ID   J_BPAL3                 Reviewed;          24 AA.
AC   P69548; P08766;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   02-JUN-2021, entry version 57.
DE   RecName: Full=DNA-binding protein J;
DE   AltName: Full=J protein;
DE   AltName: Full=Small core protein;
GN   Name=J;
OS   Escherichia phage alpha3 (Bacteriophage alpha-3).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX   NCBI_TaxID=10849;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6088949; DOI=10.1007/bf00341460;
RA   Kodaira K., Taketo A.;
RT   "Isolation and some properties of bacteriophage alpha3 gene J mutant.";
RL   Mol. Gen. Genet. 195:541-543(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1532908; DOI=10.1016/0167-4781(92)90440-b;
RA   Kodaira K., Nakano K., Okada S., Taketo A.;
RT   "Nucleotide sequence of the genome of the bacteriophage alpha 3:
RT   interrelationship of the genome structure and the gene products with those
RT   of the phages, phi X174, G4 and phi K.";
RL   Biochim. Biophys. Acta 1130:277-288(1992).
CC   -!- FUNCTION: Mediates ssDNA packaging into virion, it locates to the
CC       internal surface of the capsid, thereby displacing the internal
CC       scaffolding protein B during virion formation. Protein J binds to and
CC       is packaged with the viral ssDNA. Additionally, protein J plays a role
CC       in viral attachment efficiency to the host cell.
CC       {ECO:0000250|UniProtKB:P69592}.
CC   -!- SUBUNIT: Interacts with F protein. {ECO:0000250|UniProtKB:P69592}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P69592}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P69592}. Note=situated at the
CC       interface between the internal surface of the capsid and the nucleic
CC       acid. {ECO:0000250|UniProtKB:P69592}.
CC   -!- SIMILARITY: Belongs to the microviridae J protein family.
CC       {ECO:0000305}.
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DR   EMBL; X00774; CAA25349.1; -; Genomic_DNA.
DR   EMBL; X60322; CAA42880.1; -; Genomic_DNA.
DR   PIR; S22333; S22333.
DR   RefSeq; NP_039596.1; NC_001330.1.
DR   PDB; 1M06; X-ray; 3.50 A; J=1-24.
DR   PDBsum; 1M06; -.
DR   SMR; P69548; -.
DR   GeneID; 1260696; -.
DR   KEGG; vg:1260696; -.
DR   EvolutionaryTrace; P69548; -.
DR   Proteomes; UP000002137; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006815; Microvir_J-like.
DR   Pfam; PF04726; Microvir_J; 1.
DR   PIRSF; PIRSF004161; Microvir_J; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; DNA-binding; Host cytoplasm;
KW   Reference proteome; Viral genome packaging; Viral release from host cell;
KW   Virion.
FT   CHAIN           1..24
FT                   /note="DNA-binding protein J"
FT                   /id="PRO_0000164904"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1M06"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1M06"
SQ   SEQUENCE   24 AA;  2823 MW;  0EE261CFF11F669B CRC64;
     MKKARRSPSR RKGARLWYVG GSQF