MODE_ECOLI
ID MODE_ECOLI Reviewed; 262 AA.
AC P0A9G8; P46930;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-binding transcriptional dual regulator ModE;
GN Name=modE {ECO:0000303|PubMed:8550508};
GN Synonyms=modR {ECO:0000303|PubMed:8564363};
GN OrderedLocusNames=b0761, JW0744;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=8564363; DOI=10.1016/s0944-5013(11)80016-9;
RA Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia
RT coli and modR, a regulatory gene.";
RL Microbiol. Res. 150:347-361(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, FUNCTION AS A
RP REPRESSOR, INDUCTION, MASS SPECTROMETRY, DNA-BINDING, AND MUTAGENESIS OF
RP ALA-76; THR-125 AND GLY-133.
RC STRAIN=K12 / BW545;
RX PubMed=8550508; DOI=10.1128/jb.178.3.735-744.1996;
RA Grunden A.M., Ray R.M., Rosentel J.K., Healy F.G., Shanmugam K.T.;
RT "Repression of the Escherichia coli modABCD (molybdate transport) operon by
RT ModE.";
RL J. Bacteriol. 178:735-744(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Kim K., Allen E., Araujo R., Aparicio A., Botstein D., Cherry M., Chung E.,
RA Dietrich F., Duncan M., Federspiel N., Kalman S., Komp C., Lashkari D.,
RA Lew H., Lin D., Namath A., Oefner P., Davis R.;
RT "Sequence spanning gap between Genbank entries L34009 and X69182.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 FUNCTION AS A REPRESSOR, INDUCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8931336; DOI=10.1016/0378-1097(96)00398-9;
RA McNicholas P.M., Chiang R.C., Gunsalus R.P.;
RT "The Escherichia coli modE gene: effect of modE mutations on molybdate
RT dependent modA expression.";
RL FEMS Microbiol. Lett. 145:117-123(1996).
RN [8]
RP FUNCTION AS A REPRESSOR, ACTIVITY REGULATION, SUBUNIT, AND DNA-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=9210473; DOI=10.1111/j.1432-1033.1997.00119.x;
RA Anderson L.A., Palmer T., Price N.C., Bornemann S., Boxer D.H., Pau R.N.;
RT "Characterisation of the molybdenum-responsive ModE regulatory protein and
RT its binding to the promoter region of the modABCD (molybdenum transport)
RT operon of Escherichia coli.";
RL Eur. J. Biochem. 246:119-126(1997).
RN [9]
RP FUNCTION AS A REPRESSOR, FUNCTION AS AN ACTIVATOR, ACTIVITY REGULATION, AND
RP DNA-BINDING.
RX PubMed=9044285; DOI=10.1046/j.1365-2958.1997.d01-1864.x;
RA McNicholas P.M., Rech S.A., Gunsalus R.P.;
RT "Characterization of the ModE DNA-binding sites in the control regions of
RT modABCD and moaABCDE of Escherichia coli.";
RL Mol. Microbiol. 23:515-524(1997).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9466267; DOI=10.1046/j.1365-2958.1998.00675.x;
RA McNicholas P.M., Chiang R.C., Gunsalus R.P.;
RT "Anaerobic regulation of the Escherichia coli dmsABC operon requires the
RT molybdate-responsive regulator ModE.";
RL Mol. Microbiol. 27:197-208(1998).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW545;
RX PubMed=10206709; DOI=10.1099/13500872-145-1-41;
RA Self W.T., Grunden A.M., Hasona A., Shanmugam K.T.;
RT "Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli
RT in response to molybdenum: ModE-molybdate, a repressor of the modABCD
RT (molybdate transport) operon is a secondary transcriptional activator for
RT the hyc and nar operons.";
RL Microbiology 145:41-55(1999).
RN [12]
RP FUNCTION, REGULON, AND DNA-BINDING.
RX PubMed=16205910; DOI=10.1007/s00203-005-0039-7;
RA Tao H., Hasona A., Do P.M., Ingram L.O., Shanmugam K.T.;
RT "Global gene expression analysis revealed an unsuspected deo operon under
RT the control of molybdate sensor, ModE protein, in Escherichia coli.";
RL Arch. Microbiol. 184:225-233(2005).
RN [13] {ECO:0007744|PDB:1B9M, ECO:0007744|PDB:1B9N}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND DOMAIN.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=10075916; DOI=10.1093/emboj/18.6.1435;
RA Hall D.R., Gourley D.G., Leonard G.A., Duke E.M.H., Anderson L.A.,
RA Boxer D.H., Hunter W.N.;
RT "The high-resolution crystal structure of the molybdate-dependent
RT transcriptional regulator (ModE) from Escherichia coli: a novel combination
RT of domain folds.";
RL EMBO J. 18:1435-1446(1999).
RN [14] {ECO:0007744|PDB:1H9R, ECO:0007744|PDB:1H9S}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 123-262 IN COMPLEX WITH
RP MOLYBDATE, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=11259434; DOI=10.1074/jbc.m100919200;
RA Gourley D.G., Schuttelkopf A.W., Anderson L.A., Price N.C., Boxer D.H.,
RA Hunter W.N.;
RT "Oxyanion binding alters conformation and quaternary structure of the c-
RT terminal domain of the transcriptional regulator mode. Implications for
RT molybdate-dependent regulation, signaling, storage, and transport.";
RL J. Biol. Chem. 276:20641-20647(2001).
RN [15] {ECO:0007744|PDB:1O7L}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH MOLYBDATE, ACTIVITY
RP REGULATION, AND DOMAIN.
RX PubMed=12581638; DOI=10.1016/s0022-2836(02)01358-x;
RA Schuttelkopf A.W., Boxer D.H., Hunter W.N.;
RT "Crystal structure of activated ModE reveals conformational changes
RT involving both oxyanion and DNA-binding domains.";
RL J. Mol. Biol. 326:761-767(2003).
CC -!- FUNCTION: Functions as an intracellular molybdate sensor. The ModE-Mo
CC complex acts as a repressor of the modABC operon, which is involved in
CC the transport of molybdate (PubMed:8550508). Binds modA promoter DNA in
CC the absence of molybdate, however molybdate binding confers increased
CC DNA affinity (PubMed:9210473, PubMed:9044285). Binds the promoter of
CC moaA activating its transcription; binding is not enhanced by molybdate
CC (PubMed:9044285). The protein dimer binds the consensus palindrome
CC sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3'
CC (PubMed:9210473, PubMed:9044285, PubMed:16205910). Acts as a regulator
CC of the expression of 67 genes, many of which encode molybdoenzymes,
CC acts both directly and indirectly (PubMed:9466267, PubMed:10206709,
CC PubMed:16205910). ModE also binds tungstate (PubMed:9210473,
CC PubMed:11259434). {ECO:0000269|PubMed:10206709,
CC ECO:0000269|PubMed:11259434, ECO:0000269|PubMed:16205910,
CC ECO:0000269|PubMed:8550508, ECO:0000269|PubMed:9044285,
CC ECO:0000269|PubMed:9210473, ECO:0000269|PubMed:9466267}.
CC -!- ACTIVITY REGULATION: The ModE dimer binds two molecules of molybdate
CC (MoO4(2-)) with a Kd of 0.8 uM, which results in major changes in the
CC conformation of the DNA-binding domain and confers high-affinity DNA-
CC binding to the transcription factor (PubMed:9210473, PubMed:9044285,
CC PubMed:11259434, PubMed:12581638). Additionally molybdate binding moves
CC the 2 Mop domains closer together, trapping the ligand between them
CC (PubMed:12581638). Can also bind tungstate (PubMed:9210473,
CC PubMed:11259434). Molybdate is bound at the dimer interface using
CC residues from each monomer (PubMed:11259434, PubMed:12581638).
CC {ECO:0000269|PubMed:11259434, ECO:0000269|PubMed:12581638,
CC ECO:0000269|PubMed:9044285, ECO:0000269|PubMed:9210473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9210473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9210473}.
CC -!- INDUCTION: Constitutively expressed at low levels; probably part of the
CC modE-modF operon (PubMed:8564363, PubMed:8931336) (Probable). Does not
CC seem to be autoregulated (PubMed:8931336). {ECO:0000269|PubMed:8564363,
CC ECO:0000269|PubMed:8931336, ECO:0000305|PubMed:8550508}.
CC -!- DOMAIN: Deletion of the C-terminus (from residues 122 on) results in
CC constitutive repression of modA (PubMed:8931336). Contains two major
CC domains: the N-terminal domain I forms a winged helix-turn-helix motif
CC and interacts with DNA (Probable). The C-terminal domain II is the
CC olybdate-binding component and contains a tandem repeat of the Mop
CC domain, each of which forms a beta-barrel (Probable) (PubMed:12581638).
CC The N-terminal domain plays a major role in the dimerization of the
CC protein whereas the C-terminal domain contributes to the stability of
CC the complex (Probable). {ECO:0000269|PubMed:12581638,
CC ECO:0000269|PubMed:8931336, ECO:0000305|PubMed:10075916,
CC ECO:0000305|PubMed:12581638}.
CC -!- MASS SPECTROMETRY: Mass=28271; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8550508};
CC -!- DISRUPTION PHENOTYPE: Loss of repression of the modABC operon
CC (PubMed:8564363, PubMed:8931336). Not essential for molybdopterin
CC cofactor synthesis (PubMed:8931336). Increased dmsA expression under
CC aerobic conditions and reduced expression under anaerobic conditions
CC (PubMed:9466267). Decreased expression of hyc and narG
CC (PubMed:10206709). {ECO:0000269|PubMed:10206709,
CC ECO:0000269|PubMed:8564363, ECO:0000269|PubMed:8931336,
CC ECO:0000269|PubMed:9466267}.
CC -!- SIMILARITY: Belongs to the ModE family. {ECO:0000305}.
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DR EMBL; U07867; AAB06892.1; -; Genomic_DNA.
DR EMBL; U27192; AAB60175.1; -; Genomic_DNA.
DR EMBL; U34275; AAA77051.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73848.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35425.1; -; Genomic_DNA.
DR PIR; JC6037; JC6037.
DR RefSeq; NP_415282.1; NC_000913.3.
DR RefSeq; WP_001147439.1; NZ_SSZK01000002.1.
DR PDB; 1B9M; X-ray; 1.75 A; A/B=1-262.
DR PDB; 1B9N; X-ray; 2.09 A; A/B=1-262.
DR PDB; 1H9R; X-ray; 1.90 A; A/B=124-262.
DR PDB; 1H9S; X-ray; 1.82 A; A/B=124-262.
DR PDB; 1O7L; X-ray; 2.75 A; A/B/C/D=1-262.
DR PDBsum; 1B9M; -.
DR PDBsum; 1B9N; -.
DR PDBsum; 1H9R; -.
DR PDBsum; 1H9S; -.
DR PDBsum; 1O7L; -.
DR AlphaFoldDB; P0A9G8; -.
DR SMR; P0A9G8; -.
DR BioGRID; 4259327; 4.
DR BioGRID; 849742; 1.
DR ComplexPortal; CPX-2115; modE transcription regulation complex.
DR DIP; DIP-10238N; -.
DR IntAct; P0A9G8; 1.
DR STRING; 511145.b0761; -.
DR jPOST; P0A9G8; -.
DR PaxDb; P0A9G8; -.
DR PRIDE; P0A9G8; -.
DR EnsemblBacteria; AAC73848; AAC73848; b0761.
DR EnsemblBacteria; BAA35425; BAA35425; BAA35425.
DR GeneID; 66670968; -.
DR GeneID; 945366; -.
DR KEGG; ecj:JW0744; -.
DR KEGG; eco:b0761; -.
DR PATRIC; fig|1411691.4.peg.1517; -.
DR EchoBASE; EB3017; -.
DR eggNOG; COG2005; Bacteria.
DR eggNOG; COG3585; Bacteria.
DR HOGENOM; CLU_087839_0_0_6; -.
DR InParanoid; P0A9G8; -.
DR OMA; SYKTAWH; -.
DR PhylomeDB; P0A9G8; -.
DR BioCyc; EcoCyc:MON0-185; -.
DR EvolutionaryTrace; P0A9G8; -.
DR PRO; PR:P0A9G8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990198; C:ModE complex; IPI:ComplexPortal.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR016462; ModE.
DR InterPro; IPR003725; ModE-bd_N.
DR InterPro; IPR004606; Mop_domain.
DR InterPro; IPR005116; Transp-assoc_OB_typ1.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03459; TOBE; 2.
DR PIRSF; PIRSF005763; Txn_reg_ModE; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50331; SSF50331; 2.
DR TIGRFAMs; TIGR00637; ModE_repress; 1.
DR TIGRFAMs; TIGR00638; Mop; 1.
DR PROSITE; PS51866; MOP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Metal-binding; Molybdenum; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..262
FT /note="DNA-binding transcriptional dual regulator ModE"
FT /id="PRO_0000201125"
FT DOMAIN 124..191
FT /note="Mop 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT DOMAIN 196..260
FT /note="Mop 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT DNA_BIND 33..79
FT /note="H-T-H motif"
FT REGION 1..121
FT /note="I"
FT /evidence="ECO:0000305|PubMed:10075916"
FT REGION 125..133
FT /note="Required for dimer formation and molybdate binding"
FT BINDING 126
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT BINDING 128
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT BINDING 163
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT BINDING 166
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT BINDING 183
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT BINDING 184
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000269|PubMed:11259434,
FT ECO:0000269|PubMed:12581638, ECO:0007744|PDB:1H9S,
FT ECO:0007744|PDB:1O7L"
FT MUTAGEN 76
FT /note="A->V: Partial loss of repression by ModE."
FT /evidence="ECO:0000269|PubMed:8550508"
FT MUTAGEN 125
FT /note="T->I: Transcription repression by ModE even in the
FT absence of molybdate."
FT /evidence="ECO:0000269|PubMed:8550508"
FT MUTAGEN 133
FT /note="G->D: Transcription repression by ModE even in the
FT absence of molybdate."
FT /evidence="ECO:0000269|PubMed:8550508"
FT MUTAGEN 216..262
FT /note="Missing: Transcription repression by ModE even in
FT the absence of molybdate."
FT /evidence="ECO:0000269|PubMed:8550508"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 80..105
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 123..135
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 199..212
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1B9M"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1H9S"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1B9M"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1B9M"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1B9M"
SQ SEQUENCE 262 AA; 28281 MW; 9A17636162F4233E CRC64;
MQAEILLTLK LQQKLFADPR RISLLKHIAL SGSISQGAKD AGISYKSAWD AINEMNQLSE
HILVERATGG KGGGGAVLTR YGQRLIQLYD LLAQIQQKAF DVLSDDDALP LNSLLAAISR
FSLQTSARNQ WFGTITARDH DDVQQHVDVL LADGKTRLKV AITAQSGARL GLDEGKEVLI
LLKAPWVGIT QDEAVAQNAD NQLPGIISHI ERGAEQCEVL MALPDGQTLC ATVPVNEATS
LQQGQNVTAY FNADSVIIAT LC
