PKG16_BPPH2
ID PKG16_BPPH2 Reviewed; 332 AA.
AC P11014; B3VMQ2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA packaging protein {ECO:0000303|PubMed:2960820};
DE AltName: Full=ATPase gp16 {ECO:0000303|PubMed:23706809};
DE EC=3.6.4.- {ECO:0000269|PubMed:23706809};
DE AltName: Full=Gene product 16;
DE Short=gp16;
DE AltName: Full=Protein p16;
GN Name=16;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=3879485; DOI=10.1016/0378-1119(85)90054-x;
RA Garvey K.J., Saedi M.S., Ito J.;
RT "The complete sequence of Bacillus phage phi 29 gene 16: a protein required
RT for the genome encapsidation reaction.";
RL Gene 40:311-316(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=2960820; DOI=10.1016/0022-2836(87)90121-5;
RA Guo P., Peterson C., Anderson D.;
RT "Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein
RT gp16 of bacteriophage phi 29.";
RL J. Mol. Biol. 197:229-236(1987).
RN [5]
RP IDENTIFICATION IN A DNA-GP3-GP16 COMPLEX.
RX PubMed=9086269; DOI=10.1006/jmbi.1996.0843;
RA Grimes S., Anderson D.;
RT "The bacteriophage phi29 packaging proteins supercoil the DNA ends.";
RL J. Mol. Biol. 266:901-914(1997).
RN [6]
RP FUNCTION.
RX PubMed=11130079; DOI=10.1038/35047129;
RA Simpson A.A., Tao Y., Leiman P.G., Badasso M.O., He Y., Jardine P.J.,
RA Olson N.H., Morais M.C., Grimes S., Anderson D.L., Baker T.S.,
RA Rossmann M.G.;
RT "Structure of the bacteriophage phi29 DNA packaging motor.";
RL Nature 408:745-750(2000).
RN [7]
RP FUNCTION, INTERACTION WITH PACKAGING RNA, AND MUTAGENESIS OF ASP-118 AND
RP GLU-119.
RX PubMed=18674782; DOI=10.1016/j.jmb.2008.04.034;
RA Koti J.S., Morais M.C., Rajagopal R., Owen B.A., McMurray C.T.,
RA Anderson D.L.;
RT "DNA packaging motor assembly intermediate of bacteriophage phi29.";
RL J. Mol. Biol. 381:1114-1132(2008).
RN [8]
RP REVIEW.
RX PubMed=23683853; DOI=10.1016/j.copbio.2013.03.019;
RA Schwartz C., Guo P.;
RT "Ultrastable pRNA hexameric ring gearing hexameric phi29 DNA-packaging
RT motor by revolving without rotating and coiling.";
RL Curr. Opin. Biotechnol. 24:581-590(2013).
RN [9]
RP SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=23706809; DOI=10.1016/j.virol.2013.04.004;
RA Schwartz C., De Donatis G.M., Fang H., Guo P.;
RT "The ATPase of the phi29 DNA packaging motor is a member of the hexameric
RT AAA+ superfamily.";
RL Virology 443:20-27(2013).
CC -!- FUNCTION: ATPase required for the genome encapsidation reaction. Part
CC of the active packaging motor via the binding to the packaging RNA
CC (pRNA), itself fixed to the head-tail connector at the unique portal
CC vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an
CC initiation complex for DNA packaging. Provides the energy to actively
CC pump the viral DNA into the prohead. Approximately one molecule of ATP
CC is used in the packaging of 2 bp of viral DNA. After packaging, the
CC ATPase and the pRNA are released from the prohead.
CC {ECO:0000269|PubMed:11130079, ECO:0000269|PubMed:18674782,
CC ECO:0000269|PubMed:2960820, ECO:0000269|PubMed:3879485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23706809};
CC -!- SUBUNIT: Homohexamer (PubMed:18674782, PubMed:23706809). Interacts with
CC the packaging RNA (pRNA) (PubMed:18674782). Part of a DNA-gp3-gp16
CC complex (PubMed:9086269). {ECO:0000269|PubMed:23706809,
CC ECO:0000269|PubMed:9086269, ECO:0000305|PubMed:18674782}.
CC -!- SIMILARITY: Belongs to the phi29likevirus gp16 family. {ECO:0000305}.
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DR EMBL; M14782; AAA32289.1; -; Genomic_DNA.
DR EMBL; M14431; AAA88348.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96039.1; -; Genomic_DNA.
DR PIR; B33078; WMBP26.
DR RefSeq; YP_002004545.1; NC_011048.1.
DR PDB; 5HD9; X-ray; 1.94 A; A=4-197.
DR PDB; 6V1W; NMR; -; A=222-332.
DR PDB; 7CNB; X-ray; 2.32 A; A=226-332.
DR PDB; 7JQQ; EM; 4.10 A; A/B/C/D/E=1-332.
DR PDBsum; 5HD9; -.
DR PDBsum; 6V1W; -.
DR PDBsum; 7CNB; -.
DR PDBsum; 7JQQ; -.
DR SMR; P11014; -.
DR GeneID; 6446516; -.
DR KEGG; vg:6446516; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008784; Podovirus_Gp16.
DR Pfam; PF05894; Podovirus_Gp16; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Hydrolase; Late protein;
KW Nucleotide-binding; Reference proteome; RNA-binding;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..332
FT /note="DNA packaging protein"
FT /id="PRO_0000106601"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 118
FT /note="D->E: Complete loss of DNA packaging activity."
FT /evidence="ECO:0000269|PubMed:18674782"
FT MUTAGEN 119
FT /note="E->D: Complete loss of DNA packaging activity."
FT /evidence="ECO:0000269|PubMed:18674782"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5HD9"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:5HD9"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:7CNB"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:7CNB"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:7CNB"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:7CNB"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:7CNB"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:6V1W"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6V1W"
FT TURN 289..295
FT /evidence="ECO:0007829|PDB:7CNB"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:7CNB"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:7CNB"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:7CNB"
SQ SEQUENCE 332 AA; 38965 MW; FEF26A322498D505 CRC64;
MDKSLFYNPQ KMLSYDRILN FVIGARGIGK SYAMKVYPIN RFIKYGEQFI YVRRYKPELA
KVSNYFNDVA QEFPDHELVV KGRRFYIDGK LAGWAIPLSV WQSEKSNAYP NVSTIVFDEF
IREKDNSNYI PNEVSALLNL MDTVFRNRER VRCICLSNAV SVVNPYFLFF NLVPDVNKRF
NVYDDALIEI PDSLDFSSER RKTRFGRLID GTEYGEMSLD NQFIGDSQVF IEKRSKDSKF
VFSIVYNGFT LGVWVDVNQG LMYIDTAHDP STKNVYTLTT DDLNENMMLI TNYKNNYHLR
KLASAFMNGY LRFDNQVIRN IAYELFRKMR IQ
