,
CC ECO:0000269|PubMed:9367758}.
CC -!- INTERACTION:
CC P0A9E0; P0A9E0: araC; NbExp=3; IntAct=EBI-1113479, EBI-1113479;
CC P0A9E0; P0A8P6: xerC; NbExp=3; IntAct=EBI-1113479, EBI-1133806;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Negatively autoregulated (PubMed:328165, PubMed:6377308,
CC PubMed:3279415). Autoregulation is either greatly reduced or
CC nonexistent immediately after the addition of L-arabinose
CC (PubMed:6377308). Transcription is stimulated by CRP in the presence of
CC cAMP (PubMed:328165, PubMed:6377308). {ECO:0000269|PubMed:3279415,
CC ECO:0000269|PubMed:328165, ECO:0000269|PubMed:6377308}.
CC -!- DOMAIN: Contains an N-terminal domain that binds arabinose and mediates
CC dimerization, an inter-domain linker region, and a C-terminal domain
CC that binds DNA (PubMed:9103202, PubMed:9367758, PubMed:26800223).
CC Arabinose is bound within a beta barrel and is completely buried by the
CC N-terminal arm of the protein (PubMed:9103202). The DNA-binding domain
CC contains seven helices arranged in two semi-independent subdomains,
CC each containing one helix-turn-helix DNA binding motif, joined by a 19
CC residue central helix (PubMed:19422057). {ECO:0000269|PubMed:19422057,
CC ECO:0000269|PubMed:26800223, ECO:0000269|PubMed:9103202,
CC ECO:0000269|PubMed:9367758}.
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DR EMBL; V00256; CAA23507.1; -; Genomic_DNA.
DR EMBL; V00259; CAA23508.1; -; Genomic_DNA.
DR EMBL; J01641; AAA23466.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73175.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96633.1; -; Genomic_DNA.
DR EMBL; K01303; AAA23468.1; -; Genomic_DNA.
DR PIR; A91473; RGECA.
DR RefSeq; NP_414606.1; NC_000913.3.
DR RefSeq; WP_001300811.1; NZ_STEB01000010.1.
DR PDB; 1XJA; X-ray; 2.40 A; A/B/C/D/E=1-178.
DR PDB; 2AAC; X-ray; 1.60 A; A/B=2-178.
DR PDB; 2ARA; X-ray; 2.80 A; A=19-167.
DR PDB; 2ARC; X-ray; 1.50 A; A/B=7-170.
DR PDB; 2K9S; NMR; -; A=175-281.
DR PDBsum; 1XJA; -.
DR PDBsum; 2AAC; -.
DR PDBsum; 2ARA; -.
DR PDBsum; 2ARC; -.
DR PDBsum; 2K9S; -.
DR AlphaFoldDB; P0A9E0; -.
DR BMRB; P0A9E0; -.
DR SMR; P0A9E0; -.
DR BioGRID; 4260828; 116.
DR BioGRID; 849182; 11.
DR DIP; DIP-9125N; -.
DR IntAct; P0A9E0; 12.
DR STRING; 511145.b0064; -.
DR DrugBank; DB03142; Alpha-L-Arabinose.
DR DrugBank; DB04062; beta-D-fucose.
DR PaxDb; P0A9E0; -.
DR PRIDE; P0A9E0; -.
DR EnsemblBacteria; AAC73175; AAC73175; b0064.
DR EnsemblBacteria; BAB96633; BAB96633; BAB96633.
DR GeneID; 66671647; -.
DR GeneID; 944780; -.
DR KEGG; ecj:JW0063; -.
DR KEGG; eco:b0064; -.
DR PATRIC; fig|511145.12.peg.66; -.
DR EchoBASE; EB0052; -.
DR eggNOG; COG4977; Bacteria.
DR HOGENOM; CLU_000445_88_6_6; -.
DR InParanoid; P0A9E0; -.
DR OMA; GFEDQLY; -.
DR PhylomeDB; P0A9E0; -.
DR BioCyc; EcoCyc:PD00242; -.
DR EvolutionaryTrace; P0A9E0; -.
DR PRO; PR:P0A9E0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_000007d0; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0019568; P:arabinose catabolic process; IMP:EcoliWiki.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR037923; HTH-like.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR Pfam; PF02311; AraC_binding; 1.
DR Pfam; PF12833; HTH_18; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF51215; SSF51215; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Arabinose catabolism; Carbohydrate metabolism;
KW Cytoplasm; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..292
FT /note="Arabinose operon regulatory protein"
FT /id="PRO_0000194499"
FT DOMAIN 180..279
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 198..219
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593,
FT ECO:0000305|PubMed:2531226"
FT DNA_BIND 246..269
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593,
FT ECO:0000305|PubMed:2531226"
FT BINDING 8
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000269|PubMed:9103202,
FT ECO:0000305|PubMed:9367758, ECO:0007744|PDB:2ARC"
FT BINDING 24
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000269|PubMed:9103202,
FT ECO:0000305|PubMed:9367758, ECO:0007744|PDB:2ARC"
FT BINDING 38
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000269|PubMed:9103202,
FT ECO:0000305|PubMed:9367758, ECO:0007744|PDB:2ARC"
FT BINDING 82
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000269|PubMed:9103202,
FT ECO:0000305|PubMed:9367758, ECO:0007744|PDB:2ARC"
FT BINDING 93
FT /ligand="alpha-L-arabinopyanose"
FT /ligand_id="ChEBI:CHEBI:46987"
FT /evidence="ECO:0000269|PubMed:9103202,
FT ECO:0000305|PubMed:9367758, ECO:0007744|PDB:2ARC"
FT MUTAGEN 31
FT /note="Y->V: Eliminates the self-association, but does not
FT affect regulation properties of the protein."
FT /evidence="ECO:0000269|PubMed:17173282"
FT MUTAGEN 209
FT /note="S->A: Defective in DNA binding."
FT /evidence="ECO:0000269|PubMed:2531226"
FT MUTAGEN 213
FT /note="H->A,Y: Defective in DNA binding."
FT /evidence="ECO:0000269|PubMed:2531226"
FT MUTAGEN 257
FT /note="D->A: Does not bind DNA."
FT /evidence="ECO:0000269|PubMed:2531226"
FT MUTAGEN 258
FT /note="Q->A: Defective in DNA binding."
FT /evidence="ECO:0000269|PubMed:2531226"
FT MUTAGEN 262
FT /note="S->A: Does not affect DNA binding."
FT /evidence="ECO:0000269|PubMed:2531226"
FT CONFLICT 7
FT /note="D -> E (in Ref. 7; AAA23468)"
FT /evidence="ECO:0000305"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1XJA"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:2ARC"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2ARC"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2ARC"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:2ARC"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2ARC"
FT HELIX 148..166
FT /evidence="ECO:0007829|PDB:2ARC"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 223..241
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2K9S"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:2K9S"
SQ SEQUENCE 292 AA; 33384 MW; C5A737E285A4ECC6 CRC64;
MAEAQNDPLL PGYSFNAHLV AGLTPIEANG YLDFFIDRPL GMKGYILNLT IRGQGVVKNQ
GREFVCRPGD ILLFPPGEIH HYGRHPEARE WYHQWVYFRP RAYWHEWLNW PSIFANTGFF
RPDEAHQPHF SDLFGQIINA GQGEGRYSEL LAINLLEQLL LRRMEAINES LHPPMDNRVR
EACQYISDHL ADSNFDIASV AQHVCLSPSR LSHLFRQQLG ISVLSWREDQ RISQAKLLLS
TTRMPIATVG RNVGFDDQLY FSRVFKKCTG ASPSEFRAGC EEKVNDVAVK LS
