ID   CAPSD_BPSPP             Reviewed;         324 AA.
AC   Q38582;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 64.
DE   RecName: Full=Major capsid protein {ECO:0000305};
DE   AltName: Full=Gene product 13 {ECO:0000305};
DE            Short=gp13 {ECO:0000305};
GN   Name=13 {ECO:0000312|EMBL:CAA61870.1};
OS   Bacillus phage SPP1 (Bacteriophage SPP1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=10724 {ECO:0000312|EMBL:CAA61870.1};
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9180375; DOI=10.1006/jmbi.1997.0997;
RA   Becker B., de la Fuente N., Gassel M., Guenther D., Tavares P., Lurz R.,
RA   Trautner T.A., Alonso J.C.;
RT   "Head morphogenesis genes of the Bacillus subtilis bacteriophage SPP1.";
RL   J. Mol. Biol. 268:822-839(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA   Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT   "The complete nucleotide sequence and functional organization of Bacillus
RT   subtilis bacteriophage SPP1.";
RL   Gene 204:201-212(1997).
RN   [3]
RP   FUNCTION, INTERACTION WITH THE SCAFFOLDING PROTEIN GP11, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10656821; DOI=10.1006/jmbi.1999.3450;
RA   Droege A., Santos M.A., Stiege A.C., Alonso J.C., Lurz R., Trautner T.A.,
RA   Tavares P.;
RT   "Shape and DNA packaging activity of bacteriophage SPP1 procapsid: protein
RT   components and interactions during assembly.";
RL   J. Mol. Biol. 296:117-132(2000).
RN   [4] {ECO:0007744|PDB:4AN5}
RP   STRUCTURE BY ELECTRON MICROSCOPY (8.8 ANGSTROMS) OF THE CAPSID, FUNCTION,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH THE DECORATION PROTEIN GP12.
RX   PubMed=22514336; DOI=10.1128/jvi.00412-12;
RA   White H.E., Sherman M.B., Brasiles S., Jacquet E., Seavers P., Tavares P.,
RA   Orlova E.V.;
RT   "Capsid structure and its stability at the late stages of bacteriophage
RT   SPP1 assembly.";
RL   J. Virol. 86:6768-6777(2012).
CC   -!- FUNCTION: Capsid protein self-assembles, with the help of the
CC       scaffolding protein gp11, to form an icosahedral capsid with a T=7
CC       symmetry, about 61 nm in diameter. The capsid encapsulates the genomic
CC       DNA. {ECO:0000269|PubMed:10656821, ECO:0000269|PubMed:22514336}.
CC   -!- SUBUNIT: Interacts with the scaffolding protein gp11 (PubMed:10656821).
CC       Interacts with the decoration protein gp12 (PubMed:22514336).
CC       {ECO:0000269|PubMed:10656821, ECO:0000269|PubMed:22514336}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:10656821,
CC       ECO:0000269|PubMed:22514336}. Note=Part of the capsid.
CC       {ECO:0000269|PubMed:10656821, ECO:0000269|PubMed:22514336}.
CC   -!- SIMILARITY: Belongs to the lambda phage major capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; X89721; CAA61870.1; -; Genomic_DNA.
DR   EMBL; X97918; CAA66544.1; -; Genomic_DNA.
DR   PIR; S58142; S58142.
DR   RefSeq; NP_690674.1; NC_004166.2.
DR   PDB; 4AN5; EM; 8.80 A; A/B/C/D/E/F/G=1-324.
DR   PDB; 6R3A; EM; 4.00 A; A/B/C/D/E/F/G=2-324.
DR   PDB; 6R3B; EM; 4.50 A; A/B/C/D/E/F/G=2-324.
DR   PDB; 6RTL; EM; 4.20 A; A/B/C/D/E/F/G=2-324.
DR   PDBsum; 4AN5; -.
DR   PDBsum; 6R3A; -.
DR   PDBsum; 6R3B; -.
DR   PDBsum; 6RTL; -.
DR   SMR; Q38582; -.
DR   GeneID; 955303; -.
DR   KEGG; vg:955303; -.
DR   Proteomes; UP000002559; Genome.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR   InterPro; IPR045404; Gp13-like.
DR   Pfam; PF20036; Gp13-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Reference proteome;
KW   T=7 icosahedral capsid protein; Virion.
FT   CHAIN           1..324
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000438145"
SQ   SEQUENCE   324 AA;  35355 MW;  E3BD2B06D702160D CRC64;
     MAYTKISDVI VPELFNPYVI NTTTQLSAFF QSGIAATDDE LNALAKKAGG GSTLNMPYWN
     DLDGDSQVLN DTDDLVPQKI NAGQDKAVLI LRGNAWSSHD LAATLSGSDP MQAIGSRVAA
     YWAREMQKIV FAELAGVFSN DDMKDNKLDI SGTADGIYSA ETFVDASYKL GDHESLLTAI
     GMHSATMASA VKQDLIEFVK DSQSGIRFPT YMNKRVIVDD SMPVETLEDG TKVFTSYLFG
     AGALGYAEGQ PEVPTETARN ALGSQDILIN RKHFVLHPRG VKFTENAMAG TTPTDEELAN
     GANWQRVYDP KKIRIVQFKH RLQA