PT1_ECOLI
ID PT1_ECOLI Reviewed; 575 AA.
AC P08839;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:2960675};
DE EC=2.7.3.9 {ECO:0000269|PubMed:12705838};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:2960675};
GN Name=ptsI {ECO:0000303|PubMed:2960675}; OrderedLocusNames=b2416, JW2409;
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=2411636; DOI=10.1016/0378-1119(85)90172-6;
RA de Reuse H., Roy A., Danchin A.;
RT "Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide
RT sequence of the ptsH gene.";
RL Gene 35:199-207(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC STRAIN=K12;
RX PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT "DNA sequences of the cysK regions of Salmonella typhimurium and
RT Escherichia coli and linkage of the cysK regions to ptsH.";
RL J. Bacteriol. 170:3150-3157(1988).
RN [8]
RP PROTEIN SEQUENCE OF 1-11.
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 FUNCTION IN NITROGEN-METABOLIC PTS.
RX PubMed=7876255; DOI=10.1074/jbc.270.9.4822;
RA Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X.,
RA Reizer A., Saier M.H. Jr., Reizer J.;
RT "Novel proteins of the phosphotransferase system encoded within the rpoN
RT operon of Escherichia coli. Enzyme IIANtr affects growth on organic
RT nitrogen and the conditional lethality of an erats mutant.";
RL J. Biol. Chem. 270:4822-4839(1995).
RN [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP HIS-189 AND CYS-502, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, ACTIVE
RP SITE, AND SUBUNIT.
RX PubMed=12705838; DOI=10.1021/bi034007f;
RA Garcia-Alles L.F., Alfonso I., Erni B.;
RT "Enzyme I of the phosphotransferase system: induced-fit protonation of the
RT reaction transition state by Cys-502.";
RL Biochemistry 42:4744-4750(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-259.
RX PubMed=8805571; DOI=10.1016/s0969-2126(96)00092-5;
RA Liao D.-I., Silverton E., Seok Y.-J., Lee B.R., Peterkofsky A.,
RA Davies D.R.;
RT "The first step in sugar transport: crystal structure of the amino terminal
RT domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and
RT a model of the phosphotransfer complex with HPr.";
RL Structure 4:861-872(1996).
RN [13]
RP STRUCTURE BY NMR OF 1-259.
RX PubMed=9054557; DOI=10.1021/bi962924y;
RA Garrett D.S., Seok Y.-J., Liao D.-I., Peterkofsky A., Gronenborn A.M.,
RA Clore G.M.;
RT "Solution structure of the 30 kDa N-terminal domain of enzyme I of the
RT Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by
RT multidimensional NMR.";
RL Biochemistry 36:2517-2530(1997).
RN [14]
RP STRUCTURE BY NMR OF 1-259.
RX PubMed=9541412; DOI=10.1002/pro.5560070329;
RA Garrett D.S., Seok Y.-J., Peterkofsky A., Clore G.M., Gronenborn A.M.;
RT "Tautomeric state and pKa of the phosphorylated active site histidine in
RT the N-terminal domain of enzyme I of the Escherichia coli
RT phosphoenolpyruvate:sugar phosphotransferase system.";
RL Protein Sci. 7:789-793(1998).
RN [15]
RP STRUCTURE BY NMR OF 1-259.
RX PubMed=10048929; DOI=10.1038/5854;
RA Garrett D.S., Seok Y.-J., Peterkofsky A., Gronenborn A.M., Clore G.M.;
RT "Solution structure of the 40,000 Mr phosphoryl transfer complex between
RT the N-terminal domain of enzyme I and HPr.";
RL Nat. Struct. Biol. 6:166-173(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP MAGNESIUM IONS, FUNCTION, COFACTOR, SUBUNIT, ACTIVE SITE, AND REACTION
RP MECHANISM.
RX PubMed=17053069; DOI=10.1073/pnas.0607587103;
RA Teplyakov A., Lim K., Zhu P.-P., Kapadia G., Chen C.C.H., Schwartz J.,
RA Howard A., Reddy P.T., Peterkofsky A., Herzberg O.;
RT "Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar
RT phosphotransferase system sugar translocation signal protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16218-16223(2006).
CC -!- FUNCTION: General (non sugar-specific) component of the
CC phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar
CC PTS). This major carbohydrate active-transport system catalyzes the
CC phosphorylation of incoming sugar substrates concomitantly with their
CC translocation across the cell membrane. Enzyme I transfers the
CC phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl
CC carrier protein (HPr) (PubMed:7876255, PubMed:12705838,
CC PubMed:17053069). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-
CC PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP)
CC as alternative phosphoryl donors (PubMed:12705838).
CC {ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069,
CC ECO:0000269|PubMed:7876255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000269|PubMed:12705838};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17053069};
CC -!- ACTIVITY REGULATION: Inhibited by oxalate.
CC {ECO:0000269|PubMed:12705838}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for ZFPEP {ECO:0000269|PubMed:12705838};
CC KM=0.12 mM for EClPEP {ECO:0000269|PubMed:12705838};
CC KM=0.14 mM for PEP {ECO:0000269|PubMed:12705838};
CC KM=0.25 mM for ZClPEP {ECO:0000269|PubMed:12705838};
CC KM=0.43 mM for ZMePEP {ECO:0000269|PubMed:12705838};
CC Note=kcat is 3830 min(-1) with PEP as substrate. kcat is 370 min(-1)
CC with ZFPEP as substrate. kcat is 285 min(-1) with ZMePEP as
CC substrate. kcat is 15.8 min(-1) with ZClPEP as substrate. kcat is 2.8
CC min(-1) with EClPEP as substrate. {ECO:0000269|PubMed:12705838};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12705838,
CC ECO:0000269|PubMed:17053069}.
CC -!- INTERACTION:
CC P08839; P11989: bglG; NbExp=3; IntAct=EBI-551533, EBI-545674;
CC P08839; P0AA04: ptsH; NbExp=4; IntAct=EBI-551533, EBI-902853;
CC P08839; P08839: ptsI; NbExp=2; IntAct=EBI-551533, EBI-551533;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal domain contains the HPr binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site.
CC {ECO:0000269|PubMed:17053069}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain.
CC {ECO:0000269|PubMed:17053069}.
CC -!- MISCELLANEOUS: Enzyme I of the sugar PTS has been shown to
CC phosphorylate NPr of the nitrogen-metabolic PTS, though much less
CC efficiently than it does HPr. This process may link carbon and nitrogen
CC assimilation. {ECO:0000269|PubMed:7876255}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; J02796; AAA24441.1; -; Genomic_DNA.
DR EMBL; M10425; AAA24439.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75469.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16290.1; -; Genomic_DNA.
DR EMBL; M21994; AAA24385.1; -; Genomic_DNA.
DR EMBL; M21451; AAA23656.1; -; Genomic_DNA.
DR PIR; B29785; WQECPI.
DR RefSeq; NP_416911.1; NC_000913.3.
DR RefSeq; WP_000623140.1; NZ_LN832404.1.
DR PDB; 1EZA; NMR; -; A=1-258.
DR PDB; 1EZB; NMR; -; A=1-258.
DR PDB; 1EZC; NMR; -; A=1-258.
DR PDB; 1EZD; NMR; -; A=1-258.
DR PDB; 1ZYM; X-ray; 2.50 A; A/B=1-258.
DR PDB; 2EZA; NMR; -; A=1-258.
DR PDB; 2EZB; NMR; -; A=1-258.
DR PDB; 2EZC; NMR; -; A=1-258.
DR PDB; 2HWG; X-ray; 2.70 A; A/B=1-575.
DR PDB; 2KX9; Other; -; A/B=1-573.
DR PDB; 2L5H; Other; -; A/B=1-573.
DR PDB; 2MP0; NMR; -; A=1-258.
DR PDB; 2N5T; Other; -; A/B=1-575.
DR PDB; 2XDF; Other; -; A/B=1-573.
DR PDB; 3EZA; NMR; -; A=1-249.
DR PDB; 3EZB; NMR; -; A=1-258.
DR PDB; 3EZE; NMR; -; A=1-258.
DR PDB; 6V9K; X-ray; 1.90 A; A/B=261-575.
DR PDB; 6VU0; X-ray; 3.50 A; A/B=261-575.
DR PDBsum; 1EZA; -.
DR PDBsum; 1EZB; -.
DR PDBsum; 1EZC; -.
DR PDBsum; 1EZD; -.
DR PDBsum; 1ZYM; -.
DR PDBsum; 2EZA; -.
DR PDBsum; 2EZB; -.
DR PDBsum; 2EZC; -.
DR PDBsum; 2HWG; -.
DR PDBsum; 2KX9; -.
DR PDBsum; 2L5H; -.
DR PDBsum; 2MP0; -.
DR PDBsum; 2N5T; -.
DR PDBsum; 2XDF; -.
DR PDBsum; 3EZA; -.
DR PDBsum; 3EZB; -.
DR PDBsum; 3EZE; -.
DR PDBsum; 6V9K; -.
DR PDBsum; 6VU0; -.
DR AlphaFoldDB; P08839; -.
DR BMRB; P08839; -.
DR SMR; P08839; -.
DR BioGRID; 4260570; 520.
DR BioGRID; 851219; 3.
DR DIP; DIP-10603N; -.
DR IntAct; P08839; 14.
DR MINT; P08839; -.
DR STRING; 511145.b2416; -.
DR TCDB; 8.A.7.1.1; the phosphotransferase system enzyme i (ei) family.
DR SWISS-2DPAGE; P08839; -.
DR jPOST; P08839; -.
DR PaxDb; P08839; -.
DR PRIDE; P08839; -.
DR EnsemblBacteria; AAC75469; AAC75469; b2416.
DR EnsemblBacteria; BAA16290; BAA16290; BAA16290.
DR GeneID; 946879; -.
DR KEGG; ecj:JW2409; -.
DR KEGG; eco:b2416; -.
DR PATRIC; fig|1411691.4.peg.4315; -.
DR EchoBASE; EB0782; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_6; -.
DR InParanoid; P08839; -.
DR OMA; CNAEWAL; -.
DR PhylomeDB; P08839; -.
DR BioCyc; EcoCyc:PTSI-MON; -.
DR BioCyc; MetaCyc:PTSI-MON; -.
DR BRENDA; 2.7.3.9; 2026.
DR SABIO-RK; P08839; -.
DR EvolutionaryTrace; P08839; -.
DR PRO; PR:P08839; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR024692; PTS_EI.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..575
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147067"
FT ACT_SITE 189
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:12705838,
FT ECO:0000269|PubMed:17053069"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:12705838,
FT ECO:0000305|PubMed:17053069"
FT BINDING 296
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:17053069"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17053069"
FT BINDING 454..455
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:17053069"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17053069"
FT BINDING 465
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT MUTAGEN 189
FT /note="H->A: Very strong decrease of the affinity and
FT catalytic efficiency for PEP. Inactive; when associated
FT with A-502."
FT /evidence="ECO:0000269|PubMed:12705838"
FT MUTAGEN 502
FT /note="C->A: Inactive; when associated with A-189."
FT /evidence="ECO:0000269|PubMed:12705838"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2HWG"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1ZYM"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 36..65
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1ZYM"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3EZA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2HWG"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1ZYM"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1ZYM"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:2HWG"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:1ZYM"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1ZYM"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2HWG"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:6V9K"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2HWG"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 367..380
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 439..443
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 453..460
FT /evidence="ECO:0007829|PDB:6V9K"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:2HWG"
FT HELIX 479..494
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:6V9K"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 512..518
FT /evidence="ECO:0007829|PDB:6V9K"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 530..538
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:6V9K"
FT HELIX 558..569
FT /evidence="ECO:0007829|PDB:6V9K"
SQ SEQUENCE 575 AA; 63562 MW; 4278F0838855E950 CRC64;
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK
AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD
EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI
TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR
AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI
RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF
DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS
VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT
NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC
