ID MLC_ECOLI Reviewed; 406 AA.
AC P50456; P77593;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=DNA-binding transcriptional repressor Mlc {ECO:0000305};
DE AltName: Full=Making large colonies protein {ECO:0000303|PubMed:7766024};
DE AltName: Full=Membrane linked control {ECO:0000303|PubMed:11361067};
GN Name=mlc {ECO:0000303|PubMed:7766024};
GN Synonyms=dgsA {ECO:0000303|PubMed:9484892};
GN OrderedLocusNames=b1594, JW1586;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7766024; DOI=10.1271/bbb.59.256;
RA Hosono K., Kakuda H., Ichihara S.;
RT "Decreasing accumulation of acetate in a rich medium by Escherichia coli on
RT introduction of genes on a multicopy plasmid.";
RL Biosci. Biotechnol. Biochem. 59:256-261(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 FUNCTION.
RX PubMed=9484892; DOI=10.1046/j.1365-2958.1998.00685.x;
RA Plumbridge J.;
RT "Control of the expression of the manXYZ operon in Escherichia coli: Mlc is
RT a negative regulator of the mannose PTS.";
RL Mol. Microbiol. 27:369-380(1998).
RN [6]
RP FUNCTION, DNA-BINDING, TRANSCRIPTIONAL REGULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9484893; DOI=10.1046/j.1365-2958.1998.00694.x;
RA Decker K., Plumbridge J., Boos W.;
RT "Negative transcriptional regulation of a positive regulator: the
RT expression of malT, encoding the transcriptional activator of the maltose
RT regulon of Escherichia coli, is negatively controlled by Mlc.";
RL Mol. Microbiol. 27:381-390(1998).
RN [7]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=9781886; DOI=10.1046/j.1365-2958.1998.01035.x;
RA Kimata K., Inada T., Tagami H., Aiba H.;
RT "A global repressor (Mlc) is involved in glucose induction of the ptsG gene
RT encoding major glucose transporter in Escherichia coli.";
RL Mol. Microbiol. 29:1509-1519(1998).
RN [8]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=10464268; DOI=10.1074/jbc.274.36.25398;
RA Kim S.-Y., Nam T.-W., Shin D., Koo B.-M., Seok Y.-J., Ryu S.;
RT "Purification of Mlc and analysis of its effects on the PTS expression in
RT Escherichia coli.";
RL J. Biol. Chem. 274:25398-25402(1999).
RN [9]
RP ACTIVITY REGULATION, INTERACTION WITH DEPHOSPHORYLATED PTSG, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11032803; DOI=10.1093/emboj/19.20.5353;
RA Lee S.J., Boos W., Bouche J.P., Plumbridge J.;
RT "Signal transduction between a membrane-bound transporter, PtsG, and a
RT soluble transcription factor, Mlc, of Escherichia coli.";
RL EMBO J. 19:5353-5361(2000).
RN [10]
RP ACTIVITY REGULATION, AND INTERACTION WITH DEPHOSPHORYLATED PTSG.
RX PubMed=11157755; DOI=10.1093/emboj/20.3.491;
RA Nam T.W., Cho S.H., Shin D., Kim J.H., Jeong J.Y., Lee J.H., Roe J.H.,
RA Peterkofsky A., Kang S.O., Ryu S., Seok Y.J.;
RT "The Escherichia coli glucose transporter enzyme IICB(Glc) recruits the
RT global repressor Mlc.";
RL EMBO J. 20:491-498(2001).
RN [11]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11340070; DOI=10.1074/jbc.m101757200;
RA Shin D., Lim S., Seok Y.J., Ryu S.;
RT "Heat shock RNA polymerase (E sigma(32)) is involved in the transcription
RT of mlc and crucial for induction of the Mlc regulon by glucose in
RT Escherichia coli.";
RL J. Biol. Chem. 276:25871-25875(2001).
RN [12]
RP FUNCTION.
RX PubMed=11361067;
RA Plumbridge J.;
RT "Regulation of PTS gene expression by the homologous transcriptional
RT regulators, Mlc and NagC, in Escherichia coli (or how two similar
RT repressors can behave differently).";
RL J. Mol. Microbiol. Biotechnol. 3:371-380(2001).
RN [13]
RP FUNCTION, AND REVIEW.
RX PubMed=11934616; DOI=10.1016/s1369-5274(02)00296-5;
RA Plumbridge J.;
RT "Regulation of gene expression in the PTS in Escherichia coli: the role and
RT interactions of Mlc.";
RL Curr. Opin. Microbiol. 5:187-193(2002).
RN [14]
RP ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH DEPHOSPHORYLATED PTSG,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=12529317; DOI=10.1074/jbc.m212066200;
RA Seitz S., Lee S.J., Pennetier C., Boos W., Plumbridge J.;
RT "Analysis of the interaction between the global regulator Mlc and EIIBGlc
RT of the glucose-specific phosphotransferase system in Escherichia coli.";
RL J. Biol. Chem. 278:10744-10751(2003).
RN [15]
RP CRYSTALLIZATION OF MUTANT HIS-52, SUBUNIT, AND MUTAGENESIS OF ARG-52.
RX PubMed=16510988; DOI=10.1107/s1744309104033640;
RA Gerber K., Boos W., Welte W., Schiefner A.;
RT "Crystallization and preliminary X-ray analysis of Mlc from Escherichia
RT coli.";
RL Acta Crystallogr. F 61:183-185(2005).
RN [16]
RP INTERACTION WITH MTFA, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=16855233; DOI=10.1128/jb.00219-06;
RA Becker A.-K., Zeppenfeld T., Staab A., Seitz S., Boos W., Morita T.,
RA Aiba H., Mahr K., Titgemeyer F., Jahreis K.;
RT "YeeI, a novel protein involved in modulation of the activity of the
RT glucose-phosphotransferase system in Escherichia coli K-12.";
RL J. Bacteriol. 188:5439-5449(2006).
RN [17]
RP INTERACTION WITH MTFA, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-86.
RC STRAIN=K12;
RX PubMed=22178967; DOI=10.1128/jb.06387-11;
RA Goehler A.K., Staab A., Gabor E., Homann K., Klang E., Kosfeld A.,
RA Muus J.E., Wulftange J.S., Jahreis K.;
RT "Characterization of MtfA, a novel regulatory output signal protein of the
RT glucose-phosphotransferase system in Escherichia coli K-12.";
RL J. Bacteriol. 194:1024-1035(2012).
RN [18] {ECO:0007744|PDB:1Z6R}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZN(2+), SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF CYS-257 AND CYS-259.
RX PubMed=15929984; DOI=10.1074/jbc.m504215200;
RA Schiefner A., Gerber K., Seitz S., Welte W., Diederichs K., Boos W.;
RT "The crystal structure of Mlc, a global regulator of sugar metabolism in
RT Escherichia coli.";
RL J. Biol. Chem. 280:29073-29079(2005).
RN [19] {ECO:0007744|PDB:3BP8}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH PTSG EIIB DOMAIN AND
RP ZN(2+), DNA-BINDING, ACTIVITY REGULATION, INTERACTION WITH PTSG EIIB
RP DOMAIN, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF PHE-136;
RP ARG-306 AND LEU-310.
RX PubMed=18319344; DOI=10.1073/pnas.0709295105;
RA Nam T.W., Jung H.I., An Y.J., Park Y.H., Lee S.H., Seok Y.J., Cha S.S.;
RT "Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of
RT Mlc inactivation by membrane sequestration.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3751-3756(2008).
CC -!- FUNCTION: Global regulator of carbohydrate metabolism (PubMed:9484892,
CC PubMed:9484893, PubMed:9781886, PubMed:10464268, PubMed:11361067,
CC PubMed:11934616). Represses the expression of several genes involved in
CC sugar transport and utilization, in particular phosphoenolpyruvate-
CC carbohydrate phosphotransferase system (PTS) genes (PubMed:9484892,
CC PubMed:9484893, PubMed:9781886, PubMed:10464268). Represses expression
CC of ptsG (EIICB(Glc)), which encodes the PTS system glucose-specific
CC EIICB component (PubMed:9781886). Also represses the expression of the
CC manXYZ operon, encoding the mannose-specific PTS system, expression of
CC malT, encoding the transcriptional activator of the maltose regulon,
CC and expression of the pts operon, composed of the genes ptsH, ptsI and
CC crr (PubMed:9484892, PubMed:9484893, PubMed:10464268). Represses its
CC own expression (PubMed:9484893). Acts by binding to the regulatory
CC region of the target genes (PubMed:9484893, PubMed:9781886,
CC PubMed:10464268). {ECO:0000269|PubMed:10464268,
CC ECO:0000269|PubMed:11361067, ECO:0000269|PubMed:11934616,
CC ECO:0000269|PubMed:9484892, ECO:0000269|PubMed:9484893,
CC ECO:0000269|PubMed:9781886}.
CC -!- ACTIVITY REGULATION: Activity is modulated by glucose (PubMed:9781886,
CC PubMed:10464268). In the presence of glucose, is inhibited by
CC interaction with the dephosphorylated form of PtsG, which sequesters
CC Mlc in the inner membrane and prevents Mlc binding to its target
CC promoters (PubMed:11032803, PubMed:11157755, PubMed:12529317,
CC PubMed:18319344). The restriction of conformational freedom resulting
CC from the anchoring of four ends of Mlc to the membrane could be the
CC primary cause of its loss of DNA-binding activity in vivo
CC (PubMed:18319344). Activity is also inhibited by interaction with the
CC Mlc titration factor A (mtfA) (PubMed:16855233, PubMed:22178967). The
CC inactivation mechanisms of Mlc by dephosphorylated PtsG and MtfA differ
CC significantly (PubMed:22178967). {ECO:0000269|PubMed:10464268,
CC ECO:0000269|PubMed:11032803, ECO:0000269|PubMed:11157755,
CC ECO:0000269|PubMed:12529317, ECO:0000269|PubMed:16855233,
CC ECO:0000269|PubMed:18319344, ECO:0000269|PubMed:22178967,
CC ECO:0000269|PubMed:9781886}.
CC -!- SUBUNIT: Homodimer (PubMed:15929984). Homotetramer (PubMed:16510988,
CC PubMed:12529317, PubMed:15929984, PubMed:18319344). There is probably
CC an equilibrium between the dimeric and the tetrameric form
CC (PubMed:15929984). Interacts with dephosphorylated PtsG
CC (PubMed:11032803, PubMed:11157755, PubMed:12529317, PubMed:18319344).
CC Mlc and PtsG EIIB domain form a complex with the 1:1 stoichiometry
CC (PubMed:18319344). Interacts with MtfA (PubMed:16855233,
CC PubMed:22178967). {ECO:0000269|PubMed:11032803,
CC ECO:0000269|PubMed:11157755, ECO:0000269|PubMed:12529317,
CC ECO:0000269|PubMed:15929984, ECO:0000269|PubMed:16510988,
CC ECO:0000269|PubMed:16855233, ECO:0000269|PubMed:18319344,
CC ECO:0000269|PubMed:22178967}.
CC -!- INTERACTION:
CC P50456; P50456: mlc; NbExp=2; IntAct=EBI-1116104, EBI-1116104;
CC P50456; P76346: mtfA; NbExp=2; IntAct=EBI-1116104, EBI-1126682;
CC P50456; P69786: ptsG; NbExp=3; IntAct=EBI-1116104, EBI-903497;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Interaction with
CC dephosphorylated PtsG leads to the sequestration of Mlc in the inner
CC membrane fraction. {ECO:0000269|PubMed:11032803,
CC ECO:0000269|PubMed:12529317, ECO:0000269|PubMed:18319344}.
CC -!- INDUCTION: Expression is modulated by the cAMP-CRP complex
CC (PubMed:11340070). Negatively autoregulated (PubMed:9484893,
CC PubMed:11340070). cAMP-CRP and Mlc work together to maintain the level
CC of Mlc optimum in response to availability of glucose
CC (PubMed:11340070). Weakly repressed by NagC (PubMed:9484893).
CC Transcription is induced by heat shock via the sigma-32 factor (rpoH)
CC (PubMed:11340070). {ECO:0000269|PubMed:11340070,
CC ECO:0000269|PubMed:9484893}.
CC -!- DOMAIN: Is composed of three domains: a helix-turn-helix (HTH) DNA-
CC binding domain, a PtsG-binding domain and an oligomerization domain
CC (PubMed:12529317, PubMed:15929984, PubMed:18319344). The zinc ion
CC probably plays an important structural role for the correct orientation
CC of the HTH domain (PubMed:15929984). {ECO:0000269|PubMed:12529317,
CC ECO:0000269|PubMed:15929984, ECO:0000269|PubMed:18319344}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to a threefold
CC increase in malT expression (PubMed:9484893). Disruption also causes
CC the constitutive expression of ptsG (PubMed:9781886).
CC {ECO:0000269|PubMed:9484893, ECO:0000269|PubMed:9781886}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D32222; BAA06978.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74666.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15318.1; -; Genomic_DNA.
DR PIR; D64915; D64915.
DR RefSeq; NP_416111.1; NC_000913.3.
DR RefSeq; WP_000225262.1; NZ_SSZK01000001.1.
DR PDB; 1Z6R; X-ray; 2.70 A; A/B/C/D=1-406.
DR PDB; 3BP8; X-ray; 2.85 A; A/B=1-406.
DR PDBsum; 1Z6R; -.
DR PDBsum; 3BP8; -.
DR AlphaFoldDB; P50456; -.
DR SMR; P50456; -.
DR BioGRID; 4259119; 157.
DR ComplexPortal; CPX-2242; mlc-EIIB transcriptional regulator complex.
DR DIP; DIP-10219N; -.
DR IntAct; P50456; 9.
DR STRING; 511145.b1594; -.
DR jPOST; P50456; -.
DR PaxDb; 511145-b1594; -.
DR EnsemblBacteria; AAC74666; AAC74666; b1594.
DR GeneID; 945510; -.
DR KEGG; ecj:JW1586; -.
DR KEGG; eco:b1594; -.
DR PATRIC; fig|1411691.4.peg.668; -.
DR EchoBASE; EB2950; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_13_1_6; -.
DR InParanoid; P50456; -.
DR OMA; FFIRHQQ; -.
DR OrthoDB; 3189808at2; -.
DR PhylomeDB; P50456; -.
DR BioCyc; EcoCyc:PD01896; -.
DR EvolutionaryTrace; P50456; -.
DR PRO; PR:P50456; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; TAS:EcoCyc.
DR GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR18964:SF176; PROTEIN MLC; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; DNA-binding;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..406
FT /note="DNA-binding transcriptional repressor Mlc"
FT /id="PRO_0000095690"
FT DNA_BIND 33..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15929984,
FT ECO:0000269|PubMed:18319344, ECO:0007744|PDB:1Z6R,
FT ECO:0007744|PDB:3BP8"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15929984,
FT ECO:0000269|PubMed:18319344, ECO:0007744|PDB:1Z6R,
FT ECO:0007744|PDB:3BP8"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15929984,
FT ECO:0000269|PubMed:18319344, ECO:0007744|PDB:1Z6R,
FT ECO:0007744|PDB:3BP8"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15929984,
FT ECO:0000269|PubMed:18319344, ECO:0007744|PDB:1Z6R,
FT ECO:0007744|PDB:3BP8"
FT MUTAGEN 52
FT /note="R->H: Shows increased expression and forms larger
FT colonies."
FT /evidence="ECO:0000269|PubMed:16510988"
FT MUTAGEN 86
FT /note="H->R: Can be bound and inactivated by MtfA."
FT /evidence="ECO:0000269|PubMed:22178967"
FT MUTAGEN 136
FT /note="F->A: Decreases association with PtsG EIIB domain."
FT /evidence="ECO:0000269|PubMed:18319344"
FT MUTAGEN 257
FT /note="C->A: Strongly reduced activity; when associated
FT with A-259."
FT /evidence="ECO:0000269|PubMed:15929984"
FT MUTAGEN 257
FT /note="C->S: Strongly reduced activity; when associated
FT with S-259."
FT /evidence="ECO:0000269|PubMed:15929984"
FT MUTAGEN 259
FT /note="C->A: Strongly reduced activity; when associated
FT with A-257."
FT /evidence="ECO:0000269|PubMed:15929984"
FT MUTAGEN 259
FT /note="C->S: Strongly reduced activity; when associated
FT with S-257."
FT /evidence="ECO:0000269|PubMed:15929984"
FT MUTAGEN 306
FT /note="R->G: Forms dimers but not tetramers; when
FT associated with G-310."
FT /evidence="ECO:0000269|PubMed:18319344"
FT MUTAGEN 310
FT /note="L->G: Forms dimers but not tetramers; when
FT associated with G-306."
FT /evidence="ECO:0000269|PubMed:18319344"
FT CONFLICT 179
FT /note="G -> A (in Ref. 1; BAA06978)"
FT /evidence="ECO:0000305"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 213..230
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 309..333
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1Z6R"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1Z6R"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:1Z6R"
FT HELIX 398..403
FT /evidence="ECO:0007829|PDB:1Z6R"
SQ SEQUENCE 406 AA; 44316 MW; 423608797FC980CB CRC64;
MVAENQPGHI DQIKQTNAGA VYRLIDQLGP VSRIDLSRLA QLAPASITKI VREMLEAHLV
QELEIKEAGN RGRPAVGLVV ETEAWHYLSL RISRGEIFLA LRDLSSKLVV EESQELALKD
DLPLLDRIIS HIDQFFIRHQ KKLERLTSIA ITLPGIIDTE NGIVHRMPFY EDVKEMPLGE
ALEQHTGVPV YIQHDISAWT MAEALFGASR GARDVIQVVI DHNVGAGVIT DGHLLHAGSS
SLVEIGHTQV DPYGKRCYCG NHGCLETIAS VDSILELAQL RLNQSMSSML HGQPLTVDSL
CQAALRGDLL AKDIITGVGA HVGRILAIMV NLFNPQKILI GSPLSKAADI LFPVISDSIR
QQALPAYSQH ISVESTQFSN QGTMAGAALV KDAMYNGSLL IRLLQG
//
