WAC_BPT4
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 03-AUG-2022, entry version 128.
DE RecName: Full=Fibritin;
DE AltName: Full=Collar protein;
DE AltName: Full=Whisker antigen control protein;
GN Name=wac;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; 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 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 [11] {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 [12] {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 [13] {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 [14] {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 [15] {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 [16] {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 [17] {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 ---------------------------------------------------------------------------
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 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 SMR; P10104; -.
DR GeneID; 1258630; -.
DR KEGG; vg:1258630; -.
DR EvolutionaryTrace; P10104; -.
DR Proteomes; UP000009087; Genome.
DR InterPro; IPR012473; Fibritin_C.
DR Pfam; PF07921; Fibritin_C; 1.
DR PRINTS; PR01880; FIBRITIN.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Coiled coil; Late protein; Reference proteome;
KW 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 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:2IBL"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2IBL"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2IBL"
FT HELIX 47..81
FT /evidence="ECO:0007829|PDB:2IBL"
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
