ID   CAPSD_BPSP              Reviewed;         132 AA.
AC   P09673;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
OS   Enterobacteria phage SP (Bacteriophage SP).
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Levivirales; Leviviridae; Allolevivirus.
OX   NCBI_TaxID=12027;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3399390; DOI=10.1093/nar/16.13.6205;
RA   Hirashima A., Hirose T., Inayama S., Inokuchi Y., Jacobson A.B.;
RT   "Analysis of the complete nucleotide sequence of the group IV RNA coliphage
RT   SP.";
RL   Nucleic Acids Res. 16:6205-6221(1988).
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. Binding
CC       of the capsid proteins to the viral RNA induces a conformational change
CC       required for efficient T=3 shell formation. The capsid contains also 1
CC       copy of the A2 maturation protein. {ECO:0000250|UniProtKB:P03615}.
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:P03615}.
CC   -!- SUBUNIT: Homodimer. The capsid protein dimer binds to the viral RNA via
CC       an operator hairpin, but also many other RNA sequences in the viral
CC       genome. {ECO:0000250|UniProtKB:P03615}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03615}. Note=The
CC       shell is composed of 89 dimers of the capsid protein and 1 copy of the
CC       maturation protein. {ECO:0000250|UniProtKB:P03615}.
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DR   EMBL; X07489; CAA30374.1; -; mRNA.
DR   SMR; P09673; -.
DR   Proteomes; UP000000728; 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   2: Evidence at transcript level;
KW   Capsid protein; Reference proteome; RNA-binding;
KW   T=3 icosahedral capsid protein; Translation regulation; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03615"
FT   CHAIN           2..132
FT                   /note="Capsid protein"
FT                   /id="PRO_0000164849"
SQ   SEQUENCE   132 AA;  14129 MW;  50B1E6CC6AF0A254 CRC64;
     MAKLNQVTLS KIGKNGDQTL TLTPRGVNPT NGVASLSEAG AVPALEKRVT VSVAQPSRNR
     KNFKVQIKLQ NPTACTRDAC DPSVTRSAFA DVTLSFTSYS TDEERALIRT ELAALLADPL
     IVDAIDNLNP AY