ID   J_BPPHS                 Reviewed;          38 AA.
AC   P69592; P03651;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 82.
DE   RecName: Full=DNA-binding protein J;
DE   AltName: Full=J protein;
DE   AltName: Full=Small core protein;
GN   Name=J;
OS   Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
OX   NCBI_TaxID=1217068;
OH   NCBI_TaxID=498388; Escherichia coli C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=870828; DOI=10.1038/265687a0;
RA   Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA   Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL   Nature 265:687-695(1977).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-38.
RX   PubMed=911774; DOI=10.1021/bi00640a002;
RA   Freymeyer D.K. II, Shank P.R., Edgell M.H., Hutchison C.A. III,
RA   Vanaman T.C.;
RT   "Amino acid sequence of the small core protein from bacteriophage
RT   phiX174.";
RL   Biochemistry 16:4550-4556(1977).
RN   [3]
RP   FUNCTION.
RX   PubMed=9305849; DOI=10.1038/38537;
RA   Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A.,
RA   Rossmann M.G.;
RT   "Structure of a viral procapsid with molecular scaffolding.";
RL   Nature 389:308-313(1997).
RN   [4]
RP   CRYSTALLIZATION.
RX   PubMed=1370343; DOI=10.1038/355137a0;
RA   McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S.,
RA   Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L.;
RT   "Atomic structure of single-stranded DNA bacteriophage phi X174 and its
RT   functional implications.";
RL   Nature 355:137-143(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8158636; DOI=10.1006/jmbi.1994.1253;
RA   McKenna R., Ilag L.L., Rossmann M.G.;
RT   "Analysis of the single-stranded DNA bacteriophage phi X174, refined at a
RT   resolution of 3.0 A.";
RL   J. Mol. Biol. 237:517-543(1994).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=12215419; DOI=10.1016/s0022-2836(02)00734-9;
RA   Ermolenko D.N., Thomas S.T., Aurora R., Gronenborn A.M., Makhatadze G.I.;
RT   "Hydrophobic interactions at the Ccap position of the C-capping motif of
RT   alpha-helices.";
RL   J. Mol. Biol. 322:123-135(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), INTERACTION WITH F PROTEIN,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15046981; DOI=10.1016/j.jmb.2004.02.033;
RA   Bernal R.A., Hafenstein S., Esmeralda R., Fane B.A., Rossmann M.G.;
RT   "The phiX174 protein J mediates DNA packaging and viral attachment to host
RT   cells.";
RL   J. Mol. Biol. 337:1109-1122(2004).
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 (PubMed:9305849). Protein
CC       J binds to and is packaged with the viral ssDNA (PubMed:9305849).
CC       Additionally, protein J plays a role in viral attachment efficiency to
CC       the host cell (PubMed:15046981). {ECO:0000269|PubMed:15046981,
CC       ECO:0000269|PubMed:9305849}.
CC   -!- SUBUNIT: Interacts with F protein. {ECO:0000269|PubMed:15046981}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15046981}. Host
CC       cytoplasm {ECO:0000305}. Note=situated at the interface between the
CC       internal surface of the capsid and the nucleic acid.
CC       {ECO:0000269|PubMed:15046981}.
CC   -!- SIMILARITY: Belongs to the microviridae J protein family.
CC       {ECO:0000305}.
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DR   EMBL; J02482; AAA32577.1; -; Genomic_DNA.
DR   PIR; E93185; ZJBPF4.
DR   PDB; 1RB8; X-ray; 3.50 A; J=2-38.
DR   PDB; 2BPA; X-ray; 3.00 A; 3=2-38.
DR   PDBsum; 1RB8; -.
DR   PDBsum; 2BPA; -.
DR   SMR; P69592; -.
DR   DIP; DIP-61254N; -.
DR   IntAct; P69592; 1.
DR   EvolutionaryTrace; P69592; -.
DR   Proteomes; UP000005893; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; DNA-binding;
KW   Host cytoplasm; Reference proteome; Viral genome packaging;
KW   Viral release from host cell; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000269|PubMed:911774"
FT   CHAIN           2..38
FT                   /note="DNA-binding protein J"
FT                   /id="PRO_0000164907"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:2BPA"
SQ   SEQUENCE   38 AA;  4227 MW;  4C69016FD1EACAE4 CRC64;
     MSKGKKRSGA RPGRPQPLRG TKGKRKGARL WYVGGQQF