ID   EFG_ECOLI               Reviewed;         704 AA.
AC   P0A6M8; P02996; Q2M705; Q9F439;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE            EC=3.6.5.- {ECO:0000269|PubMed:8985244};
GN   Name=fusA; Synonyms=far, fus; OrderedLocusNames=b3340, JW3302;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6322136; DOI=10.1093/nar/12.4.2181;
RA   Zengel J.M., Archer R.H., Lindahl L.;
RT   "The nucleotide sequence of the Escherichia coli fus gene, coding for
RT   elongation factor G.";
RL   Nucleic Acids Res. 12:2181-2192(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1398129; DOI=10.1016/0378-1119(92)90014-g;
RA   Johanson U., Hughes D.;
RT   "Comparison of the complete sequence of the str operon in Salmonella
RT   typhimurium and Escherichia coli.";
RL   Gene 120:93-98(1992).
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   PROTEIN SEQUENCE OF 2-704.
RX   PubMed=7042386; DOI=10.1016/0014-5793(82)80503-6;
RA   Ovchinnikov Y.A., Alakhov Y.B., Bundulis Y.P., Bundule M.A., Dovgas N.V.,
RA   Kozlov V.P., Motuz L.P., Vinokurov L.M.;
RT   "The primary structure of elongation factor G from Escherichia coli. A
RT   complete amino acid sequence.";
RL   FEBS Lett. 139:130-135(1982).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RC   STRAIN=K12;
RX   PubMed=6989816; DOI=10.1016/s0021-9258(19)85545-x;
RA   Post L.E., Nomura M.;
RT   "DNA sequences from the str operon of Escherichia coli.";
RL   J. Biol. Chem. 255:4660-4666(1980).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=L44;
RA   Weigel C.T.O.;
RL   Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 2-13.
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 476-702.
RX   PubMed=7016587; DOI=10.1016/0014-5793(81)80237-2;
RA   Alakhov Y.B., Dovgas N.V., Motuz L.P., Vinokurov L.M., Ovchinnikov Y.A.;
RT   "The primary structure of the elongation factor G from Escherichia coli:
RT   amino acid sequence of the C-terminal domain.";
RL   FEBS Lett. 126:183-186(1981).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-704.
RX   PubMed=7011903; DOI=10.1016/0378-1119(80)90012-8;
RA   Yokota T., Sugisaki H., Takanami M., Kaziro Y.;
RT   "The nucleotide sequence of the cloned tufA gene of Escherichia coli.";
RL   Gene 12:25-31(1980).
RN   [11]
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   [12]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8985244; DOI=10.1038/385037a0;
RA   Rodnina M.V., Savelsbergh A., Katunin V.I., Wintermeyer W.;
RT   "Hydrolysis of GTP by elongation factor G drives tRNA movement on the
RT   ribosome.";
RL   Nature 385:37-41(1997).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-504 AND LYS-643, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [14]
RP   3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES WITH EF-G.
RX   PubMed=12859903; DOI=10.1016/s0092-8674(03)00476-8;
RA   Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.;
RT   "Locking and unlocking of ribosomal motions.";
RL   Cell 114:123-134(2003).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation (PubMed:8985244). During this step, the
CC       ribosome changes from the pre-translocational (PRE) to the post-
CC       translocational (POST) state as the newly formed A-site-bound peptidyl-
CC       tRNA and P-site-bound deacylated tRNA move to the P and E sites,
CC       respectively (PubMed:8985244). Catalyzes the coordinated movement of
CC       the two tRNA molecules, the mRNA and conformational changes in the
CC       ribosome (PubMed:8985244). {ECO:0000269|PubMed:8985244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:8985244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000269|PubMed:8985244};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X00415; CAA25120.1; -; Genomic_DNA.
DR   EMBL; X64592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U18997; AAA58137.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76365.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77951.1; -; Genomic_DNA.
DR   EMBL; AH002539; AAA50991.1; -; Genomic_DNA.
DR   EMBL; X65735; CAA46645.1; -; Genomic_DNA.
DR   PIR; G65127; EFECG.
DR   RefSeq; NP_417799.1; NC_000913.3.
DR   RefSeq; WP_000124700.1; NZ_STEB01000004.1.
DR   PDB; 2RDO; EM; 9.10 A; 7=1-704.
DR   PDB; 3J0E; EM; 9.90 A; H=2-703.
DR   PDB; 3J9Z; EM; 3.60 A; S1=2-703.
DR   PDB; 3JA1; EM; 3.60 A; S3=2-703.
DR   PDB; 4V7B; EM; 6.80 A; AY=1-704.
DR   PDB; 4V7D; EM; 7.60 A; BZ=2-704.
DR   PDB; 4V9O; X-ray; 2.90 A; BV/DV/FV/HV=1-704.
DR   PDB; 4V9P; X-ray; 2.90 A; BV/DV/FV/HV=1-704.
DR   PDB; 7N2C; EM; 2.72 A; EF=2-704.
DR   PDB; 7PJV; EM; 3.10 A; x=1-704.
DR   PDB; 7PJY; EM; 3.10 A; x=1-704.
DR   PDB; 7UG7; EM; 2.58 A; EF=1-700.
DR   PDBsum; 2RDO; -.
DR   PDBsum; 3J0E; -.
DR   PDBsum; 3J9Z; -.
DR   PDBsum; 3JA1; -.
DR   PDBsum; 4V7B; -.
DR   PDBsum; 4V7D; -.
DR   PDBsum; 4V9O; -.
DR   PDBsum; 4V9P; -.
DR   PDBsum; 7N2C; -.
DR   PDBsum; 7PJV; -.
DR   PDBsum; 7PJY; -.
DR   PDBsum; 7UG7; -.
DR   AlphaFoldDB; P0A6M8; -.
DR   EMDB; EMD-13461; -.
DR   EMDB; EMD-13464; -.
DR   EMDB; EMD-1430; -.
DR   EMDB; EMD-1917; -.
DR   EMDB; EMD-1918; -.
DR   EMDB; EMD-24132; -.
DR   EMDB; EMD-26486; -.
DR   EMDB; EMD-5775; -.
DR   EMDB; EMD-5797; -.
DR   EMDB; EMD-5798; -.
DR   EMDB; EMD-5800; -.
DR   EMDB; EMD-6315; -.
DR   EMDB; EMD-6316; -.
DR   SMR; P0A6M8; -.
DR   BioGRID; 4259389; 142.
DR   BioGRID; 852158; 1.
DR   DIP; DIP-31836N; -.
DR   IntAct; P0A6M8; 76.
DR   STRING; 511145.b3340; -.
DR   CarbonylDB; P0A6M8; -.
DR   iPTMnet; P0A6M8; -.
DR   jPOST; P0A6M8; -.
DR   PaxDb; 511145-b3340; -.
DR   EnsemblBacteria; AAC76365; AAC76365; b3340.
DR   GeneID; 83578310; -.
DR   GeneID; 947847; -.
DR   KEGG; ecj:JW3302; -.
DR   KEGG; eco:b3340; -.
DR   PATRIC; fig|1411691.4.peg.3391; -.
DR   EchoBASE; EB0355; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   InParanoid; P0A6M8; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 9804431at2; -.
DR   PhylomeDB; P0A6M8; -.
DR   BioCyc; EcoCyc:EG10360-MONOMER; -.
DR   BRENDA; 3.6.5.3; 2026.
DR   EvolutionaryTrace; P0A6M8; -.
DR   PRO; PR:P0A6M8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IDA:UniProtKB.
DR   CDD; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   CDD; cd04088; EFG_mtEFG_II; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   SWISS-2DPAGE; P0A6M8; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Elongation factor; GTP-binding; Hydrolase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7042386,
FT                   ECO:0000269|PubMed:9298646"
FT   CHAIN           2..704
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091119"
FT   DOMAIN          8..290
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         504
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         643
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   CONFLICT        296..297
FT                   /note="NG -> DC (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300..302
FT                   /note="Missing (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="T -> C (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="I -> V (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        584
FT                   /note="H -> K (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        594
FT                   /note="K -> H (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        646
FT                   /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657
FT                   /note="E -> Q (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        662
FT                   /note="E -> EQ (in Ref. 5; AA sequence and 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..16
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           25..34
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           54..58
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          107..117
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           151..160
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          166..175
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          195..199
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            209..211
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           212..215
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           220..227
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           231..238
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           245..256
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            269..272
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           275..285
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          289..292
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          318..327
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            328..330
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          331..344
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          348..351
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            352..355
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          356..359
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          363..366
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          368..378
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          400..402
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          416..421
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           425..427
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           428..441
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          446..449
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          456..462
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           463..477
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          482..484
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          491..496
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          498..504
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          509..512
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          517..524
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            529..532
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          533..537
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          542..545
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            547..549
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           550..560
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          562..564
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            565..567
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          573..582
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          585..587
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           590..604
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           606..608
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          610..623
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           625..627
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           628..637
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          641..644
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          651..660
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           666..673
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   TURN            674..676
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   STRAND          680..689
FT                   /evidence="ECO:0007829|PDB:4V9O"
FT   HELIX           692..697
FT                   /evidence="ECO:0007829|PDB:4V9O"
SQ   SEQUENCE   704 AA;  77581 MW;  8C72B9F87253BC7B CRC64;
     MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTA FWSGMAKQYE PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ
     PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVNQIKT RLGANPVPLQ LAIGAEEHFT
     GVVDLVKMKA INWNDADQGV TFEYEDIPAD MVELANEWHQ NLIESAAEAS EELMEKYLGG
     EELTEAEIKG ALRQRVLNNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD
     DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKAARERF
     GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV
     EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE
     ANVGKPQVAY RETIRQKVTD VEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI
     KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDMGIRLHF GSYHDVDSSE LAFKLAASIA
     FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLKGQESEVT GVKIHAEVPL
     SEMFGYATQL RSLTKGRASY TMEFLKYDEA PSNVAQAVIE ARGK
//