ID   DECO_BP234              Reviewed;         146 AA.
AC   A7XXC1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   12-AUG-2020, entry version 22.
DE   RecName: Full=Decoration protein {ECO:0000305};
DE   AltName: Full=Auxilliary protein {ECO:0000303|PubMed:30737287};
DE   AltName: Full=Gene product 88 {ECO:0000305};
DE            Short=gp88 {ECO:0000305};
GN   ORFNames=P23p88 {ECO:0000312|EMBL:ABU96921.1};
OS   Thermus virus P23-45 (Thermus thermophilus phage P23-45).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Oshimavirus.
OX   NCBI_TaxID=466051;
OH   NCBI_TaxID=274; Thermus thermophilus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18355836; DOI=10.1016/j.jmb.2008.02.018;
RA   Minakhin L., Goel M., Berdygulova Z., Ramanculov E., Florens L., Glazko G.,
RA   Karamychev V.N., Slesarev A.I., Kozyavkin S.A., Khromov I., Ackermann H.W.,
RA   Washburn M., Mushegian A., Severinov K.;
RT   "Genome comparison and proteomic characterization of Thermus thermophilus
RT   bacteriophages P23-45 and P74-26: siphoviruses with triplex-forming
RT   sequences and the longest known tails.";
RL   J. Mol. Biol. 378:468-480(2008).
RN   [2]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.74 ANGSTROMS), SUBUNIT, INTERACTION
RP   WITH THE CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=30737287; DOI=10.1073/pnas.1813204116;
RA   Bayfield O.W., Klimuk E., Winkler D.C., Hesketh E.L., Chechik M., Cheng N.,
RA   Dykeman E.C., Minakhin L., Ranson N.A., Severinov K., Steven A.C.,
RA   Antson A.A.;
RT   "Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with
RT   supersized T=7 capsids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:3556-3561(2019).
CC   -!- FUNCTION: Cooperatively binds the expanded capsid, thereby stabilizing
CC       the mature capsid shell and allowing the large viral DNA to be packaged
CC       (PubMed:30737287). Trimers of capsid decoration proteins molecules are
CC       located at local and icosahedral threefold axes and stabilize the
CC       expanded capsid, which shows increased spacing between capsomers
CC       (PubMed:30737287). {ECO:0000269|PubMed:30737287}.
CC   -!- SUBUNIT: Homotrimer (PubMed:30737287). Interacts with the major capsid
CC       protein (PubMed:30737287). {ECO:0000269|PubMed:30737287}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30737287}.
CC       Note=Located between the capsid hexons. {ECO:0000269|PubMed:30737287}.
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; EU100883; ABU96921.1; -; Genomic_DNA.
DR   RefSeq; YP_001467941.1; NC_009803.1.
DR   PDB; 6I9E; X-ray; 3.74 A; H/I/J/K/L/M/N=1-146.
DR   PDBsum; 6I9E; -.
DR   SMR; A7XXC1; -.
DR   GeneID; 5600470; -.
DR   KEGG; vg:5600470; -.
DR   Proteomes; UP000001132; Genome.
DR   GO; GO:0098021; C:viral capsid, decoration; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid decoration protein; Capsid protein;
KW   Reference proteome; Virion.
FT   CHAIN           1..146
FT                   /note="Decoration protein"
FT                   /id="PRO_0000447198"
SQ   SEQUENCE   146 AA;  16641 MW;  BD93BC878E19E534 CRC64;
     MDKVKLFQTI GRVEYWERVP RLHAYGVFAL PFPMDPDVNW AQWFTGPHPR AFLVSIHKYG
     PKAGHVYPTN LTDEDALLNV IGMVLDGHDY ENDPNVTVTL KAAVPIEYVQ QDPQAPALQP
     HQAVLDAAEV LKLKVIKGHY FFDYTR