ID   CAPSH_BPAR1             Reviewed;         521 AA.
AC   Q9ZXI0;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   02-DEC-2020, entry version 58.
DE   RecName: Full=Major capsid protein {ECO:0000250|UniProtKB:P04535, ECO:0000255|HAMAP-Rule:MF_04117};
DE   AltName: Full=Gene product 23 {ECO:0000250|UniProtKB:P04535};
DE   AltName: Full=Major head protein {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000305};
DE   AltName: Full=gp23 {ECO:0000250|UniProtKB:P04535, ECO:0000255|HAMAP-Rule:MF_04117};
DE   Contains:
DE     RecName: Full=Mature major capsid protein {ECO:0000255|HAMAP-Rule:MF_04117, ECO:0000305};
DE     AltName: Full=gp23* {ECO:0000250|UniProtKB:P04535, ECO:0000255|HAMAP-Rule:MF_04117};
GN   Name=23;
OS   Escherichia phage AR1 (Bacteriophage AR1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=66711;
OH   NCBI_TaxID=83334; Escherichia coli O157:H7.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9758911; DOI=10.1007/bf02253447;
RA   Yu S.L., Ding H.C., Seah J.N., Wu K.M., Chang Y.C., Chang K.S., Tam M.F.,
RA   Syu W.J.;
RT   "Characterization of a phage specific to hemorrhagic Escherichia coli
RT   O157:H7 and disclosure of variations in host outer membrane protein ompC.";
RL   J. Biomed. Sci. 5:370-382(1998).
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:0000250|UniProtKB:P04535,
CC       ECO:0000255|HAMAP-Rule:MF_04117}.
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:0000250|UniProtKB:P04535, ECO:0000255|HAMAP-Rule:MF_04117}.
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   -!- SUBCELLULAR LOCATION: [Mature major capsid protein]: Virion. Note=Part
CC       of the capsid icosahedric shell of the mature virion. The capsid is
CC       made of 930 copies arranged as 160 hexamers. {ECO:0000255|HAMAP-
CC       Rule:MF_04117}.
CC   -!- PTM: A proteolytic cleavage gives rise to the mature major capsid
CC       protein during virus maturation. {ECO:0000255|HAMAP-Rule:MF_04117}.
CC   -!- SIMILARITY: Belongs to the T4 phage capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF022930; AAD01755.1; -; Genomic_DNA.
DR   RefSeq; YP_009167989.1; NC_027983.1.
DR   SMR; Q9ZXI0; -.
DR   GeneID; 26041918; -.
DR   KEGG; vg:26041918; -.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Capsid protein; Late protein; Virion.
FT   CHAIN           1..521
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000164923"
FT   CHAIN           66..521
FT                   /note="Mature major capsid protein"
FT                   /id="PRO_0000432355"
FT   SITE            65..66
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04117"
SQ   SEQUENCE   521 AA;  56281 MW;  A0525026738B1720 CRC64;
     MTIKTKAELL NKWKPLLEGE GLPEIANSKQ AIIAKIFENQ EKDFQTAPEY KDEKIAQAFG
     SFLTEAEIGG DHGYNATNIA AGQTSGAVTQ IGPAVMGMVR RAIPNLIAFD ICGVQPMNSP
     TGQVFALRAV YGKDPIASGA KEAFHPMYGP DAMFSGQGAA KKFAALKASD TLEVGTIYTH
     FFQDTGTVYL QATEVKQIDT SANDAAKLDA EIKKQMEAGV LVEIAEGMAT SIAELQEGFN
     GSTDNPWNEM GFRIDKQVIE AKSRQLKAAY SIELAQDLRA VHGMDADAEL SGILATEIML
     EINREVVDWI NYSAQVGKSG MTLTPGSKAG VFDFQDPIDI RGARWAGESF KALLFQIDKE
     AVEIARQTGR GEGNFIIASR NVVNVLASVD TGISYAAQGL ATGFNTDTTK SVFAGVLGGK
     YRVYIDQYAK QDYFTVGYKG PNEMDAGIYY APYVALTPLR GSDPKNFQPV MGFKTRYGIG
     INPFAESAAQ APASRIQSGM PSILNSLGKN AYFRRVYVKG I