TARGB_BPMU
ID TARGB_BPMU Reviewed; 312 AA.
AC P03763;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ATP-dependent target DNA activator B;
DE EC=3.6.1.- {ECO:0000269|PubMed:23776210};
DE AltName: Full=Gene product 04;
DE Short=gp04;
DE AltName: Full=Gene product B;
DE Short=gpB;
DE AltName: Full=MuB;
GN Name=B; OrderedLocusNames=Mup04;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6095204; DOI=10.1093/nar/12.22.8627;
RA Miller J.L., Anderson S.K., Fujita D.J., Chaconas G., Baldwin D.L.,
RA Harshey R.M.;
RT "The nucleotide sequence of the B gene of bacteriophage Mu.";
RL Nucleic Acids Res. 12:8627-8638(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Priess H., Brauer B., Schmidt C., Kamp D.;
RT "Sequence of the left end of Mu.";
RL (In) Symonds N., Toussaint A., van de Putte P., Howe M.M. (eds.);
RL Phage Mu, pp.277-296, Cold Spring Harbor Laboratory Press, New York (1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 277-312.
RX PubMed=6269958; DOI=10.1016/0378-1119(81)90111-6;
RA Engler J.A., van Bree M.P.;
RT "The nucleotide sequence and protein-coding capability of the transposable
RT element IS5.";
RL Gene 14:155-163(1981).
RN [5]
RP INDUCTION.
RX PubMed=2524470; DOI=10.1128/jb.171.6.3440-3448.1989;
RA Stoddard S.F., Howe M.M.;
RT "Localization and regulation of bacteriophage Mu promoters.";
RL J. Bacteriol. 171:3440-3448(1989).
RN [6]
RP FUNCTION.
RX PubMed=1646076; DOI=10.1016/0092-8674(91)90552-a;
RA Baker T.A., Mizuuchi M., Mizuuchi K.;
RT "MuB protein allosterically activates strand transfer by the transposase of
RT phage Mu.";
RL Cell 65:1003-1013(1991).
RN [7]
RP INTERACTION WITH DDE-RECOMBINASE A.
RX PubMed=9203582; DOI=10.1101/gad.11.12.1561;
RA Levchenko I., Yamauchi M., Baker T.A.;
RT "ClpX and MuB interact with overlapping regions of Mu transposase:
RT implications for control of the transposition pathway.";
RL Genes Dev. 11:1561-1572(1997).
RN [8]
RP FUNCTION.
RX PubMed=11298282; DOI=10.1046/j.1365-2958.2001.02364.x;
RA Roldan L.A., Baker T.A.;
RT "Differential role of the Mu B protein in phage Mu integration vs.
RT replication: mechanistic insights into two transposition pathways.";
RL Mol. Microbiol. 40:141-155(2001).
RN [9]
RP SUBUNIT.
RX PubMed=12049743; DOI=10.1016/s1097-2765(02)00514-2;
RA Greene E.C., Mizuuchi K.;
RT "Direct observation of single MuB polymers: evidence for a DNA-dependent
RT conformational change for generating an active target complex.";
RL Mol. Cell 9:1079-1089(2002).
RN [10]
RP FUNCTION.
RX PubMed=14661976; DOI=10.1021/bi035360o;
RA Goldhaber-Gordon I., Early M.H., Baker T.A.;
RT "MuA transposase separates DNA sequence recognition from catalysis.";
RL Biochemistry 42:14633-14642(2003).
RN [11]
RP INTERACTION WITH DDE-RECOMBINASE A, AND DNA-BINDING.
RX PubMed=12791691; DOI=10.1074/jbc.m303693200;
RA Coros C.J., Sekino Y., Baker T.A., Chaconas G.;
RT "Effect of mutations in the C-terminal domain of Mu B on DNA binding and
RT interactions with Mu A transposase.";
RL J. Biol. Chem. 278:31210-31217(2003).
RN [12]
RP FUNCTION.
RX PubMed=17709741; DOI=10.1073/pnas.0706564104;
RA Tan X., Mizuuchi M., Mizuuchi K.;
RT "DNA transposition target immunity and the determinants of the MuB
RT distribution patterns on DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13925-13929(2007).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17988683; DOI=10.1016/j.jmb.2007.09.079;
RA Lemberg K.M., Schweidenback C.T., Baker T.A.;
RT "The dynamic Mu transpososome: MuB activation prevents disintegration.";
RL J. Mol. Biol. 374:1158-1171(2007).
RN [14]
RP FUNCTION.
RX PubMed=20226074; DOI=10.1186/1759-8753-1-8;
RA Ge J., Lou Z., Harshey R.M.;
RT "Immunity of replicating Mu to self-integration: a novel mechanism
RT employing MuB protein.";
RL Mob. DNA 1:8-8(2010).
RN [15]
RP FUNCTION.
RX PubMed=24478936; DOI=10.4161/mge.27515;
RA Dramicanin M., Ramon-Maiques S.;
RT "MuB gives a new twist to target DNA selection.";
RL Mob. Genet. Elements 3:E27515-E27515(2013).
RN [16]
RP FUNCTION, SUBUNIT, COFACTOR, MUTAGENESIS OF 150-ARG--ARG-152; ARG-187;
RP ASN-202; ARG-220; ARG-224; 233-LYS--LYS-236 AND ARG-268, AND CATALYTIC
RP ACTIVITY.
RX PubMed=23776210; DOI=10.1073/pnas.1309499110;
RA Mizuno N., Dramicanin M., Mizuuchi M., Adam J., Wang Y., Han Y.W., Yang W.,
RA Steven A.C., Mizuuchi K., Ramon-Maiques S.;
RT "MuB is an AAA+ ATPase that forms helical filaments to control target
RT selection for DNA transposition.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E2441-E2450(2013).
RN [17]
RP STRUCTURE BY NMR OF 223-312, DNA-BINDING, AND DOMAIN.
RX PubMed=11060014; DOI=10.1093/emboj/19.21.5625;
RA Hung L.H., Chaconas G., Shaw G.S.;
RT "The solution structure of the C-terminal domain of the Mu B transposition
RT protein.";
RL EMBO J. 19:5625-5634(2000).
RN [18] {ECO:0007744|PDB:2MQK}
RP STRUCTURE BY NMR OF 1-63, AND DOMAIN.
RX PubMed=26169224; DOI=10.1016/j.jsb.2015.07.004;
RA Dramicanin M., Lopez-Mendez B., Boskovic J., Campos-Olivas R.,
RA Ramon-Maiques S.;
RT "The N-terminal domain of MuB protein has striking structural similarity to
RT DNA-binding domains and mediates MuB filament-filament interactions.";
RL J. Struct. Biol. 191:100-111(2015).
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.
CC {ECO:0000269|PubMed:11298282, ECO:0000269|PubMed:14661976,
CC ECO:0000269|PubMed:1646076, ECO:0000269|PubMed:17709741,
CC ECO:0000269|PubMed:17988683, ECO:0000269|PubMed:20226074,
CC ECO:0000269|PubMed:23776210, ECO:0000269|PubMed:24478936}.
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:23776210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23776210};
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. {ECO:0000269|PubMed:12049743,
CC ECO:0000269|PubMed:12791691, ECO:0000269|PubMed:17988683,
CC ECO:0000269|PubMed:23776210, ECO:0000269|PubMed:9203582}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
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. {ECO:0000269|PubMed:2524470}.
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 (PubMed:26169224). The central
CC region contains the ATPase module (PubMed:26169224). The C-terminus
CC comprises four helices arranged in a loosely packed bundle which can
CC bind to dsDNA (PubMed:11060014). {ECO:0000269|PubMed:11060014,
CC ECO:0000269|PubMed:26169224}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X01149; CAA25599.1; -; Genomic_DNA.
DR EMBL; M64097; AAA32382.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01100.1; -; Genomic_DNA.
DR EMBL; M11195; AAA32370.1; -; Genomic_DNA.
DR PIR; A04388; ZBBPU2.
DR RefSeq; NP_050608.1; NC_000929.1.
DR PDB; 1F6V; NMR; -; A=223-312.
DR PDB; 2MQK; NMR; -; A=1-63.
DR PDBsum; 1F6V; -.
DR PDBsum; 2MQK; -.
DR BMRB; P03763; -.
DR SMR; P03763; -.
DR GeneID; 2636257; -.
DR KEGG; vg:2636257; -.
DR EvolutionaryTrace; P03763; -.
DR Proteomes; UP000002611; 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; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA integration; DNA replication; DNA-binding;
KW Early protein; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transposition;
KW Viral DNA replication.
FT CHAIN 1..312
FT /note="ATP-dependent target DNA activator B"
FT /id="PRO_0000077679"
FT DNA_BIND 21..40
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT DNA_BIND 223..312
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000269|PubMed:23776210"
FT SITE 152
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000269|PubMed:23776210"
FT SITE 202
FT /note="Sensor-1; involved in ATP-binding and hydrolysis"
FT /evidence="ECO:0000269|PubMed:23776210"
FT SITE 224
FT /note="R-finger; involved in ATP-binding"
FT /evidence="ECO:0000269|PubMed:23776210"
FT SITE 268
FT /note="Sensor-2; involved in ATP-binding and hydrolysis"
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 150..152
FT /note="RRK->AGA: Complete loss of strand transfer
FT stimulation activity."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 152
FT /note="K->A: Complete loss of strand transfer stimulation
FT activity and self-integration protection."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 187
FT /note="R->A: 20 fold decrease in ATPase activity due to
FT impaired ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 202
FT /note="N->A: 60 fold decrease in ATPase activity due to
FT impaired ATP hydrolysis. No effect on ATP-binding and
FT polymerization."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 220
FT /note="R->A: 12 fold decrease in ATPase activity due to
FT impaired ATP-binding."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 224
FT /note="R->A: 60 fold decrease in ATPase activity due to
FT impaired ATP-binding. No polymerization."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 233..236
FT /note="KTKK->ATAA: Complete loss of MuA regulation of
FT ATPase activity. Complete loss of strand transfer
FT stimulation activity."
FT /evidence="ECO:0000269|PubMed:23776210"
FT MUTAGEN 268
FT /note="R->A: Almost complete loss of ATPase activity due to
FT impaired ATP-binding. No polymerization."
FT /evidence="ECO:0000269|PubMed:23776210"
FT CONFLICT 281
FT /note="A -> V (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2MQK"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2MQK"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2MQK"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:2MQK"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1F6V"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:1F6V"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:1F6V"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1F6V"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1F6V"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:1F6V"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1F6V"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:1F6V"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1F6V"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:1F6V"
SQ SEQUENCE 312 AA; 35106 MW; C86455BCC2266D1C CRC64;
MNISDIRAGL RTLVENEETT FKQIALESGL STGTISSFIN DKYNGDNERV SQMLQRWLEK
YHAVAELPEP PRFVETQTVK QIWTSMRFAS LTESIAVVCG NPGVGKTEAA REYRRTNNNV
WMITITPSCA SVLECLTELA FELGMNDAPR RKGPLSRALR RRLEGTQGLV IIDEADHLGA
EVLEELRLLQ ESTRIGLVLM GNHRVYSNMT GGNRTVEFAR LFSRIAKRTA INKTKKADVK
AIADAWQING EKELELLQQI AQKPGALRIL NHSLRLAAMT AHGKGERVNE DYLRQAFREL
DLDVDISTLL RN
