ID   WAC_BPT4                Reviewed;         487 AA.
AC   P10104; O10628; Q9T0U8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Fibritin {ECO:0000303|PubMed:7932704};
DE   AltName: Full=Collar protein;
DE   AltName: Full=Whisker antigen control protein {ECO:0000303|PubMed:3194206};
GN   Name=wac {ECO:0000303|PubMed:3194206};
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Straboviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D;
RX   PubMed=3194206; DOI=10.1093/nar/16.21.10361;
RA   Prilipov A.G., Selivanov N.A., Nikolaeva L.I., Mesyanzhinov V.V.;
RT   "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene wac.";
RL   Nucleic Acids Res. 16:10361-10361(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D;
RX   PubMed=7932704; DOI=10.1006/jmbi.1994.1595;
RA   Efimov V.P., Nepluev I.V., Sobolev B.N., Zurabishvili T.G., Schulthess T.,
RA   Lustig A., Engel J., Haener M., Aebi U., Venyaminov S.Y., Potekhin S.A.,
RA   Mesyanzhinov V.V.;
RT   "Fibritin encoded by bacteriophage T4 gene wac has a parallel triple-
RT   stranded alpha-helical coiled-coil structure.";
RL   J. Mol. Biol. 242:470-486(1994).
RN   [3]
RP   SEQUENCE REVISION TO 358 AND 479.
RC   STRAIN=D;
RA   Mesyanzhinov V.V.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 480-487.
RC   STRAIN=D;
RX   PubMed=2657662; DOI=10.1093/nar/17.9.3583;
RA   Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.;
RT   "Nucleotide sequences of bacteriophage T4 genes 13, 14 and 15.";
RL   Nucleic Acids Res. 17:3583-3583(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC   STRAIN=D;
RX   PubMed=3357780; DOI=10.1093/nar/16.5.2334;
RA   Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.;
RT   "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene 12.";
RL   Nucleic Acids Res. 16:2334-2334(1988).
RN   [7]
RP   FUNCTION.
RX   PubMed=423246; DOI=10.1016/0022-2836(79)90454-6;
RA   Terzaghi B.E., Terzaghi E., Coombs D.;
RT   "The role of the collar/whisker complex in bacteriophage T4D tail fiber
RT   attachment.";
RL   J. Mol. Biol. 127:1-14(1979).
RN   [8]
RP   TOPOLOGY, AND COILED COIL.
RX   PubMed=1878168; DOI=10.1080/07391102.1991.10507859;
RA   Sobolev B.N., Mesyanzhinov V.V.;
RT   "The wac gene product of bacteriophage T4 contains coiled-coil structural
RT   patterns.";
RL   J. Biomol. Struct. Dyn. 8:953-965(1991).
RN   [9]
RP   FUNCTION, AND COILED COIL.
RX   PubMed=15659683; DOI=10.1128/jb.187.3.1055-1066.2005;
RA   Letarov A., Manival X., Desplats C., Krisch H.M.;
RT   "gpwac of the T4-type bacteriophages: structure, function, and evolution of
RT   a segmented coiled-coil protein that controls viral infectivity.";
RL   J. Bacteriol. 187:1055-1066(2005).
RN   [10]
RP   CROSS-LINK TO HOST DNCV.
RX   PubMed=36848932; DOI=10.1038/s41586-023-05862-7;
RA   Jenson J.M., Li T., Du F., Ea C.K., Chen Z.J.;
RT   "Ubiquitin-like conjugation by bacterial cGAS enhances anti-phage
RT   defence.";
RL   Nature 616:326-331(2023).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 369-487, COILED COIL, AND SUBUNIT.
RX   PubMed=9261070; DOI=10.1016/s0969-2126(97)00233-5;
RA   Tao Y., Strelkov S.V., Mesyanzhinov V.V., Rossmann M.G.;
RT   "Structure of bacteriophage T4 fibritin: a segmented coiled coil and the
RT   role of the C-terminal domain.";
RL   Structure 5:789-798(1997).
RN   [12] {ECO:0007744|PDB:1AVY}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 414-487.
RX   PubMed=9757094; DOI=10.1107/s0907444997018878;
RA   Strelkov S.V., Tao Y., Shneider M.M., Mesyanzhinov V.V., Rossmann M.G.;
RT   "Structure of bacteriophage T4 fibritin M: a troublesome packing
RT   arrangement.";
RL   Acta Crystallogr. D 54:805-816(1998).
RN   [13] {ECO:0007744|PDB:1RFO}
RP   STRUCTURE BY NMR OF 458-484, AND SUBUNIT.
RX   PubMed=15033360; DOI=10.1016/j.jmb.2004.02.020;
RA   Guthe S., Kapinos L., Moglich A., Meier S., Grzesiek S., Kiefhaber T.;
RT   "Very fast folding and association of a trimerization domain from
RT   bacteriophage T4 fibritin.";
RL   J. Mol. Biol. 337:905-915(2004).
RN   [14] {ECO:0007744|PDB:1OX3}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-81.
RX   PubMed=15165860; DOI=10.1016/j.jmb.2004.04.001;
RA   Boudko S.P., Strelkov S.V., Engel J., Stetefeld J.;
RT   "Design and crystal structure of bacteriophage T4 mini-fibritin NCCF.";
RL   J. Mol. Biol. 339:927-935(2004).
RN   [15] {ECO:0007744|PDB:2BSG}
RP   STRUCTURE BY ELECTRON MICROSCOPY (15.00 ANGSTROMS).
RX   PubMed=16116440; DOI=10.1038/nsmb975;
RA   Kostyuchenko V.A., Chipman P.R., Leiman P.G., Arisaka F.,
RA   Mesyanzhinov V.V., Rossmann M.G.;
RT   "The tail structure of bacteriophage T4 and its mechanism of contraction.";
RL   Nat. Struct. Mol. Biol. 12:810-813(2005).
RN   [16] {ECO:0007744|PDB:2KBL}
RP   STRUCTURE BY NMR OF 458-484, AND SUBUNIT.
RX   PubMed=19361528; DOI=10.1016/j.jmb.2009.03.073;
RA   Habazettl J., Reiner A., Kiefhaber T.;
RT   "NMR structure of a monomeric intermediate on the evolutionarily optimized
RT   assembly pathway of a small trimerization domain.";
RL   J. Mol. Biol. 389:103-114(2009).
RN   [17] {ECO:0007744|PDB:3J2O}
RP   STRUCTURE BY ELECTRON MICROSCOPY (25.00 ANGSTROMS) OF 2-487, INTERACTION
RP   WITH GP13, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23434847; DOI=10.1016/j.jmb.2013.02.012;
RA   Fokine A., Zhang Z., Kanamaru S., Bowman V.D., Aksyuk A.A., Arisaka F.,
RA   Rao V.B., Rossmann M.G.;
RT   "The molecular architecture of the bacteriophage T4 neck.";
RL   J. Mol. Biol. 425:1731-1744(2013).
RN   [18] {ECO:0007744|PDB:4NCU, ECO:0007744|PDB:4NCV, ECO:0007744|PDB:4NCW}
RP   X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 458-484.
RX   PubMed=24637609; DOI=10.1039/c3ob42251h;
RA   Berthelmann A., Lach J., Grawert M.A., Groll M., Eichler J.;
RT   "Versatile C(3)-symmetric scaffolds and their use for covalent
RT   stabilization of the foldon trimer.";
RL   Org. Biomol. Chem. 12:2606-2614(2014).
CC   -!- FUNCTION: Chaperone involved in tail fiber assembly and retraction.
CC       Acts as a chaperone helping to attach the long tail fibers to the virus
CC       during the assembly process. During phage assembly, twelve fibritin
CC       molecules attach to the phage neck via gp13: six molecules forming the
CC       collar and six molecules forming the whiskers.
CC       {ECO:0000269|PubMed:15659683, ECO:0000269|PubMed:23434847,
CC       ECO:0000269|PubMed:423246}.
CC   -!- SUBUNIT: Homotrimer (PubMed:9261070, PubMed:15033360, PubMed:19361528).
CC       Interacts (via N-terminal domain) with neck protein gp13; this
CC       interaction allows attachment of the fibrous collar and wiskers
CC       (PubMed:23434847). {ECO:0000269|PubMed:15033360,
CC       ECO:0000269|PubMed:19361528, ECO:0000269|PubMed:23434847,
CC       ECO:0000269|PubMed:9261070}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:23434847}.
CC       Note=Localizes to the neck. {ECO:0000269|PubMed:23434847}.
CC   -!- DOMAIN: The central domain consists of 12 alpha-helical domains (19-40
CC       residues long) with coiled-coil structural patterns.
CC   -!- PTM: Cross-linked via an isopeptide bond to E.coli host protein DncV
CC       during infection (PubMed:36848932). {ECO:0000269|PubMed:36848932}.
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; X12888; CAA31379.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42679.1; -; Genomic_DNA.
DR   EMBL; X14868; CAA33006.1; -; Genomic_DNA.
DR   EMBL; X06792; CAA29952.1; -; Genomic_DNA.
DR   PIR; S01917; FIBPT4.
DR   RefSeq; NP_049771.1; NC_000866.4.
DR   PDB; 1AA0; X-ray; 2.20 A; A=372-484.
DR   PDB; 1AVY; X-ray; 1.85 A; A/B/C=414-487.
DR   PDB; 1OX3; X-ray; 2.00 A; A=2-81.
DR   PDB; 1RFO; NMR; -; A/B/C=458-484.
DR   PDB; 1V1H; X-ray; 1.90 A; A/B/C/D/E/F=456-484.
DR   PDB; 1V1I; X-ray; 1.90 A; A/B/C=456-484.
DR   PDB; 2BSG; EM; 15.00 A; A/B/C=1-487.
DR   PDB; 2IBL; X-ray; 1.32 A; A=2-81.
DR   PDB; 2KBL; NMR; -; A=458-484.
DR   PDB; 3A1M; X-ray; 2.00 A; A/B/C/D/E/F=458-484.
DR   PDB; 3J2O; EM; 25.00 A; A/B/C/D/E/F=2-487.
DR   PDB; 4MMQ; X-ray; 3.25 A; B=458-484.
DR   PDB; 4MMR; X-ray; 3.10 A; B=458-484.
DR   PDB; 4MMS; X-ray; 2.40 A; B/D/F=458-484.
DR   PDB; 4MMT; X-ray; 3.05 A; B=458-484.
DR   PDB; 4MMU; X-ray; 3.00 A; B=458-484.
DR   PDB; 4MMV; X-ray; 2.81 A; B=458-484.
DR   PDB; 4NCU; X-ray; 1.11 A; A=458-484.
DR   PDB; 4NCV; X-ray; 1.20 A; A/B/C=458-484.
DR   PDB; 4NCW; X-ray; 1.30 A; A/B/C=458-484.
DR   PDB; 5TDL; X-ray; 3.50 A; A=458-484.
DR   PDB; 6APD; X-ray; 4.10 A; A/B/C=458-484.
DR   PDB; 6CNV; X-ray; 4.10 A; B=458-484.
DR   PDB; 6CRV; EM; 3.20 A; A/B/C=458-484.
DR   PDB; 6CRW; EM; 3.90 A; A/B/C=458-484.
DR   PDB; 6CRX; EM; 3.90 A; A/B/C=458-484.
DR   PDB; 6CRZ; EM; 3.30 A; A/B/C=458-484.
DR   PDB; 6CS0; EM; 3.80 A; A/B/C=458-484.
DR   PDB; 6CS1; EM; 4.60 A; A/B/C=458-484.
DR   PDB; 6CS2; EM; 4.40 A; A/B/C=458-484.
DR   PDB; 6JX7; EM; 3.31 A; A/B/C=455-484.
DR   PDB; 6OE5; X-ray; 4.10 A; A=458-484.
DR   PDB; 6Z97; EM; 3.40 A; A/B/C=458-484.
DR   PDB; 6ZGH; EM; 6.80 A; A/B/C=459-478.
DR   PDB; 6ZHD; EM; 3.70 A; A/B/C=458-484.
DR   PDB; 7A4N; EM; 2.75 A; A/B/C=458-484.
DR   PDB; 7L7F; EM; 3.24 A; E/F=458-484.
DR   PDB; 7NS6; EM; 3.18 A; I/J/K/L/M/N=458-484.
DR   PDB; 7QDG; EM; 3.40 A; A/B/C=459-486.
DR   PDB; 7QDH; EM; 4.20 A; A/B/C=459-486.
DR   PDB; 7QUR; EM; 2.27 A; A/B/C=458-484.
DR   PDB; 7QUS; EM; 2.39 A; A/B/C=458-484.
DR   PDB; 7Z6V; EM; 3.10 A; A/B/C=458-485.
DR   PDB; 7Z7X; EM; 3.30 A; A/B/C=458-485.
DR   PDB; 7Z85; EM; 3.10 A; A/B/C=458-485.
DR   PDB; 7Z86; EM; 3.40 A; A/B/C=458-485.
DR   PDB; 7Z9Q; EM; 3.60 A; A/B/C=458-485.
DR   PDB; 7Z9R; EM; 4.20 A; A/B/C=458-485.
DR   PDB; 7ZCE; EM; 3.50 A; A/B/C=458-484.
DR   PDB; 7ZCF; EM; 4.00 A; C=458-484.
DR   PDB; 7ZH1; EM; 2.48 A; A/B/C=458-484.
DR   PDB; 7ZH2; EM; 2.71 A; A/B/C=458-484.
DR   PDB; 7ZH5; EM; 3.30 A; A/B/C=458-484.
DR   PDB; 7ZJ6; EM; 2.60 A; A/B/C=458-484.
DR   PDB; 7ZJ7; EM; 3.95 A; A/B/C=459-484.
DR   PDB; 7ZJ8; EM; 3.10 A; A/B/C=458-484.
DR   PDB; 7ZR7; EM; 3.70 A; A/B/C=458-484.
DR   PDB; 7ZR8; EM; 3.70 A; A=458-484.
DR   PDB; 7ZR9; EM; 4.00 A; A/B/C=458-484.
DR   PDB; 7ZRC; EM; 3.50 A; A/B/C=458-484.
DR   PDB; 8AJA; EM; 2.59 A; A/B/C=458-484.
DR   PDB; 8AJL; EM; 2.77 A; A/B/C=458-484.
DR   PDB; 8AQS; EM; 2.92 A; A=458-484.
DR   PDB; 8AQT; EM; 4.40 A; B=460-484.
DR   PDB; 8AQU; EM; 3.22 A; B=458-484.
DR   PDB; 8AQV; EM; 2.96 A; B=460-484.
DR   PDB; 8AQW; EM; 3.30 A; B=460-484.
DR   PDB; 8BON; EM; 3.20 A; A/B/C=458-484.
DR   PDB; 8CIM; EM; 3.00 A; A/B/C=458-484.
DR   PDB; 8H3D; EM; 3.27 A; A/B/C=458-485.
DR   PDB; 8H3E; EM; 3.06 A; A/B/C=458-485.
DR   PDBsum; 1AA0; -.
DR   PDBsum; 1AVY; -.
DR   PDBsum; 1OX3; -.
DR   PDBsum; 1RFO; -.
DR   PDBsum; 1V1H; -.
DR   PDBsum; 1V1I; -.
DR   PDBsum; 2BSG; -.
DR   PDBsum; 2IBL; -.
DR   PDBsum; 2KBL; -.
DR   PDBsum; 3A1M; -.
DR   PDBsum; 3J2O; -.
DR   PDBsum; 4MMQ; -.
DR   PDBsum; 4MMR; -.
DR   PDBsum; 4MMS; -.
DR   PDBsum; 4MMT; -.
DR   PDBsum; 4MMU; -.
DR   PDBsum; 4MMV; -.
DR   PDBsum; 4NCU; -.
DR   PDBsum; 4NCV; -.
DR   PDBsum; 4NCW; -.
DR   PDBsum; 5TDL; -.
DR   PDBsum; 6APD; -.
DR   PDBsum; 6CNV; -.
DR   PDBsum; 6CRV; -.
DR   PDBsum; 6CRW; -.
DR   PDBsum; 6CRX; -.
DR   PDBsum; 6CRZ; -.
DR   PDBsum; 6CS0; -.
DR   PDBsum; 6CS1; -.
DR   PDBsum; 6CS2; -.
DR   PDBsum; 6JX7; -.
DR   PDBsum; 6OE5; -.
DR   PDBsum; 6Z97; -.
DR   PDBsum; 6ZGH; -.
DR   PDBsum; 6ZHD; -.
DR   PDBsum; 7A4N; -.
DR   PDBsum; 7L7F; -.
DR   PDBsum; 7NS6; -.
DR   PDBsum; 7QDG; -.
DR   PDBsum; 7QDH; -.
DR   PDBsum; 7QUR; -.
DR   PDBsum; 7QUS; -.
DR   PDBsum; 7Z6V; -.
DR   PDBsum; 7Z7X; -.
DR   PDBsum; 7Z85; -.
DR   PDBsum; 7Z86; -.
DR   PDBsum; 7Z9Q; -.
DR   PDBsum; 7Z9R; -.
DR   PDBsum; 7ZCE; -.
DR   PDBsum; 7ZCF; -.
DR   PDBsum; 7ZH1; -.
DR   PDBsum; 7ZH2; -.
DR   PDBsum; 7ZH5; -.
DR   PDBsum; 7ZJ6; -.
DR   PDBsum; 7ZJ7; -.
DR   PDBsum; 7ZJ8; -.
DR   PDBsum; 7ZR7; -.
DR   PDBsum; 7ZR8; -.
DR   PDBsum; 7ZR9; -.
DR   PDBsum; 7ZRC; -.
DR   PDBsum; 8AJA; -.
DR   PDBsum; 8AJL; -.
DR   PDBsum; 8AQS; -.
DR   PDBsum; 8AQT; -.
DR   PDBsum; 8AQU; -.
DR   PDBsum; 8AQV; -.
DR   PDBsum; 8AQW; -.
DR   PDBsum; 8BON; -.
DR   PDBsum; 8CIM; -.
DR   PDBsum; 8H3D; -.
DR   PDBsum; 8H3E; -.
DR   EMDB; EMD-14885; -.
DR   EMDB; EMD-15475; -.
DR   EMDB; EMD-15482; -.
DR   SMR; P10104; -.
DR   GeneID; 1258630; -.
DR   KEGG; vg:1258630; -.
DR   OrthoDB; 1450at10239; -.
DR   EvolutionaryTrace; P10104; -.
DR   Proteomes; UP000009087; Segment.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 2.
DR   InterPro; IPR012473; Fibritin_C.
DR   Pfam; PF07921; Fibritin_C; 1.
DR   PRINTS; PR01880; FIBRITIN.
DR   SUPFAM; SSF58046; Fibritin; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Coiled coil; Isopeptide bond; Late protein;
KW   Reference proteome; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   CHAIN           2..487
FT                   /note="Fibritin"
FT                   /id="PRO_0000165075"
FT   COILED          52..84
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          99..131
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          145..156
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          177..195
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          210..221
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          232..257
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          265..284
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          289..300
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          309..327
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          335..346
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          361..386
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          393..404
FT                   /evidence="ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   COILED          419..454
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:15659683,
FT                   ECO:0000269|PubMed:1878168"
FT   CROSSLNK        100
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in host protein DncV)"
FT                   /evidence="ECO:0000269|PubMed:36848932"
FT   CONFLICT        358
FT                   /note="P -> H (in Ref. 4; CAA31379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        479
FT                   /note="F -> L (in Ref. 4; CAA31379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="S -> P (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:1OX3"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:1OX3"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:1OX3"
FT   HELIX           47..81
FT                   /evidence="ECO:0007829|PDB:1OX3"
FT   HELIX           373..386
FT                   /evidence="ECO:0007829|PDB:1AA0"
FT   STRAND          389..392
FT                   /evidence="ECO:0007829|PDB:1AA0"
FT   HELIX           393..405
FT                   /evidence="ECO:0007829|PDB:1AA0"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:1AA0"
FT   HELIX           422..456
FT                   /evidence="ECO:0007829|PDB:1AVY"
FT   STRAND          465..467
FT                   /evidence="ECO:0007829|PDB:4MMV"
FT   STRAND          470..473
FT                   /evidence="ECO:0007829|PDB:4NCU"
FT   STRAND          476..479
FT                   /evidence="ECO:0007829|PDB:4NCU"
FT   HELIX           480..483
FT                   /evidence="ECO:0007829|PDB:4NCU"
SQ   SEQUENCE   487 AA;  51872 MW;  253A30F0F0ED13B5 CRC64;
     MTDIVLNDLP FVDGPPAEGQ SRISWIKNGE EILGADTQYG SEGSMNRPTV SVLRNVEVLD
     KNIGILKTSL ETANSDIKTI QGILDVSGDI EALAQIGINK KDISDLKTLT SEHTEILNGT
     NNTVDSILAD IGPFNAEANS VYRTIRNDLL WIKRELGQYT GQDINGLPVV GNPSSGMKHR
     IINNTDVITS QGIRLSELET KFIESDVGSL TIEVGNLREE LGPKPPSFSQ NVYSRLNEID
     TKQTTVESDI SAIKTSIGYP GNNSIITSVN TNTDNIASIN LELNQSGGIK QRLTVIETSI
     GSDDIPSSIK GQIKDNTTSI ESLNGIVGEN TSSGLRANVS WLNQIVGTDS SGGQPSPPGS
     LLNRVSTIET SVSGLNNAVQ NLQVEIGNNS AGIKGQVVAL NTLVNGTNPN GSTVEERGLT
     NSIKANETNI ASVTQEVNTA KGNISSLQGD VQALQEAGYI PEAPRDGQAY VRKDGEWVFL
     STFLSPA
//