CAPSA_BPT7
ID CAPSA_BPT7 Reviewed; 345 AA.
AC P19726; P03717;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04119, ECO:0000303|PubMed:20962334};
DE AltName: Full=Gene product 10A {ECO:0000303|PubMed:20962334};
DE Short=Gp10A {ECO:0000303|PubMed:20962334};
DE AltName: Full=Major head protein {ECO:0000255|HAMAP-Rule:MF_04119};
GN OrderedLocusNames=10;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=1938901; DOI=10.1128/jb.173.21.6998-7003.1991;
RA Condron B.G., Atkins J.F., Gesteland R.F.;
RT "Frameshifting in gene 10 of bacteriophage T7.";
RL J. Bacteriol. 173:6998-7003(1991).
RN [3]
RP INTERACTION WITH THE CONNECTOR PROTEIN.
RX PubMed=23580619; DOI=10.1073/pnas.1215563110;
RA Guo F., Liu Z., Vago F., Ren Y., Wu W., Wright E.T., Serwer P., Jiang W.;
RT "Visualization of uncorrelated, tandem symmetry mismatches in the internal
RT genome packaging apparatus of bacteriophage T7.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6811-6816(2013).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23884409; DOI=10.1074/jbc.m113.491209;
RA Cuervo A., Pulido-Cid M., Chagoyen M., Arranz R., Gonzalez-Garcia V.A.,
RA Garcia-Doval C., Caston J.R., Valpuesta J.M., van Raaij M.J.,
RA Martin-Benito J., Carrascosa J.L.;
RT "Structural characterization of the bacteriophage T7 tail machinery.";
RL J. Biol. Chem. 288:26290-26299(2013).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (10.8 ANGSTROMS), INTERACTION WITH THE
RP MINOR CAPSID PROTEIN, AND FUNCTION.
RX PubMed=20962334; DOI=10.1074/jbc.m110.187211;
RA Ionel A., Velazquez-Muriel J.A., Luque D., Cuervo A., Caston J.R.,
RA Valpuesta J.M., Martin-Benito J., Carrascosa J.L.;
RT "Molecular rearrangements involved in the capsid shell maturation of
RT bacteriophage T7.";
RL J. Biol. Chem. 286:234-242(2011).
RN [6] {ECO:0007744|PDB:3J7V, ECO:0007744|PDB:3J7W, ECO:0007744|PDB:3J7X}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), INTERACTION WITH THE
RP CAPSID ASSEMBLY SCAFFOLDING PROTEIN, SUBUNIT, AND DOMAIN.
RX PubMed=25313071; DOI=10.1073/pnas.1407020111;
RA Guo F., Liu Z., Fang P.A., Zhang Q., Wright E.T., Wu W., Zhang C., Vago F.,
RA Ren Y., Jakana J., Chiu W., Serwer P., Jiang W.;
RT "Capsid expansion mechanism of bacteriophage T7 revealed by multistate
RT atomic models derived from cryo-EM reconstructions.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4606-E4614(2014).
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 is formed, encapsidates one single copy of the viral
CC genome. {ECO:0000269|PubMed:20962334}.
CC -!- SUBUNIT: Homohexamer (PubMed:25313071). Interacts with the connector
CC protein and the minor capsid protein (PubMed:20962334,
CC PubMed:23580619). 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 (PubMed:25313071).
CC {ECO:0000255|HAMAP-Rule:MF_04119, ECO:0000269|PubMed:20962334,
CC ECO:0000269|PubMed:23580619, ECO:0000269|PubMed:25313071}.
CC -!- INTERACTION:
CC P19726; P19726: 10; NbExp=2; IntAct=EBI-8665048, EBI-8665048;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04119,
CC ECO:0000269|PubMed:20962334, ECO:0000269|PubMed:23884409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=VC10A; Synonyms=Major capsid protein 10A;
CC IsoId=P19726-1; Sequence=Displayed;
CC Name=VC10B; Synonyms=Minor capsid protein 10B;
CC IsoId=P19727-1; 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, ECO:0000269|PubMed:25313071}.
CC -!- MISCELLANEOUS: [Isoform VC10A]: Produced by conventional translation.
CC {ECO:0000269|PubMed:1938901}.
CC -!- SIMILARITY: Belongs to the T7virus major capsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04119}.
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DR EMBL; V01146; CAA24427.1; -; Genomic_DNA.
DR PIR; A04344; VABPA7.
DR RefSeq; NP_041998.1; NC_001604.1. [P19726-1]
DR PDB; 2XVR; EM; 10.80 A; A/B/C/D/E/F/G=1-345.
DR PDB; 3IZG; EM; -; A/B/C/D/E/F/G=1-345.
DR PDB; 3J7V; EM; 4.50 A; A/B/C/D/E/F/G=1-345.
DR PDB; 3J7W; EM; 3.50 A; A/B/C/D/E/F/G=1-345.
DR PDB; 3J7X; EM; 3.80 A; A/B/C/D/E/F/G=1-345.
DR PDBsum; 2XVR; -.
DR PDBsum; 3IZG; -.
DR PDBsum; 3J7V; -.
DR PDBsum; 3J7W; -.
DR PDBsum; 3J7X; -.
DR SMR; P19726; -.
DR DIP; DIP-29317N; -.
DR IntAct; P19726; 1.
DR MINT; P19726; -.
DR GeneID; 1261026; -.
DR KEGG; vg:1261026; -.
DR EvolutionaryTrace; P19726; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR HAMAP; MF_04119; CAPSID_PROTEIN_T7; 1.
DR InterPro; IPR039009; Capsid_Gp10A/Gp10B.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; Ribosomal frameshifting;
KW Virion.
FT CHAIN 1..345
FT /note="Major capsid protein"
FT /id="PRO_0000106522"
FT REGION 11..25
FT /note="Intercapsomeric interactions"
FT /evidence="ECO:0000269|PubMed:25313071"
FT REGION 152..156
FT /note="Intercapsomeric interactions"
FT /evidence="ECO:0000269|PubMed:25313071"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3J7W"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3J7W"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:3J7W"
FT HELIX 118..147
FT /evidence="ECO:0007829|PDB:3J7W"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:3J7W"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3J7W"
FT HELIX 178..196
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3J7W"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3J7W"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 295..313
FT /evidence="ECO:0007829|PDB:3J7W"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 318..330
FT /evidence="ECO:0007829|PDB:3J7W"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3J7W"
SQ SEQUENCE 345 AA; 36546 MW; 0CB7973954FE69F5 CRC64;
MASMTGGQQM GTNQGKGVVA AGDKLALFLK VFGGEVLTAF ARTSVTTSRH MVRSISSGKS
AQFPVLGRTQ AAYLAPGENL DDKRKDIKHT EKVITIDGLL TADVLIYDIE DAMNHYDVRS
EYTSQLGESL AMAADGAVLA EIAGLCNVES KYNENIEGLG TATVIETTQN KAALTDQVAL
GKEIIAALTK ARAALTKNYV PAADRVFYCD PDSYSAILAA LMPNAANYAA LIDPEKGSIR
NVMGFEVVEV PHLTAGGAGT AREGTTGQKH VFPANKGEGN VKVAKDNVIG LFMHRSAVGT
VKLRDLALER ARRANFQADQ IIAKYAMGHG GLRPEAAGAV VFKVE
