CAPSD_BPFR
ID CAPSD_BPFR Reviewed; 130 AA.
AC P03614;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Enterobacteria phage fr (Bacteriophage fr).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Levivirus.
OX NCBI_TaxID=12017;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3753874;
RA Berzin V.M., Avots A.J., Jansone I.V., Tsimanis A.J.;
RT "Primary structure of a fragment of cDNA from phage fr.";
RL Bioorg. Khim. 12:149-152(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3628010; DOI=10.1093/nar/15.16.6741;
RA Berzin V.M., Avots A.J., Jansone I.V., Gintnere L., Tsimanis A.J.;
RT "Sequence of the genes coding for the A-protein and coat protein of
RT bacteriophage fr.";
RL Nucleic Acids Res. 15:6741-6741(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2207135; DOI=10.1016/0167-4781(90)90149-v;
RA Adhin M.R., Avots A.J., Berzin V.M., Overbeek G.P., van Duin J.;
RT "Complete nucleotide sequence of the group I RNA bacteriophage fr.";
RL Biochim. Biophys. Acta 1050:104-109(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-130.
RX PubMed=5584177; DOI=10.1007/bf00334062;
RA Wittmann-Liebold B., Wittmann H.G.;
RT "Coat proteins of strains of two RNA viruses: comparison of their amino
RT acid sequences.";
RL Mol. Gen. Genet. 100:358-363(1967).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=7966339; DOI=10.1006/jmbi.1994.1729;
RA Liljas L., Fridborg K., Valegaard K., Bundule M., Pumpens P.;
RT "Crystal structure of bacteriophage fr capsids at 3.5-A resolution.";
RL J. Mol. Biol. 244:279-290(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=9740779; DOI=10.1006/viro.1998.9279;
RA Axblom C., Tars K., Fridborg K., Orna L., Bundule M., Liljas L.;
RT "Structure of phage fr capsids with a deletion in the FG loop: implications
RT for viral assembly.";
RL Virology 249:80-88(1998).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 26 nm in diameter, and consisting of 89
CC capsid proteins dimers (178 capsid proteins). Involved in viral genome
CC encapsidation through the interaction between a capsid protein dimer
CC and the multiple packaging signals present in the RNA genome. The
CC capsid contains also 1 copy of the A2 maturation protein.
CC {ECO:0000250|UniProtKB:P03612}.
CC -!- FUNCTION: Acts as a translational repressor of viral replicase
CC synthesis late in infection. This latter function is the result of
CC capsid protein interaction with an RNA hairpin which contains the
CC replicase ribosome-binding site. {ECO:0000250|UniProtKB:P03612}.
CC -!- SUBUNIT: Homodimer. The capsid proteins form dimers that assemble by
CC group of 5. Twelve such pentamers are linked together with free dimers.
CC The homodimers binds to the viral RNA via an operator hairpin, but also
CC to many other RNA sequences in the viral genome; this interaction
CC probably shifts the virus from the replicative to the assembly phase
CC and ensures specific encapsidation of the viral genome.
CC {ECO:0000250|UniProtKB:P03612}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03612}. Note=The
CC shell is composed of 178 copies of the capsid protein and 1 copy of the
CC maturation protein. {ECO:0000250|UniProtKB:P03612}.
CC -!- SIMILARITY: Belongs to the Levivirus capsid protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1fr5";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1frs";
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DR EMBL; M31635; AAA32189.1; -; Genomic_RNA.
DR EMBL; X15031; CAA33136.1; -; mRNA.
DR PIR; S08018; VCBPFR.
DR PDB; 1FR5; X-ray; 3.50 A; A/B/C=2-130.
DR PDB; 1FRS; X-ray; 3.50 A; A/B/C=2-130.
DR PDBsum; 1FR5; -.
DR PDBsum; 1FRS; -.
DR SMR; P03614; -.
DR EvolutionaryTrace; P03614; -.
DR Proteomes; UP000002582; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.380.10; -; 1.
DR InterPro; IPR002703; Levivir_coat.
DR InterPro; IPR015954; Phage_RNA-type_capsid.
DR Pfam; PF01819; Levi_coat; 1.
DR SUPFAM; SSF55405; SSF55405; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing;
KW Reference proteome; RNA-binding; T=3 icosahedral capsid protein;
KW Translation regulation; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:5584177"
FT CHAIN 2..130
FT /note="Capsid protein"
FT /id="PRO_0000164840"
FT REGION 32..105
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03612"
FT CONFLICT 12..13
FT /note="DN -> ND (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..120
FT /note="NPIA -> IAPN (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1FR5"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1FR5"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 53..68
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1FR5"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:1FR5"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:1FR5"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:1FR5"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1FR5"
SQ SEQUENCE 130 AA; 13867 MW; A07C78E719428465 CRC64;
MASNFEEFVL VDNGGTGDVK VAPSNFANGV AEWISSNSRS QAYKVTCSVR QSSANNRKYT
VKVEVPKVAT QVQGGVELPV AAWRSYMNME LTIPVFATND DCALIVKALQ GTFKTGNPIA
TAIAANSGIY
