ID   CAPSA_BPT3              Reviewed;         347 AA.
AC   P19693;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   23-FEB-2022, entry version 59.
DE   RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04119};
DE   AltName: Full=Gene product 10A {ECO:0000250|UniProtKB:P19726};
DE            Short=Gp10A {ECO:0000250|UniProtKB:P19726};
DE   AltName: Full=Major head protein {ECO:0000255|HAMAP-Rule:MF_04119};
GN   Name=10;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC   Escherichia virus T3.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Luria;
RX   PubMed=2760923; DOI=10.1016/0022-2836(89)90464-6;
RA   Condreay J.P., Wright S.E., Molineux I.J.;
RT   "Nucleotide sequence and complementation studies of the gene 10 region of
RT   bacteriophage T3.";
RL   J. Mol. Biol. 207:555-561(1989).
CC   -!- FUNCTION: Assembles with the minor capsid protein to form an
CC       icosahedral capsid with a T=7 symmetry, about 60 nm in diameter, and
CC       consisting of 415 capsid proteins. The major and minor capsid proteins
CC       are incorporated into the capsid in about a 90/10 ratio respectively.
CC       Once the capsid formed, encapsidates one single copy of the viral
CC       genome. {ECO:0000250|UniProtKB:P19726}.
CC   -!- SUBUNIT: Homohexamer. Interacts with the connector protein and the
CC       minor capsid protein. Interacts with the capsid assembly scaffolding
CC       protein; capsid proteins and scaffolding proteins form building blocks
CC       that assemble to form the procapsid, each hexamer of the major capsid
CC       protein interacting with 2 scaffolding proteins. {ECO:0000255|HAMAP-
CC       Rule:MF_04119}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04119}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Major capsid protein 10A;
CC         IsoId=P19693-1; Sequence=Displayed;
CC       Name=Minor capsid protein 10B;
CC         IsoId=P19728-1; Sequence=External;
CC   -!- DOMAIN: The N-terminus interacts with an internal region of the major
CC       capsid protein subunit in an adjacent capsomere (intercapsomeric
CC       interactions) to stabilize the capsid. {ECO:0000255|HAMAP-
CC       Rule:MF_04119}.
CC   -!- MISCELLANEOUS: [Isoform Major capsid protein 10A]: Produced by
CC       conventional translation. {ECO:0000269|PubMed:2760923}.
CC   -!- SIMILARITY: Belongs to the T7virus major capsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04119}.
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; X17255; CAA35154.1; -; Genomic_DNA.
DR   EMBL; X15840; CAB57820.1; -; Genomic_DNA.
DR   PIR; S04618; VABPA3.
DR   RefSeq; NP_523335.1; NC_003298.1. [P19693-1]
DR   SMR; P19693; -.
DR   GeneID; 927448; -.
DR   KEGG; vg:927448; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04119; CAPSID_PROTEIN_T7; 1.
DR   InterPro; IPR039009; Capsid_Gp10A/Gp10B.
PE   3: Inferred from homology;
KW   Capsid protein; Ribosomal frameshifting; Virion.
FT   CHAIN           1..347
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000106520"
SQ   SEQUENCE   347 AA;  36882 MW;  16F1F9651652E152 CRC64;
     MANIQGGQQI GTNQGKGQSA ADKLALFLKV FGGEVLTAFA RTSVTMPRHM LRSIASGKSA
     QFPVIGRTKA AYLKPGENLD DKRKDIKHTE KVIHIDGLLT ADVLIYDIED AMNHYDVRAE
     YTAQLGESLA MAADGAVLAE LAGLVNLPDG SNENIEGLGK PTVLTLVKPT TGSLTDPVEL
     GKAIIAQLTI ARASLTKNYV PAADRTFYTT PDNYSAILAA LMPNAANYQA LLDPERGTIR
     NVMGFEVVEV PHLTAGGAGD TREDAPADQK HAFPATSSTT VKVALDNVVG LFQHRSAVGT
     VKLKDLALER ARRANYQADQ IIAKYAMGHG GLRPEAAGAI VLPKVSE