CAPSP_BPT4
ID CAPSP_BPT4 Reviewed; 427 AA.
AC P19896;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 29-SEP-2021, entry version 95.
DE RecName: Full=Capsid vertex protein {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000303|PubMed:15071181};
DE AltName: Full=Gene product 24 {ECO:0000303|PubMed:15071181};
DE AltName: Full=gp24 {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000303|PubMed:15071181};
DE Contains:
DE RecName: Full=Mature capsid vertex protein {ECO:0000255|HAMAP-Rule:MF_04113};
DE AltName: Full=gp24* {ECO:0000255|HAMAP-Rule:MF_04113};
GN Name=24;
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].
RA Yasuda G., Parker M.L., Doermann G.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 PROTEOLYTIC CLEAVAGE.
RX PubMed=1195380; DOI=10.1016/s0022-2836(75)80116-1;
RA Tsugita A., Black L.W., Showe M.K.;
RT "Protein cleavage during virus assembly: characterization of cleavage in T4
RT phage.";
RL J. Mol. Biol. 98:215-217(1975).
RN [4]
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 [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS), SUBUNIT, FUNCTION, AND
RP 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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=15878991; DOI=10.1073/pnas.0502164102;
RA Fokine A., Leiman P.G., Shneider M.M., Ahvazi B., Boeshans K.M.,
RA Steven A.C., Black L.W., Mesyanzhinov V.V., Rossmann M.G.;
RT "Structural and functional similarities between the capsid proteins of
RT bacteriophages T4 and HK97 point to a common ancestry.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7163-7168(2005).
CC -!- FUNCTION: Capsid protein that self-associates to form pentons, building
CC the capsid in association with hexamers of the major capsid protein and
CC one dodecamer of the portal protein. The capsid vertex protein self-
CC associates to form 11 pentons, building the T=13 laevo capsid in
CC association with 160 hexamers of the major capsid protein.
CC {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000269|PubMed:11162794,
CC ECO:0000269|PubMed:15071181}.
CC -!- SUBUNIT: Homopentamer. Interacts with the portal protein. Interacts
CC with the major capsid protein that forms 160 hexamers.
CC {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000269|PubMed:11162794}.
CC -!- SUBCELLULAR LOCATION: [Capsid vertex protein]: Virion. Note=Part of the
CC capsid icosahedric shell of the immature virion. The capsid contains 55
CC copies. {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000269|PubMed:11162794,
CC ECO:0000269|PubMed:15071181}.
CC -!- SUBCELLULAR LOCATION: [Mature capsid vertex protein]: Virion. Note=Part
CC of the capsid icosahedric shell of the mature virion. The capsid
CC contains 55 copies. {ECO:0000255|HAMAP-Rule:MF_04113,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:15071181}.
CC -!- PTM: A proteolytic cleavage gives rise to the mature capsid vertex
CC protein. {ECO:0000255|HAMAP-Rule:MF_04113, ECO:0000269|PubMed:1195380}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae capsid vertex family.
CC {ECO:0000305}.
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DR EMBL; AF158101; AAD42429.1; -; Genomic_DNA.
DR PIR; JF0074; GHBP24.
DR RefSeq; NP_049789.1; NC_000866.4.
DR PDB; 1YUE; X-ray; 2.90 A; A=1-427.
DR PDB; 5VF3; EM; 3.30 A; a=11-427.
DR PDBsum; 1YUE; -.
DR PDBsum; 5VF3; -.
DR SMR; P19896; -.
DR GeneID; 1258587; -.
DR KEGG; vg:1258587; -.
DR EvolutionaryTrace; P19896; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04113; CAPSID_P_T4; 1.
DR InterPro; IPR038999; CAPSP.
DR InterPro; IPR010762; Gp23/Gp24_T4-like.
DR Pfam; PF07068; Gp23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Late protein; Reference proteome; Virion.
FT CHAIN 1..427
FT /note="Capsid vertex protein"
FT /id="PRO_0000165012"
FT CHAIN 11..427
FT /note="Mature capsid vertex protein"
FT /id="PRO_0000430269"
FT SITE 10..11
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04113,
FT ECO:0000269|PubMed:1195380"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1YUE"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 89..94
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 197..221
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1YUE"
FT TURN 281..286
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 356..370
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 372..383
FT /evidence="ECO:0007829|PDB:1YUE"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:1YUE"
FT TURN 392..397
FT /evidence="ECO:0007829|PDB:1YUE"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1YUE"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:1YUE"
SQ SEQUENCE 427 AA; 46993 MW; 120631DAD028ADD5 CRC64;
MAKINELLRE STTTNSNSIG RPNLVALTRA TTKLIYSDIV ATQRTNQPVA AFYGIKYLNP
DNEFTFKTGA TYAGEAGYVD REQITELTEE SKLTLNKGDL FKYNNIVYKV LEDTPFATIE
ESDLELALQI AIVLLKVRLF SDAASTSKFE SSDSEIADAR FQINKWQTAV KSRKLKTGIT
VELAQDLEAN GFDAPNFLED LLATEMADEI NKDILQSLIT VSKRYKVTGI TDSGFIDLSY
ASAPEAGRSL YRMVCEMVSH IQKESTYTAT FCVASARAAA ILAASGWLKH KPEDDKYLSQ
NAYGFLANGL PLYCDTNSPL DYVIVGVVEN IGEKEIVGSI FYAPYTEGLD LDDPEHVGAF
KVVVDPESLQ PSIGLLVRYA LSANPYTVAK DEKEARIIDG GDMDKMAGRS DLSVLLGVKL
PKIIIDE
