TARGB_BPD10
ID TARGB_BPD10 Reviewed; 312 AA.
AC P13771; C9DGL2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ATP-dependent target DNA activator B;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P03763};
DE AltName: Full=Gene product B;
DE Short=gpB;
DE AltName: Full=MuB;
GN Name=B;
OS Escherichia phage D108 (Bacteriophage D108).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus; unclassified Muvirus.
OX NCBI_TaxID=665033;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kropinski A.M., Villegas A., Lingohr E.J.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-312.
RX PubMed=2836266; DOI=10.1016/0378-1119(88)90584-7;
RA Waggoner B.T., Wade T., Pato M.L.;
RT "Identification of the bacteriophage D108 kil gene and of the second region
RT of sequence nonhomology with bacteriophage Mu.";
RL Gene 62:111-119(1988).
CC -!- FUNCTION: Selects the target DNA sites for transposition. Recruits DDE-
CC recombinase A to the target sites and catalytically activates it.
CC Displays non-specific DNA-binding properties. Polymerizes as helical
CC filaments around the DNA. Coating of the DNA by the target DNA
CC activator B might play a role in favoring target-primed replication
CC over integration. Prevents self-integration into an integrated copy of
CC the viral genome. This mechanism is called target immunity and is
CC achieved by two mechanisms: first, the target DNA activator B
CC dissociates from the viral genome ends upon interaction in cis with
CC DDE-recombinase A, which makes the viral genome ends a poor target for
CC new insertions. Second, the interior of the viral genome may also be
CC protected from integration events by the target DNA activator B being
CC strongly bound throughout the whole viral genome (By similarity).
CC {ECO:0000250}.
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:P03763};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homomultimer. Polymerizes in presence of ATP, preferentially
CC on DNA. ATP hydrolysis triggers polymers dissassembly. Interacts with
CC DDE-recombinase A; this interaction stimulates the catalytic activity
CC of the latter as well as the ATPase activity of MuB followed by its
CC dissociation from DNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC Expression of early genes is repressed by viral Repc (latency) and
CC favored by viral Ner protein.
CC -!- DOMAIN: The N-terminus region contains a putative DNA-binding region
CC that allows filament-filament interactions and probably favors MuB
CC polymerization and filament clustering (By similarity). The central
CC region contains the ATPase module (By similarity). The C-terminus
CC comprises four helices arranged in a loosely packed bundle which can
CC bind to dsDNA (By similarity). {ECO:0000250|UniProtKB:P03763}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18902; AAA32205.1; -; Genomic_DNA.
DR EMBL; GQ357916; ACV50263.1; -; Genomic_DNA.
DR RefSeq; YP_003335752.1; NC_013594.1.
DR BMRB; P13771; -.
DR SMR; P13771; -.
DR GeneID; 8658815; -.
DR KEGG; vg:8658815; -.
DR Proteomes; UP000000320; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1180.10; -; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR036733; B_transposit_C_sf.
DR InterPro; IPR009084; B_transpositn_C.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13401; AAA_22; 1.
DR Pfam; PF09077; Phage-MuB_C; 1.
DR SUPFAM; SSF47681; SSF47681; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA integration; DNA replication; DNA-binding; Early protein;
KW Host cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transposition; Viral DNA replication.
FT CHAIN 1..312
FT /note="ATP-dependent target DNA activator B"
FT /id="PRO_0000077678"
FT DNA_BIND 21..40
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT DNA_BIND 223..312
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT SITE 151
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT SITE 152
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT SITE 202
FT /note="Sensor-1; involved in ATP-binding and hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT SITE 224
FT /note="R-finger; involved in ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:P03763"
FT SITE 268
FT /note="Sensor-2; involved in ATP-binding and hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P03763"
SQ SEQUENCE 312 AA; 35080 MW; 3F1455A1C72AFF44 CRC64;
MNISDIRAGL RTLVENEETT FKQIALESGL STGTISSFIN DKYNGDNERV SQMLQRWLEK
YHAVAELPEP PRFVETQTVK QIWTSMRFAS LTESIAVVCG NPGVGKTEAA REYRRTNNNV
WMITITPSCA SVLECLTELA FELGMNDAPR RKGPLSRALR RRLEGTQGLV IIDEADHLGA
EVLEELRLLQ ESTRTGLVLM GNHRVYSNMT GGNRTVEFAR LFSRIAKRTA INKTKKADVK
AIADAWQING ENELELLQQI AQKPGALRIL NHSLRLAAMT AHGKGERVNE DYLRQAFREL
DLDVDISTLL RN
