ID   CAPSD_BPJP3             Reviewed;         130 AA.
AC   P34700;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
OS   Enterobacteria phage JP34 (Bacteriophage JP34).
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Levivirales; Leviviridae; Levivirus.
OX   NCBI_TaxID=12019;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2718383; DOI=10.1016/0042-6822(89)90371-1;
RA   Adhin M.R., Hirashima A., van Duin J.;
RT   "Nucleotide sequence from the ssRNA bacteriophage JP34 resolves the
RT   discrepancy between serological and biophysical classification.";
RL   Virology 170:238-242(1989).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04343; AAA72210.1; -; Genomic_RNA.
DR   PIR; A46324; A46324.
DR   SMR; P34700; -.
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   3: Inferred from homology;
KW   Capsid protein; RNA-binding; T=3 icosahedral capsid protein;
KW   Translation regulation; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P69171"
FT   CHAIN           2..130
FT                   /note="Capsid protein"
FT                   /id="PRO_0000164842"
FT   REGION          31..104
FT                   /note="Viral RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03612"
SQ   SEQUENCE   130 AA;  13742 MW;  BEBDC343B966D013 CRC64;
     MATLRSFVLV DNGGTGDVTV VPVSNANGVA EWLSNNSRSQ AYRVTASYRA SGADKRKYTI
     KLEVPKIVTQ VVNGVELPVS AWKAYASIDL TIPIFAATDD VTVISKSLAG LFKVGNPIAD
     AISSQSGFYA