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 04-NOV-2026, entry version 226. 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}; GN OrderedLocusNames=b2416, JW2409; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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 INTERACTION WITH TMAR, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-122, RP AND MUTAGENESIS OF TYR-122. RC STRAIN=K12 / BW25113; RX PubMed=33376208; DOI=10.1073/pnas.2016017118; RA Szoke T., Albocher N., Govindarajan S., Nussbaum-Shochat A., RA Amster-Choder O.; RT "Tyrosine phosphorylation-dependent localization of TmaR that controls RT activity of a major bacterial sugar regulator by polar sequestration."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [13] RP X-RAY CRYSTALLOGRAPHY. 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 [14] 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 [15] 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 [16] 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 [17] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE ANALOG AND MAGNESIUM IONS, RP FUNCTION, COFACTOR, SUBUNIT, ACTIVE SITE, AND REACTION 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:12705838, PubMed:17053069, CC PubMed:7876255). 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 (PubMed:12705838, PubMed:17053069). Interacts with CC the pole-localizer protein TmaR (PubMed:33376208). Binding to TmaR is CC reversible as long as TmaR can get phosphorylated, whereas binding to CC non-phosphorylated TmaR is very strong and shifts the equilibrium CC toward binding (PubMed:33376208). {ECO:0000269|PubMed:12705838, CC ECO:0000269|PubMed:17053069, ECO:0000269|PubMed:33376208}. 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:0000269|PubMed:33376208}. CC Note=Localizes mainly near one pole of the cell (PubMed:33376208). CC Localization at the pole requires phosphorylation at Tyr-122 and is CC controlled by the pole-localizer protein TmaR (PubMed:33376208). CC {ECO:0000269|PubMed:33376208}. 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 -!- PTM: Phosphorylated on Tyr-122 (PubMed:33376208). Phosphorylation on CC Tyr-122 is important for polar localization but not for interaction CC with TmaR and for activity (PubMed:33376208). CC {ECO:0000269|PubMed:33376208}. 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}. 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; 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_CP009789.1. 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=1-259. 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 AlphaFoldDB; P08839; -. DR BMRB; P08839; -. DR MDposit; P08839; -. DR MDRepo; P08839; -. DR SMR; P08839; -. DR BioGRID; 4260570; 528. DR BioGRID; 851219; 3. DR DIP; DIP-10603N; -. DR FunCoup; P08839; 521. DR IntAct; P08839; 14. DR STRING; 511145.b2416; -. DR TCDB; 8.A.7.1.1; the phosphotransferase system enzyme i (ei) family. DR iPTMnet; P08839; -. DR jPOST; P08839; -. DR PaxDb; 511145-b2416; -. DR EnsemblBacteria; AAC75469; AAC75469; b2416. DR GeneID; 946879; -. DR KEGG; ecj:JW2409; -. DR KEGG; eco:b2416; -. DR KEGG; ecoc:C3026_13430; -. 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; AADPLMI; -. DR OrthoDB; 9765468at2; -. DR PhylomeDB; P08839; -. DR BioCyc; EcoCyc:PTSI-MONOMER; -. DR BioCyc; MetaCyc:PTSI-MONOMER; -. DR BRENDA; 2.7.3.9; 2026. DR SABIO-RK; P08839; -. DR EvolutionaryTrace; P08839; -. DR PRO; PR:P08839; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P08839; -. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; HDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; EXP:UniProtKB. DR GO; GO:0015764; P:N-acetylglucosamine transport; IBA:GO_Central. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR FunFam; 1.10.274.10:FF:000001; Phosphoenolpyruvate-protein phosphotransferase; 1. DR FunFam; 3.20.20.60:FF:000007; Phosphoenolpyruvate-protein phosphotransferase; 1. DR FunFam; 3.50.30.10:FF:000001; Phosphoenolpyruvate-protein phosphotransferase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1. DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR050499; PEP-utilizing_PTS_enzyme. 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 NCBIfam; TIGR01417; PTS_I_fam; 1. DR NCBIfam; NF008382; ptsI; 1. DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. DR PANTHER; PTHR46244:SF6; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1. 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 PRINTS; PR01736; PHPHTRNFRASE. DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 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; Phosphoprotein; Phosphotransferase system; KW Reference proteome; 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 MOD_RES 122 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:33376208" FT MUTAGEN 122 FT /note="Y->F: Is not detected in polar clusters. Is FT completely diffused throughout the cytoplasm. Does not FT affect function in sugar uptake or interaction with TmaR." FT /evidence="ECO:0000269|PubMed:33376208" 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 HELIX 22..25 FT /evidence="ECO:0007829|PDB:2MP0" FT HELIX 29..32 FT /evidence="ECO:0007829|PDB:1EZA" 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 144..147 FT /evidence="ECO:0007829|PDB:1EZB" 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..237 FT /evidence="ECO:0007829|PDB:1ZYM" FT HELIX 238..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 //