CAPSH_BPT4
ID CAPSH_BPT4 Reviewed; 521 AA.
AC P04535; Q94N06;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 23-FEB-2022, entry version 95.
DE RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000303|PubMed:6335532};
DE AltName: Full=Gene product 23 {ECO:0000303|PubMed:6335532};
DE AltName: Full=Major head protein {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000305};
DE AltName: Full=gp23 {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000303|PubMed:6335532};
DE Contains:
DE RecName: Full=Mature major capsid protein {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000305};
DE AltName: Full=gp23* {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000303|PubMed:1069310};
GN Name=gp23;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=D;
RX PubMed=6335532; DOI=10.1016/0022-2836(84)90019-6;
RA Parker M.L., Christensen A.C., Boosman A., Stockard J., Young E.T.,
RA Doermann A.H.;
RT "Nucleotide sequence of bacteriophage T4 gene 23 and the amino acid
RT sequence of its product.";
RL J. Mol. Biol. 180:399-416(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-138.
RX PubMed=6323755; DOI=10.1128/jvi.50.2.555-562.1984;
RA Champness W.C., Snyder L.;
RT "Bacteriophage T4 gol site: sequence analysis and effects of the site on
RT plasmid transformation.";
RL J. Virol. 50:555-562(1984).
RN [4]
RP PROTEIN SEQUENCE OF 295-449.
RX PubMed=3447164;
RA Tsugita A., van den Broek R.;
RT "The amino acid sequence of crystalline sheets: a proteolytic fragment of
RT the major head protein (gP23) of bacteriophage T4.";
RL Protein Seq. Data Anal. 1:99-102(1987).
RN [5]
RP FUNCTION.
RX PubMed=4612249; DOI=10.1002/jss.400020218;
RA Aebi U., Bijlenga R., van den Broek J., van den Broek H., Eiserling F.,
RA Kellenberger C., Kellenberger E., Mesyanzhinov V., Muller L., Showe M.,
RA Smith R., Steven A.;
RT "The transformation of tau particles into T4 heads. II. Transformations of
RT the surface lattice and related observations on form determination.";
RL J. Supramol. Struct. 2:253-275(1974).
RN [6]
RP PROTEIN SEQUENCE OF 66-75, PROTEOLYTIC CLEAVAGE, AND FUNCTION.
RX PubMed=1069310; DOI=10.1073/pnas.73.11.4205;
RA Isobe T., Black L.W., Tsugita A.;
RT "Protein cleavage during virus assembly: a novel specificity of assembly
RT dependent cleavage in bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:4205-4209(1976).
RN [7]
RP INTERACTION WITH THE PORTAL PROTEIN, AND SUBCELLULAR LOCATION.
RX PubMed=6406677; DOI=10.1016/s0022-2836(83)80089-8;
RA Driedonks R.A., Caldentey J.;
RT "Gene 20 product of bacteriophage T4. II. Its structural organization in
RT prehead and bacteriophage.";
RL J. Mol. Biol. 166:341-360(1983).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS), INTERACTION WITH SOC,
RP INTERACTION WITH HOC, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11162794; DOI=10.1006/viro.2000.0735;
RA Olson N.H., Gingery M., Eiserling F.A., Baker T.S.;
RT "The structure of isometric capsids of bacteriophage T4.";
RL Virology 279:385-391(2001).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15071181; DOI=10.1073/pnas.0400444101;
RA Fokine A., Chipman P.R., Leiman P.G., Mesyanzhinov V.V., Rao V.B.,
RA Rossmann M.G.;
RT "Molecular architecture of the prolate head of bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6003-6008(2004).
RN [10]
RP INTERACTION WITH HOST GROL, AND INTERACTION WITH HOST GP31.
RX PubMed=15919824; DOI=10.1073/pnas.0500048102;
RA Bakkes P.J., Faber B.W., van Heerikhuizen H., van der Vies S.M.;
RT "The T4-encoded cochaperonin, gp31, has unique properties that explain its
RT requirement for the folding of the T4 major capsid protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8144-8149(2005).
RN [11]
RP REVIEW.
RX PubMed=21129201; DOI=10.1186/1743-422x-7-356;
RA Rao V.B., Black L.W.;
RT "Structure and assembly of bacteriophage T4 head.";
RL Virol. J. 7:356-356(2010).
RN [12]
RP 3D-STRUCTURE MODELING OF 74-521, INTERACTION WITH THE CAPSID VERTEX
RP PROTEIN, INTERACTION WITH HOC, AND INTERACTION WITH SOC.
RX PubMed=22808021; DOI=10.1371/journal.pone.0038902;
RA Miernikiewicz P., Owczarek B., Piotrowicz A., Boczkowska B., Rzewucka K.,
RA Figura G., Letarov A., Kulikov E., Kopciuch A., Switala-Jelen K.,
RA Oslizlo A., Hodyra K., Gubernator J., Dabrowska K.;
RT "Recombinant expression and purification of T4 phage Hoc, Soc, gp23, gp24
RT proteins in native conformations with stability studies.";
RL PLoS ONE 7:E38902-E38902(2012).
CC -!- FUNCTION: Major capsid protein that self-associates to form hexamers,
CC building most of the capsid in association with pentons made of the
CC capsid vertex protein and one dodecamer of the portal protein. The
CC major capsid protein self-associates to form 160 hexamers, building
CC most of the T=13 laevo capsid. Folding of major capsid protein requires
CC the assistance of two chaperones, the host chaperone groL acting with
CC the phage encoded gp23-specific chaperone, gp31. The capsid also
CC contains two nonessential outer capsid proteins, Hoc and Soc, which
CC decorate the capsid surface. Through binding to adjacent gp23 subunits,
CC Soc reinforces the capsid structure. {ECO:0000255|HAMAP-Rule:MF_04117,
CC ECO:0000269|PubMed:1069310, ECO:0000269|PubMed:11162794,
CC ECO:0000269|PubMed:15071181, ECO:0000269|PubMed:4612249}.
CC -!- SUBUNIT: Homohexamer. Interacts with the portal protein. Interacts with
CC the capsid vertex protein that forms pentamers. Interacts with hoc; one
CC hoc molecule associates with each capsid hexamer. Interacts with soc;
CC this interaction reinforces the capsid structure. A total of 960
CC subunits of the major capsid protein forms the 160 hexamers.
CC {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000269|PubMed:11162794,
CC ECO:0000269|PubMed:15919824, ECO:0000269|PubMed:22808021,
CC ECO:0000269|PubMed:6406677}.
CC -!- SUBCELLULAR LOCATION: [Major capsid protein]: Virion. Note=Part of the
CC capsid icosahedric shell of the immature virion. The capsid is made of
CC 930 copies arranged as 160 hexamers. {ECO:0000255|HAMAP-Rule:MF_04117,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:6406677}.
CC -!- SUBCELLULAR LOCATION: [Mature major capsid protein]: Virion. Note=Part
CC of the icosahedric capsid shell of the mature virion.
CC {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000269|PubMed:11162794,
CC ECO:0000269|PubMed:15071181}.
CC -!- PTM: A proteolytic cleavage gives rise to the mature major capsid
CC protein during virus maturation. {ECO:0000255|HAMAP-Rule:MF_04117,
CC ECO:0000269|PubMed:1069310}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae major capsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04117}.
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DR EMBL; X01774; CAA25911.1; -; Genomic_DNA.
DR EMBL; K01765; AAA32503.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42428.1; -; Genomic_DNA.
DR PIR; A92911; VHBPT4.
DR RefSeq; NP_049787.1; NC_000866.4.
DR PDB; 5VF3; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=66-521.
DR PDB; 6UZC; EM; 4.50 A; A/B/C/D/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z=1-521.
DR PDBsum; 5VF3; -.
DR PDBsum; 6UZC; -.
DR SMR; P04535; -.
DR DIP; DIP-59725N; -.
DR IntAct; P04535; 2.
DR GeneID; 1258751; -.
DR KEGG; vg:1258751; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR HAMAP; MF_04117; CAPSID_H_T4; 1.
DR InterPro; IPR038997; CAPSID_Myoviridae.
DR InterPro; IPR010762; Gp23/Gp24_T4-like.
DR Pfam; PF07068; Gp23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Late protein;
KW Reference proteome; T=13 icosahedral capsid protein; Virion.
FT CHAIN 1..521
FT /note="Major capsid protein"
FT /id="PRO_0000164921"
FT CHAIN 66..521
FT /note="Mature major capsid protein"
FT /evidence="ECO:0000305|PubMed:1069310"
FT /id="PRO_0000430196"
FT SITE 65..66
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04117,
FT ECO:0000269|PubMed:1069310"
FT CONFLICT 311
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> N (in Ref. 1; AAA32503)"
FT /evidence="ECO:0000305"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 290..313
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 337..342
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 347..367
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 510..519
FT /evidence="ECO:0007829|PDB:5VF3"
SQ SEQUENCE 521 AA; 56022 MW; 41E495E66D96A453 CRC64;
MTIKTKAELL NKWKPLLEGE GLPEIANSKQ AIIAKIFENQ EKDFQTAPEY KDEKIAQAFG
SFLTEAEIGG DHGYNATNIA AGQTSGAVTQ IGPAVMGMVR RAIPNLIAFD ICGVQPMNSP
TGQVFALRAV YGKDPVAAGA KEAFHPMYGP DAMFSGQGAA KKFPALAAST QTTVGDIYTH
FFQETGTVYL QASVQVTIDA GATDAAKLDA EIKKQMEAGA LVEIAEGMAT SIAELQEGFN
GSTDNPWNEM GFRIDKQVIE AKSRQLKAAY SIELAQDLRA VHGMDADAEL SGILATEIML
EINREVVDWI NYSAQVGKSG MTLTPGSKAG VFDFQDPIDI RGARWAGESF KALLFQIDKE
AVEIARQTGR GEGNFIIASR NVVNVLASVD TGISYAAQGL ATGFSTDTTK SVFAGVLGGK
YRVYIDQYAK QDYFTVGYKG PNEMDAGIYY APYVALTPLR GSDPKNFQPV MGFKTRYGIG
INPFAESAAQ APASRIQSGM PSILNSLGKN AYFRRVYVKG I
