ID   PKG16_BPB03             Reviewed;         321 AA.
AC   Q37897;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA packaging protein {ECO:0000250|UniProtKB:P11014};
DE   AltName: Full=ATPase gp16 {ECO:0000250|UniProtKB:P11014};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P11014};
DE   AltName: Full=Gene product 16;
DE            Short=gp16;
DE   AltName: Full=Protein p16;
GN   Name=16;
OS   Bacillus phage B103 (Bacteriophage B103).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Beecentumtrevirus.
OX   NCBI_TaxID=10778;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9358052; DOI=10.1016/s0378-1119(97)00363-6;
RA   Pecenkova T., Benes V., Paces J., Vlcek C., Paces V.;
RT   "Bacteriophage B103: complete DNA sequence of its genome and relationship
RT   to other Bacillus phages.";
RL   Gene 199:157-163(1997).
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:0000250|UniProtKB:P11014}.
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:0000250|UniProtKB:P11014};
CC   -!- SUBUNIT: Homohexamer. Interacts with the packaging RNA. Part of a DNA-
CC       gp3-gp16 complex. {ECO:0000250|UniProtKB:P11014}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus gp16 family. {ECO:0000305}.
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DR   EMBL; X99260; CAA67647.1; -; Genomic_DNA.
DR   RefSeq; NP_690650.1; NC_004165.1.
DR   SMR; Q37897; -.
DR   GeneID; 955369; -.
DR   KEGG; vg:955369; -.
DR   Proteomes; UP000000971; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008784; Podovirus_Gp16.
DR   Pfam; PF05894; Podovirus_Gp16; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Late protein; Nucleotide-binding;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..321
FT                   /note="DNA packaging protein"
FT                   /id="PRO_0000106600"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  37651 MW;  6BB405E6E07BF1F3 CRC64;
     MLSYDRILNF VIGARGIGKS YAMKKHPIKR FIKHGEQFIY VRRYKPELKK IGNYFNDIAQ
     EFPNHEFKVK GRQFCIDGKL TGWAIPLSAW QSEKSNAYPM VTTIIFDEFI RERDNSGYIP
     NEVDALLNLM DTVFRTRENG RCICLSNAVS IINPYFVYFG LVPDINKRFN AYKHILIEIP
     DSKDFSDERR KTKFGQLIDG TEYGEMSLDN EFVNDSDVFI EKRSKNSKFV FSIVYKGMRM
     GVWVDTQQML LYLTTDHDPS TKNVYALTAD DLEEGMILVS NYKKNYHIRK LCSAFMNGQL
     RFDNQLMRTI GYEMFKKMRV Q