ID   CAPSD_BP234             Reviewed;         409 AA.
AC   A7XXC2;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   12-AUG-2020, entry version 35.
DE   RecName: Full=Major capsid protein {ECO:0000305};
DE   AltName: Full=Gene product 89 {ECO:0000305};
DE            Short=gp89 {ECO:0000305};
DE   AltName: Full=Major head protein {ECO:0000305};
GN   ORFNames=P23p89 {ECO:0000312|EMBL:ABU96922.1};
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), FUNCTION, SUBUNIT,
RP   INTERACTION WITH THE DECORATION PROTEIN, INTERACTION WITH THE PORTAL
RP   PROTEIN, 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: Assembles to form an icosahedric capsid shell with a T=7
CC       symmetry although with a diameter of about 82 nm, which is a larger
CC       volume than the usual T=7 capsids (PubMed:30737287). A dramatic
CC       reconfiguration of the capsid shell that expands the procaspid from a
CC       diameter of 66 nm to a supersized capsid of 82 nm, allows packaging of
CC       the large viral DNA genome (PubMed:30737287). The capsid decoration
CC       protein binds the expanded capsid and stabilizes it (PubMed:30737287).
CC       {ECO:0000269|PubMed:30737287}.
CC   -!- SUBUNIT: Homomultimer (PubMed:30737287). Interacts with the portal
CC       protein (Probable). Interacts with the decoration protein
CC       (PubMed:30737287). {ECO:0000269|PubMed:30737287,
CC       ECO:0000305|PubMed:30737287}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30737287}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P03713}. Note=Forms the capsid
CC       icosahedric shell. {ECO:0000269|PubMed:30737287}.
CC   -!- SIMILARITY: Belongs to the lambda phage major capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; EU100883; ABU96922.1; -; Genomic_DNA.
DR   RefSeq; YP_001467942.1; NC_009803.1.
DR   PDB; 6I9E; X-ray; 3.74 A; A/B/C/D/E/F/G=1-409.
DR   PDB; 6IBC; X-ray; 4.39 A; A/B/C/D/E/F/G=1-409.
DR   PDBsum; 6I9E; -.
DR   PDBsum; 6IBC; -.
DR   SMR; A7XXC2; -.
DR   GeneID; 5600496; -.
DR   KEGG; vg:5600496; -.
DR   Proteomes; UP000001132; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   InterPro; IPR005564; Major_capsid_GpE.
DR   Pfam; PF03864; Phage_cap_E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host cytoplasm; Reference proteome;
KW   T=7 icosahedral capsid protein; Virion.
FT   CHAIN           1..409
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000447199"
SQ   SEQUENCE   409 AA;  46630 MW;  9DDF2D11ED25A2FF CRC64;
     MRVPININNA LARVRDPLSI GGLKFPTTKE IQEAVAAIAD KFNQENDLVD RFFPEDSTFA
     SELELYLLRT QDAEQTGMTF VHQVGSTSLP VEARVAKVDL AKATWSPLAF KESRVWDEKE
     ILYLGRLADE VQAGVINEQI AESLTWLMAR MRNRRRWLTW QVMRTGRITI QPNDPYNPNG
     LKYVIDYGVT DIELPLPQKF DAKDGNGNSA VDPIQYFRDL IKAATYFPDR RPVAIIVGPG
     FDEVLADNTF VQKYVEYEKG WVVGQNTVQP PREVYRQAAL DIFKRYTGLE VMVYDKTYRD
     QDGSVKYWIP VGELIVLNQS TGPVGRFVYT AHVAGQRNGK VVYATGPYLT VKDHLQDDPP
     YYAIIAGFHG LPQLSGYNTE DFSFHRFKWL KYANNVQSYL PPFPPKVEL