PTGA_ECOLI
ID PTGA_ECOLI Reviewed; 169 AA.
AC P69783; P08837; Q47703;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PTS system glucose-specific EIIA component {ECO:0000303|PubMed:2457575};
DE AltName: Full=EIIA-Glc {ECO:0000303|PubMed:2457575};
DE AltName: Full=EIII-Glc {ECO:0000303|PubMed:2457575};
DE AltName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:3129430};
GN Name=crr {ECO:0000303|PubMed:2960675}; Synonyms=gsr, iex, tgs, treD;
GN OrderedLocusNames=b2417, JW2410;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2457575; DOI=10.1128/jb.170.9.3827-3837.1988;
RA de Reuse H., Danchin A.;
RT "The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-
RT dependent phosphotransferase system: a complex operon with several modes of
RT transcription.";
RL J. Bacteriol. 170:3827-3837(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2960675; DOI=10.1016/s0021-9258(18)47721-6;
RA Saffen D.W., Presper K.A., Doering T.L., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. Molecular
RT cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr
RT genes.";
RL J. Biol. Chem. 262:16241-16253(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8764513; DOI=10.1111/j.1574-6968.1996.tb08368.x;
RA Yang Y., Zhao G., Winkler M.E.;
RT "Identification of the pdxK gene that encodes pyridoxine (vitamin B6)
RT kinase in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 141:89-95(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Various ECOR strains;
RX PubMed=1630305; DOI=10.1093/oxfordjournals.molbev.a040751;
RA Hall B.G., Sharp P.M.;
RT "Molecular population genetics of Escherichia coli: DNA sequence diversity
RT at the celC, crr, and gutB loci of natural isolates.";
RL Mol. Biol. Evol. 9:654-665(1992).
RN [5]
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 [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-21.
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 [9]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=789369; DOI=10.1016/s0021-9258(17)32988-5;
RA Saier M.H. Jr., Roseman S.;
RT "Sugar transport. The crr mutation: its effect on repression of enzyme
RT synthesis.";
RL J. Biol. Chem. 251:6598-6605(1976).
RN [12]
RP ACTIVE SITE.
RX PubMed=6383826; DOI=10.1111/j.1432-1033.1984.tb08438.x;
RA Doerschug M., Frank R., Kalbitzer H.R., Hengstenberg W., Deutscher J.;
RT "Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the
RT Escherichia coli phosphotransferase system.";
RL Eur. J. Biochem. 144:113-119(1984).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3129430; DOI=10.1016/s0021-9258(18)68691-0;
RA Nuoffer C., Zanolari B., Erni B.;
RT "Glucose permease of Escherichia coli. The effect of cysteine to serine
RT mutations on the function, stability, and regulation of transport and
RT phosphorylation.";
RL J. Biol. Chem. 263:6647-6655(1988).
RN [14]
RP FUNCTION, MUTAGENESIS OF PHE-4; HIS-76 AND HIS-91, ACTIVE SITE, COFACTOR,
RP AND PHOSPHORYLATION AT HIS-91.
RX PubMed=2657735; DOI=10.1073/pnas.86.11.4052;
RA Presper K.A., Wong C.Y., Liu L., Meadow N.D., Roseman S.;
RT "Site-directed mutagenesis of the phosphocarrier protein. IIIGlc, a major
RT signal-transducing protein in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4052-4055(1989).
RN [15]
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 [16]
RP FUNCTION.
RX PubMed=17158705; DOI=10.1128/mmbr.00024-06;
RA Deutscher J., Francke C., Postma P.W.;
RT "How phosphotransferase system-related protein phosphorylation regulates
RT carbohydrate metabolism in bacteria.";
RL Microbiol. Mol. Biol. Rev. 70:939-1031(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), ACTIVE SITE, AND COFACTOR.
RX PubMed=1961703; DOI=10.1073/pnas.88.23.10382;
RA Worthylake D., Meadow N.D., Roseman S., Liao D.-I., Herzberg O.,
RA Remington S.J.;
RT "Three-dimensional structure of the Escherichia coli phosphocarrier protein
RT IIIglc.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10382-10386(1991).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLYCEROL KINASE, AND
RP SUBUNIT.
RX PubMed=8430315; DOI=10.1126/science.8430315;
RA Hurley J.H., Faber H.R., Worthylake D., Meadow N.D., Roseman S.,
RA Pettigrew D.W., Remington S.J.;
RT "Structure of the regulatory complex of Escherichia coli IIIGlc with
RT glycerol kinase.";
RL Science 259:673-677(1993).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 2-169 IN COMPLEX WITH GLYCEROL
RP KINASE AND ZINC ION, COFACTOR, AND SUBUNIT.
RX PubMed=8170944; DOI=10.1073/pnas.91.9.3544;
RA Feese M., Pettigrew D.W., Meadow N.D., Roseman S., Remington S.J.;
RT "Cation-promoted association of a regulatory and target protein is
RT controlled by protein phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3544-3548(1994).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 9-169 IN COMPLEX WITH ZINC ION,
RP COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX PubMed=9405042; DOI=10.1021/bi971999e;
RA Feese M.D., Comolli L., Meadow N.D., Roseman S., Remington S.J.;
RT "Structural studies of the Escherichia coli signal transducing protein
RT IIAGlc: implications for target recognition.";
RL Biochemistry 36:16087-16096(1997).
RN [21]
RP STRUCTURE BY NMR.
RX PubMed=1911770; DOI=10.1021/bi00105a032;
RA Pelton J.G., Torchia D.A., Meadow N.D., Wong C.Y., Roseman S.;
RT "1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing
RT protein of Escherichia coli, using three-dimensional triple-resonance
RT techniques.";
RL Biochemistry 30:10043-10057(1991).
RN [22]
RP STRUCTURE BY NMR.
RX PubMed=2014267; DOI=10.1073/pnas.88.8.3479;
RA Pelton J.G., Torchia D.A., Meadow N.D., Wong C.-Y., Roseman S.;
RT "Secondary structure of the phosphocarrier protein IIIGlc, a signal-
RT transducing protein from Escherichia coli, determined by heteronuclear
RT three-dimensional NMR spectroscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3479-3483(1991).
RN [23]
RP STRUCTURE BY NMR.
RX PubMed=1606145; DOI=10.1021/bi00137a017;
RA Pelton J.G., Torchia D.A., Meadow N.D., Roseman S.;
RT "Structural comparison of phosphorylated and unphosphorylated forms of
RT IIIGlc, a signal-transducing protein from Escherichia coli, using three-
RT dimensional NMR techniques.";
RL Biochemistry 31:5215-5224(1992).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane
CC (PubMed:3129430, PubMed:17158705). The enzyme II complex composed of
CC PtsG and Crr is involved in glucose transport (PubMed:2657735). The
CC non-phosphorylated EIII-Glc is an inhibitor for uptake of certain
CC sugars such as maltose, melibiose, lactose, and glycerol.
CC Phosphorylated EIII-Glc, however, may be an activator for adenylate
CC cyclase. It is an important regulatory protein for cell metabolism
CC (PubMed:789369). {ECO:0000269|PubMed:2657735,
CC ECO:0000269|PubMed:3129430, ECO:0000269|PubMed:789369,
CC ECO:0000305|PubMed:17158705}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:9405042};
CC Note=Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion
CC is important for dimerization. {ECO:0000269|PubMed:8170944};
CC -!- SUBUNIT: Heterodimer with glycerol kinase (glpk).
CC {ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315,
CC ECO:0000305|PubMed:9405042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00416}.
CC -!- DISRUPTION PHENOTYPE: In mutants defective in enzyme I and histidine-
CC containing phosphate carrier protein (HPr), cells lacking this gene are
CC able to grow on the non-PTS compounds such as glycerol, maltose,
CC melibiose, mannose 6-phosphate, and alpha-glycerol phosphate.
CC {ECO:0000269|PubMed:789369}.
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DR EMBL; J02796; AAA24442.1; -; Genomic_DNA.
DR EMBL; M21994; AAA24386.1; -; Genomic_DNA.
DR EMBL; M93578; AAA23602.1; -; Genomic_DNA.
DR EMBL; M93579; AAA23605.1; -; Genomic_DNA.
DR EMBL; M93580; AAA23603.1; -; Genomic_DNA.
DR EMBL; M93581; AAA23606.1; -; Genomic_DNA.
DR EMBL; M93582; AAA23604.1; -; Genomic_DNA.
DR EMBL; M93584; AAA23610.1; -; Genomic_DNA.
DR EMBL; M93587; AAA23612.1; -; Genomic_DNA.
DR EMBL; M93594; AAA23607.1; -; Genomic_DNA.
DR EMBL; M93595; AAA23608.1; -; Genomic_DNA.
DR EMBL; M93596; AAA23611.1; -; Genomic_DNA.
DR EMBL; M93597; AAA23609.1; -; Genomic_DNA.
DR EMBL; M93598; AAA23613.1; -; Genomic_DNA.
DR EMBL; U53700; AAC44167.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75470.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16291.1; -; Genomic_DNA.
DR PIR; C29785; WQECP3.
DR RefSeq; NP_416912.1; NC_000913.3.
DR RefSeq; WP_000522247.1; NZ_STEB01000039.1.
DR PDB; 1F3G; X-ray; 2.10 A; A=9-169.
DR PDB; 1F3Z; X-ray; 1.98 A; A=9-169.
DR PDB; 1GGR; NMR; -; A=2-169.
DR PDB; 1GLA; X-ray; 2.60 A; F=2-169.
DR PDB; 1GLB; X-ray; 2.60 A; F=2-169.
DR PDB; 1GLC; X-ray; 2.65 A; F=2-169.
DR PDB; 1GLD; X-ray; 2.93 A; F=2-169.
DR PDB; 1GLE; X-ray; 2.94 A; F=2-169.
DR PDB; 1O2F; NMR; -; A=2-169.
DR PDB; 2F3G; X-ray; 2.13 A; A/B=2-169.
DR PDB; 2MP0; NMR; -; B=2-169.
DR PDB; 4JBW; X-ray; 3.91 A; M/N/O/P=1-169.
DR PDBsum; 1F3G; -.
DR PDBsum; 1F3Z; -.
DR PDBsum; 1GGR; -.
DR PDBsum; 1GLA; -.
DR PDBsum; 1GLB; -.
DR PDBsum; 1GLC; -.
DR PDBsum; 1GLD; -.
DR PDBsum; 1GLE; -.
DR PDBsum; 1O2F; -.
DR PDBsum; 2F3G; -.
DR PDBsum; 2MP0; -.
DR PDBsum; 4JBW; -.
DR AlphaFoldDB; P69783; -.
DR BMRB; P69783; -.
DR SMR; P69783; -.
DR BioGRID; 4260572; 36.
DR ComplexPortal; CPX-1978; Enzyme IIA-maltose transport inhibitory complex.
DR ComplexPortal; CPX-5943; Glucose-specific enzyme II complex.
DR DIP; DIP-31863N; -.
DR IntAct; P69783; 5.
DR STRING; 511145.b2417; -.
DR TCDB; 4.A.1.1.1; the pts glucose-glucoside (glc) family.
DR iPTMnet; P69783; -.
DR SWISS-2DPAGE; P69783; -.
DR jPOST; P69783; -.
DR PaxDb; P69783; -.
DR PRIDE; P69783; -.
DR EnsemblBacteria; AAC75470; AAC75470; b2417.
DR EnsemblBacteria; BAA16291; BAA16291; BAA16291.
DR GeneID; 67416817; -.
DR GeneID; 946880; -.
DR KEGG; ecj:JW2410; -.
DR KEGG; eco:b2417; -.
DR PATRIC; fig|1411691.4.peg.4314; -.
DR EchoBASE; EB0163; -.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_5_1_6; -.
DR InParanoid; P69783; -.
DR OMA; HTKHAVG; -.
DR PhylomeDB; P69783; -.
DR BioCyc; EcoCyc:CRR-MON; -.
DR BioCyc; MetaCyc:CRR-MON; -.
DR BRENDA; 2.7.1.199; 2026.
DR EvolutionaryTrace; P69783; -.
DR PRO; PR:P69783; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990154; C:enzyme IIA-maltose transporter complex; IPI:ComplexPortal.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045912; P:negative regulation of carbohydrate metabolic process; IDA:EcoCyc.
DR GO; GO:1902344; P:negative regulation of maltose transport; IC:ComplexPortal.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; IC:ComplexPortal.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:ComplexPortal.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Kinase; Metal-binding;
KW Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|Ref.9"
FT CHAIN 2..169
FT /note="PTS system glucose-specific EIIA component"
FT /id="PRO_0000186532"
FT DOMAIN 39..143
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 91
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416,
FT ECO:0000269|PubMed:2657735, ECO:0000269|PubMed:6383826,
FT ECO:0000305|PubMed:1961703, ECO:0000305|PubMed:9405042"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with glycerol kinase"
FT /evidence="ECO:0000269|PubMed:2657735,
FT ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:9405042,
FT ECO:0000305|PubMed:1961703"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with glycerol kinase"
FT /evidence="ECO:0000269|PubMed:2657735,
FT ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:9405042,
FT ECO:0000305|PubMed:1961703"
FT SITE 76
FT /note="Important for phospho-donor activity"
FT /evidence="ECO:0000269|PubMed:2657735"
FT MOD_RES 91
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000269|PubMed:2657735"
FT MUTAGEN 4
FT /note="F->W: Same activity as the wild-type."
FT /evidence="ECO:0000269|PubMed:2657735"
FT MUTAGEN 76
FT /note="H->Q: Unable to transfer phosphoryl group."
FT /evidence="ECO:0000269|PubMed:2657735"
FT MUTAGEN 91
FT /note="H->Q: Unable to be phosphorylated by Hpr."
FT /evidence="ECO:0000269|PubMed:2657735"
FT CONFLICT 23..31
FT /note="Missing (in Ref. 3; AAC44167)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1GLC"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1F3Z"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1F3Z"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1GLA"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1F3Z"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1GLB"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1F3Z"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1F3Z"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1F3Z"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1F3G"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1F3Z"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1F3Z"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1F3Z"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1F3Z"
SQ SEQUENCE 169 AA; 18251 MW; EA18020745531215 CRC64;
MGLFDKLKSL VSDDKKDTGT IEIIAPLSGE IVNIEDVPDV VFAEKIVGDG IAIKPTGNKM
VAPVDGTIGK IFETNHAFSI ESDSGVELFV HFGIDTVELK GEGFKRIAEE GQRVKVGDTV
IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL IKLSGSVTVG ETPVIRIKK
