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Protein

ATP-dependent target DNA activator B

Gene

B

Organism
Escherichia phage Mu (Bacteriophage Mu)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-primed replication over integration. Prevents self-integration into an integrated copy of the viral genome. This mechanism is called target immunity and is achieved by two mechanisms: first, the target DNA activator B dissociates from the viral genome ends upon interaction in cis with DDE-recombinase A, which makes the viral genome ends a poor target for new insertions. Second, the interior of the viral genome may also ne protected from integration events by the target DNA activator B being strongly bound throughout the whole viral genome.8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei151Involved in DNA bindingCurated1
Sitei152Involved in DNA bindingCurated1
Sitei224R-finger; involved in ATP-bindingCurated1
Sitei268Sensor-1; involved in ATP-binding and hydrolysisCurated1
Sitei268Sensor-2; involved in ATP-binding and hydrolysisCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi21 – 40H-T-H motifSequence analysisAdd BLAST20
Nucleotide bindingi100 – 107ATPBy similarity8
DNA bindingi223 – 312Add BLAST90

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Hydrolase
Biological processDNA integration, DNA replication, Transposition, Viral DNA replication
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent target DNA activator B (EC:3.6.1.3)
Alternative name(s):
Gene product 04
Short name:
gp04
Gene product B
Short name:
gpB
MuB
Gene namesi
Name:B
Ordered Locus Names:Mup04
OrganismiEscherichia phage Mu (Bacteriophage Mu)
Taxonomic identifieri10677 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeMuvirus
Virus hostiEnterobacteriaceae [TaxID: 543]
Proteomesi
  • UP000002611 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150 – 152RRK → AGA: Complete loss of strand transfer stimulation activity. 1 Publication3
Mutagenesisi152K → A: Complete loss of strand transfer stimulation activity and self-integration protection. 1
Mutagenesisi187R → A: 20 fold decrease in ATPase activity due to impaired ATP hydrolysis. 1 Publication1
Mutagenesisi202N → A: 60 fold decrease in ATPase activity due to impaired ATP hydrolysis. No effect on ATP-binding and polymerization. 1 Publication1
Mutagenesisi220R → A: 12 fold decrease in ATPase activity due to impaired ATP-binding. 1 Publication1
Mutagenesisi224R → A: 60 fold decrease in ATPase activity due to impaired ATP-binding. No polymerization. 1 Publication1
Mutagenesisi233 – 236KTKK → ATAA: Complete loss of MuA regulation of ATPase activity. Complete loss of strand transfer stimulation activity. 1 Publication4
Mutagenesisi268R → A: Almost complete loss of ATPase activity due to impaired ATP-binding. No polymerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000776791 – 312ATP-dependent target DNA activator BAdd BLAST312

Expressioni

Inductioni

Expressed in the early phase of the viral replicative cycle. Expression of early genes is repressed by viral Repc (latency) and favored by viral Ner protein.1 Publication

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Homomultimer. Polymerizes in presence of ATP, preferentially on DNA. ATP hydrolysis triggers polymers dissassembly. Interacts with DDE-recombinase A; this interaction stimulates the catalytic activity of the latter as well as the ATPase activity of MuB followed by its dissociation from DNA.5 Publications

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP03763
SMRiP03763
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03763

Family & Domainsi

Domaini

The N-terminus contains the DNA-binding region required for target capture and an AAA+ ATPase domain. The C-terminus comprises four helices arranged in a loosely packed bundle which can also bind to dsDNA.

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

KOiK07132
OrthoDBiVOG090002CQ

Family and domain databases

Gene3Di1.10.1180.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR036733 B_transposit_C_sf
IPR009084 B_transpositn_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF13401 AAA_22, 1 hit
PF09077 Phage-MuB_C, 1 hit
SUPFAMiSSF47681 SSF47681, 1 hit
SSF52540 SSF52540, 1 hit

Sequencei

Sequence statusi: Complete.

P03763-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNISDIRAGL RTLVENEETT FKQIALESGL STGTISSFIN DKYNGDNERV
60 70 80 90 100
SQMLQRWLEK YHAVAELPEP PRFVETQTVK QIWTSMRFAS LTESIAVVCG
110 120 130 140 150
NPGVGKTEAA REYRRTNNNV WMITITPSCA SVLECLTELA FELGMNDAPR
160 170 180 190 200
RKGPLSRALR RRLEGTQGLV IIDEADHLGA EVLEELRLLQ ESTRIGLVLM
210 220 230 240 250
GNHRVYSNMT GGNRTVEFAR LFSRIAKRTA INKTKKADVK AIADAWQING
260 270 280 290 300
EKELELLQQI AQKPGALRIL NHSLRLAAMT AHGKGERVNE DYLRQAFREL
310
DLDVDISTLL RN
Length:312
Mass (Da):35,106
Last modified:July 21, 1986 - v1
Checksum:iC86455BCC2266D1C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti281A → V no nucleotide entry (PubMed:6269958).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01149 Genomic DNA Translation: CAA25599.1
M64097 Genomic DNA Translation: AAA32382.1
AF083977 Genomic DNA Translation: AAF01100.1
M11195 Genomic DNA Translation: AAA32370.1
PIRiA04388 ZBBPU2
RefSeqiNP_050608.1, NC_000929.1

Genome annotation databases

GeneIDi2636257
KEGGivg:2636257

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01149 Genomic DNA Translation: CAA25599.1
M64097 Genomic DNA Translation: AAA32382.1
AF083977 Genomic DNA Translation: AAF01100.1
M11195 Genomic DNA Translation: AAA32370.1
PIRiA04388 ZBBPU2
RefSeqiNP_050608.1, NC_000929.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F6VNMR-A223-312[»]
2MQKNMR-A1-63[»]
ProteinModelPortaliP03763
SMRiP03763
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2636257
KEGGivg:2636257

Phylogenomic databases

KOiK07132
OrthoDBiVOG090002CQ

Miscellaneous databases

EvolutionaryTraceiP03763

Family and domain databases

Gene3Di1.10.1180.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR036733 B_transposit_C_sf
IPR009084 B_transpositn_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF13401 AAA_22, 1 hit
PF09077 Phage-MuB_C, 1 hit
SUPFAMiSSF47681 SSF47681, 1 hit
SSF52540 SSF52540, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTARGB_BPMU
AccessioniPrimary (citable) accession number: P03763
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 25, 2017
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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