ID FIBER_BPK1F Reviewed; 1064 AA. AC Q04830; Q2WC71; Q858B1; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 4. DT 24-JAN-2024, entry version 126. DE RecName: Full=Tail spike protein {ECO:0000305}; DE Short=TSP; DE AltName: Full=Endo-N-acetylneuraminidase; DE Short=Endo-N; DE AltName: Full=Endo-alpha-sialidase {ECO:0000305}; DE EC=3.2.1.129 {ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967, ECO:0000269|PubMed:3546309}; DE AltName: Full=EndoNF; DE AltName: Full=G102; DE Contains: DE RecName: Full=Mature tail spike protein {ECO:0000250|UniProtKB:P49714}; DE Contains: DE RecName: Full=Intramolecular chaperone {ECO:0000250|UniProtKB:P49714}; OS Escherichia phage K1F (Bacteriophage K1F). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographiviridae; Studiervirinae; Kayfunavirus; Kayfunavirus K1F. OX NCBI_TaxID=344021; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-31 AND 917-920, AND SUBCELLULAR RP LOCATION (MATURE TAIL SPIKE PROTEIN). RX PubMed=8331067; DOI=10.1128/jb.175.14.4354-4363.1993; RA Petter J.G., Vimr E.R.; RT "Complete nucleotide sequence of the bacteriophage K1F tail gene encoding RT endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in RT bacteriophage PK1E."; RL J. Bacteriol. 175:4354-4363(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 913-922, RP IDENTIFICATION (TAIL SPIKE PROTEIN), PROTEOLYTIC CLEAVAGE (TAIL SPIKE RP PROTEIN), CATALYTIC ACTIVITY (TAIL SPIKE PROTEIN), AND FUNCTION RP (INTRAMOLECULAR CHAPERONE). RX PubMed=12556457; DOI=10.1074/jbc.m212048200; RA Muehlenhoff M., Stummeyer K., Grove M., Sauerborn M., Gerardy-Schahn R.; RT "Proteolytic processing and oligomerization of bacteriophage-derived RT endosialidases."; RL J. Biol. Chem. 278:12634-12644(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16321955; DOI=10.1128/jb.187.24.8499-8503.2005; RA Scholl D., Merril C.; RT "The genome of bacteriophage K1F, a T7-like phage that has acquired the RT ability to replicate on K1 strains of Escherichia coli."; RL J. Bacteriol. 187:8499-8503(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16689790; DOI=10.1111/j.1365-2958.2006.05173.x; RA Stummeyer K., Schwarzer D., Claus H., Vogel U., Gerardy-Schahn R., RA Muhlenhoff M.; RT "Evolution of bacteriophages infecting encapsulated bacteria: lessons from RT Escherichia coli K1-specific phages."; RL Mol. Microbiol. 60:1123-1135(2006). RN [5] RP CHARACTERIZATION, FUNCTION (MATURE TAIL SPIKE PROTEIN), CATALYTIC ACTIVITY RP (MATURE TAIL SPIKE PROTEIN), SUBUNIT (MATURE TAIL SPIKE PROTEIN), AND RP BIOPHYSICOCHEMICAL PROPERTIES (MATURE TAIL SPIKE PROTEIN). RX PubMed=3546309; DOI=10.1016/s0021-9258(18)61387-0; RA Hallenbeck P.C., Vimr E.R., Yu F., Bassler B., Troy F.A.; RT "Purification and properties of a bacteriophage-induced endo-N- RT acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate RT units."; RL J. Biol. Chem. 262:3553-3561(1987). RN [6] RP PROTEOLYTIC CLEAVAGE (TAIL SPIKE PROTEIN), CATALYTIC ACTIVITY (MATURE TAIL RP SPIKE PROTEIN), AND MUTAGENESIS OF SER-911. RX PubMed=19189967; DOI=10.1074/jbc.m808475200; RA Schwarzer D., Stummeyer K., Haselhorst T., Freiberger F., Rode B., RA Grove M., Scheper T., von Itzstein M., Muehlenhoff M., Gerardy-Schahn R.; RT "Proteolytic release of the intramolecular chaperone domain confers RT processivity to endosialidase F."; RL J. Biol. Chem. 284:9465-9474(2009). RN [7] {ECO:0007744|PDB:1V0E, ECO:0007744|PDB:1V0F} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-910, INTERACTION WITH SIALIC RP ACID (MATURE TAIL SPIKE PROTEIN), SUBUNIT (MATURE TAIL SPIKE PROTEIN), RP MUTAGENESIS OF GLU-581; ARG-596 AND ARG-647, AND ACTIVE SITE (MATURE TAIL RP SPIKE PROTEIN). RX PubMed=15608653; DOI=10.1038/nsmb874; RA Stummeyer K., Dickmanns A., Muhlenhoff M., Gerardy-Schahn R., Ficner R.; RT "Crystal structure of the polysialic acid-degrading endosialidase of RT bacteriophage K1F."; RL Nat. Struct. Mol. Biol. 12:90-96(2005). RN [8] {ECO:0007744|PDB:3JU4} RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 246-910, AND SUBUNIT. RX PubMed=20124697; DOI=10.1107/s0907444909048720; RA Schulz E.C., Neumann P., Gerardy-Schahn R., Sheldrick G.M., Ficner R.; RT "Structure analysis of endosialidase NF at 0.98 A resolution."; RL Acta Crystallogr. D 66:176-180(2010). RN [9] {ECO:0007744|PDB:3GVJ, ECO:0007744|PDB:3GVK, ECO:0007744|PDB:3GVL} RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 246-910 IN COMPLEX WITH RP OLIGOMERIC SIALIC ACID, ACTIVE SITE (MATURE TAIL SPIKE PROTEIN), RP MUTAGENESIS OF TRP-328; HIS-350; LYS-410; HIS-542; ARG-549; GLU-581 AND RP ARG-647, INTERACTION WITH SIALIC ACID (MATURE TAIL SPIKE PROTEIN), AND RP FUNCTION (MATURE TAIL SPIKE PROTEIN). RX PubMed=20096705; DOI=10.1016/j.jmb.2010.01.028; RA Schulz E.C., Schwarzer D., Frank M., Stummeyer K., Muhlenhoff M., RA Dickmanns A., Gerardy-Schahn R., Ficner R.; RT "Structural basis for the recognition and cleavage of polysialic acid by RT the bacteriophage K1F tailspike protein EndoNF."; RL J. Mol. Biol. 397:341-351(2010). CC -!- FUNCTION: [Mature tail spike protein]: Receptor binding protein, which CC mediates the attachment to the host capsule (PubMed:20096705, CC PubMed:3546309). Degrades the alpha-2,8-linked polysialic acid of CC E.coli K1 capsule by cleaving within the polymer chain of polysialic CC acid (PubMed:3546309). {ECO:0000269|PubMed:20096705, CC ECO:0000269|PubMed:3546309}. CC -!- FUNCTION: [Intramolecular chaperone]: The C-terminal chaperone protein CC mediates homotrimerization and proper folding of the catalytic endo-N CC trimer. {ECO:0000269|PubMed:12556457}. CC -!- CATALYTIC ACTIVITY: [Mature tail spike protein]: CC Reaction=Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or CC poly(sialic) acids.; EC=3.2.1.129; CC Evidence={ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967, CC ECO:0000269|PubMed:3546309}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Mature tail spike protein]: CC Kinetic parameters: CC KM=71 uM for poly-alpha-2,8-sialosyl carbohydrates CC {ECO:0000269|PubMed:3546309}; CC KM=1.2 mM for oligo-alpha-2,8-sialosyl carbohydrates CC {ECO:0000269|PubMed:3546309}; CC KM=7.1 uM for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates CC {ECO:0000269|PubMed:3546309}; CC Vmax=19 umol/min/mg enzyme for poly-alpha-2,8-sialosyl carbohydrates CC cleavage {ECO:0000269|PubMed:3546309}; CC Vmax=18 umol/min/mg enzyme for oligo-alpha-2,8-sialosyl carbohydrates CC cleavage {ECO:0000269|PubMed:3546309}; CC Vmax=13 umol/min/mg enzyme for poly-alpha-2,8-alpha-2,9-sialosyl CC carbohydrates {ECO:0000269|PubMed:3546309}; CC -!- SUBUNIT: [Mature tail spike protein]: Homotrimer (PubMed:3546309, CC PubMed:20124697). Interacts with sialic acid (PubMed:15608653, CC PubMed:20096705). {ECO:0000269|PubMed:15608653, CC ECO:0000269|PubMed:20096705, ECO:0000269|PubMed:20124697, CC ECO:0000269|PubMed:3546309}. CC -!- INTERACTION: CC Q04830; Q04830: -; NbExp=2; IntAct=EBI-15829658, EBI-15829658; CC -!- SUBCELLULAR LOCATION: [Mature tail spike protein]: Virion CC {ECO:0000269|PubMed:8331067}. Note=Tail spike. CC {ECO:0000269|PubMed:8331067}. CC -!- PTM: [Tail spike protein]: Proteolytic cleavage and release of the CC chaperone in the host cytosol stabilizes the folded protein CC (PubMed:12556457, PubMed:19189967). The cleavage gives rise to the CC mature tail spike protein but is not essential for catalytic activity CC (By similarity). However, release of the chaperone domain confers CC kinetic stability and processivity to the endosialidase CC (PubMed:19189967). {ECO:0000250|UniProtKB:P49714, CC ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 58 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37340.1; Type=Frameshift; Evidence={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; M63657; AAC37340.1; ALT_FRAME; Unassigned_DNA. DR EMBL; AJ505988; CAD44528.2; -; Genomic_DNA. DR EMBL; DQ111067; AAZ73001.1; -; Genomic_DNA. DR EMBL; AM084414; CAJ29390.1; -; Genomic_DNA. DR PIR; A36887; A36887. DR RefSeq; YP_338127.1; NC_007456.1. DR PDB; 1V0E; X-ray; 1.90 A; A/B/C/D/E/F=246-910. DR PDB; 1V0F; X-ray; 2.55 A; A/B/C/D/E/F=246-910. DR PDB; 3GVJ; X-ray; 1.48 A; A=246-910. DR PDB; 3GVK; X-ray; 1.84 A; A/B/C=246-910. DR PDB; 3GVL; X-ray; 1.41 A; A=246-910. DR PDB; 3GW6; X-ray; 2.60 A; A/B/C/D/E/F=790-1064. DR PDB; 3JU4; X-ray; 0.98 A; A=246-910. DR PDBsum; 1V0E; -. DR PDBsum; 1V0F; -. DR PDBsum; 3GVJ; -. DR PDBsum; 3GVK; -. DR PDBsum; 3GVL; -. DR PDBsum; 3GW6; -. DR PDBsum; 3JU4; -. DR SMR; Q04830; -. DR DIP; DIP-48774N; -. DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid. DR DrugBank; DB04265; N-acetyl-beta-neuraminic acid. DR CAZy; GH58; Glycoside Hydrolase Family 58. DR MEROPS; S74.001; -. DR GeneID; 3707741; -. DR KEGG; vg:3707741; -. DR OrthoDB; 303at10239; -. DR BRENDA; 3.2.1.129; 716. DR SABIO-RK; Q04830; -. DR EvolutionaryTrace; Q04830; -. DR Proteomes; UP000001530; Genome. DR Proteomes; UP000001722; Genome. DR GO; GO:0098024; C:virus tail, fiber; IDA:UniProtKB. DR GO; GO:0016996; F:endo-alpha-(2,8)-sialidase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW. DR GO; GO:0098994; P:disruption of host cell envelope during viral entry; IEA:UniProtKB-KW. DR GO; GO:0098996; P:disruption of host cell glycocalyx during viral entry; IEA:UniProtKB-KW. DR GO; GO:0044409; P:entry into host; IDA:UniProtKB. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB. DR CDD; cd10144; Peptidase_S74_CIMCD; 1. DR Gene3D; 2.10.10.80; -; 1. DR Gene3D; 2.120.10.10; -; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR Gene3D; 1.20.5.1240; Endo-n-acetylneuraminidase; 1. DR Gene3D; 3.30.2460.10; Endo-n-acetylneuraminidase domain; 1. DR Gene3D; 4.10.1090.10; Endosialidase, domain 4; 1. DR Gene3D; 3.30.750.60; Endosialidase, N-terminal extension domain; 1. DR InterPro; IPR023366; ATP_synth_asu-like_sf. DR InterPro; IPR024427; Endosialidase_beta_barrel. DR InterPro; IPR024428; Endosialidase_beta_prop. DR InterPro; IPR024430; Endosialidase_C_dom. DR InterPro; IPR044914; Endosialidase_C_dom_sf. DR InterPro; IPR024429; Endosialidase_N-extension. DR InterPro; IPR001724; Glycl_Hydrolase_58. DR InterPro; IPR005604; Phage_T7_tail_fibre-like_N. DR InterPro; IPR030392; S74_ICA. DR InterPro; IPR036278; Sialidase_sf. DR InterPro; IPR040775; Tail_spike_N. DR Pfam; PF12195; End_beta_barrel; 1. DR Pfam; PF12217; End_beta_propel; 1. DR Pfam; PF12218; End_N_terminal; 1. DR Pfam; PF12219; End_tail_spike; 1. DR Pfam; PF13884; Peptidase_S74; 1. DR Pfam; PF03906; Phage_T7_tail; 1. DR Pfam; PF18668; Tail_spike_N; 1. DR PRINTS; PR00849; GLHYDRLASE58. DR SUPFAM; SSF69349; Phage fibre proteins; 1. DR SUPFAM; SSF50939; Sialidases; 1. DR PROSITE; PS51688; ICA; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Degradation of host capsule during virus entry; KW Degradation of host cell envelope components during virus entry; KW Direct protein sequencing; Glycosidase; Host-virus interaction; Hydrolase; KW Reference proteome; Repeat; Viral attachment to host adhesion receptor; KW Viral attachment to host cell; Viral tail fiber protein; KW Viral tail protein; Virion; Virus entry into host cell. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000269|PubMed:8331067" FT CHAIN 2..1064 FT /note="Tail spike protein" FT /id="PRO_0000057709" FT CHAIN 2..911 FT /note="Mature tail spike protein" FT /id="PRO_0000458688" FT CHAIN 912..1064 FT /note="Intramolecular chaperone" FT /evidence="ECO:0000305|PubMed:12556457" FT /id="PRO_0000438182" FT REPEAT 360..371 FT /note="BNR 1" FT REPEAT 496..503 FT /note="BNR 2" FT REPEAT 608..619 FT /note="BNR 3" FT DOMAIN 911..1064 FT /note="Peptidase S74" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025" FT COILED 1044..1064 FT /evidence="ECO:0000255" FT ACT_SITE 581 FT /evidence="ECO:0000269|PubMed:15608653, FT ECO:0000269|PubMed:20096705" FT ACT_SITE 596 FT /evidence="ECO:0000269|PubMed:15608653" FT ACT_SITE 647 FT /evidence="ECO:0000269|PubMed:15608653, FT ECO:0000269|PubMed:20096705" FT SITE 542 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 545 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 549 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 578 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 598 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 599 FT /note="Binding to sialic acid" FT /evidence="ECO:0000269|PubMed:20096705" FT SITE 911..912 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:O09496" FT MUTAGEN 328 FT /note="W->R: Almost complete loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:20096705" FT MUTAGEN 350 FT /note="H->A,N,Q: Almost complete loss of enzymatic FT activity." FT /evidence="ECO:0000269|PubMed:20096705" FT MUTAGEN 410 FT /note="K->A: 80% loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:20096705" FT MUTAGEN 542 FT /note="H->A: 60% loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:20096705" FT MUTAGEN 549 FT /note="R->A: Almost complete loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:20096705" FT MUTAGEN 581 FT /note="E->A: Almost complete loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:15608653, FT ECO:0000269|PubMed:20096705" FT MUTAGEN 596 FT /note="R->A: Complete loss of enzymatic activity; when FT associated with A-581. Complete loss of enzymatic activity; FT when associated with A-647." FT /evidence="ECO:0000269|PubMed:15608653" FT MUTAGEN 647 FT /note="R->A: Almost complete loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:15608653, FT ECO:0000269|PubMed:20096705" FT MUTAGEN 911 FT /note="S->A: Complete loss of proteolytic processing. FT 190-fold reduced enzymatic activity." FT /evidence="ECO:0000269|PubMed:19189967" FT CONFLICT 628 FT /note="H -> R (in Ref. 1; AAC37340)" FT /evidence="ECO:0000305" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:3JU4" FT HELIX 255..264 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:3JU4" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 323..327 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 339..352 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 356..364 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:3GVK" FT TURN 380..384 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 385..388 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 398..407 FT /evidence="ECO:0007829|PDB:3JU4" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 413..422 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 441..445 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 456..461 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 469..472 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 475..478 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 481..485 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 500..505 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 524..531 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 537..543 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 545..548 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 550..556 FT /evidence="ECO:0007829|PDB:3JU4" FT TURN 557..561 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:3JU4" FT HELIX 573..575 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 579..587 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 590..598 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 606..612 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 618..621 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 633..636 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 639..645 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 667..674 FT /evidence="ECO:0007829|PDB:3JU4" FT TURN 675..677 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 686..690 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 696..698 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 702..710 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 713..721 FT /evidence="ECO:0007829|PDB:3JU4" FT TURN 728..734 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 746..753 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 784..786 FT /evidence="ECO:0007829|PDB:3GVK" FT STRAND 790..792 FT /evidence="ECO:0007829|PDB:3GVK" FT STRAND 796..803 FT /evidence="ECO:0007829|PDB:3GVK" FT TURN 808..811 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 812..817 FT /evidence="ECO:0007829|PDB:3GVK" FT STRAND 819..826 FT /evidence="ECO:0007829|PDB:3GVK" FT HELIX 833..835 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 837..847 FT /evidence="ECO:0007829|PDB:3JU4" FT HELIX 848..850 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 853..857 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 861..863 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 867..870 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 872..879 FT /evidence="ECO:0007829|PDB:3GVK" FT STRAND 884..889 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 891..893 FT /evidence="ECO:0007829|PDB:3JU4" FT STRAND 901..905 FT /evidence="ECO:0007829|PDB:3GVK" FT HELIX 924..930 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 936..938 FT /evidence="ECO:0007829|PDB:3GW6" FT HELIX 941..947 FT /evidence="ECO:0007829|PDB:3GW6" FT HELIX 948..950 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 953..956 FT /evidence="ECO:0007829|PDB:3GW6" FT HELIX 959..968 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 984..989 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 992..1006 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 1008..1010 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 1012..1026 FT /evidence="ECO:0007829|PDB:3GW6" FT STRAND 1029..1034 FT /evidence="ECO:0007829|PDB:3GW6" FT HELIX 1036..1059 FT /evidence="ECO:0007829|PDB:3GW6" SQ SEQUENCE 1064 AA; 118905 MW; 82FAB75EDC68DAB6 CRC64; MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND ARIHFGVIAQ QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN EIVEHTDEEG NVTTTEEPVY TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK LERIEARLSA LEQK //