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Protein

DDE-recombinase A

Gene

A

Organism
Enterobacteria phage Mu (Bacteriophage Mu)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair.
Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE-recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target-primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome.
Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication.

Cofactori

Mg2+2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi269 – 2691Magnesium; catalytic
Metal bindingi336 – 3361Magnesium; catalyticCurated
Metal bindingi392 – 3921Magnesium; catalytic

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi176 – 19621H-T-H motif; viral genome ends bindingPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • double-stranded DNA endodeoxyribonuclease activity Source: CACAO
  • ligase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • transposase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Nuclease

Keywords - Biological processi

DNA excision, DNA integration, DNA recombination, DNA replication, Transposition, Viral DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DDE-recombinase A (EC:3.1.22.-, EC:6.5.1.-)
Alternative name(s):
DDE-transposase A
Gene product 03
Short name:
gp03
Gene product A
Short name:
gpA
MuA
Gene namesi
Name:A
Ordered Locus Names:Mup03
OrganismiEnterobacteria phage Mu (Bacteriophage Mu)
Taxonomic identifieri10677 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeMulikevirus
Virus hostiEnterobacteriaceae [TaxID: 543]
Proteomesi
  • UP000002611 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • host Source: UniProtKB
  • host cell cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi269 – 2691D → N: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications
Mutagenesisi269 – 2691D → V: Loss of DNA-protein assembly. 2 Publications
Mutagenesisi294 – 2941D → N: Almost complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications
Mutagenesisi348 – 3481G → D: Loss of DNA-protein assembly. 1 Publication
Mutagenesisi392 – 3921E → A: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications
Mutagenesisi392 – 3921E → Q: Complete loss of both the DNA cleavage and joining activities without bloing tetramer assembly. 2 Publications
Mutagenesisi550 – 5501D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi556 – 5561E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi558 – 5581E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi567 – 5671D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi573 – 5731E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi575 – 5795RRRQK → KKKQR: No effect on DNA-binding and flaps endonuclease activity. 1 Publication
Mutagenesisi575 – 5795RRRQK → LQLQQ: Almost complete loss of flaps endonuclease activity, DNA-binding and transpososome assembly. 1 Publication
Mutagenesisi576 – 5794RRQK → QRQQ: Partial loss of flaps endonuclease activity resulting in delayed flaps removal. Complete loss of DNA-binding.
Mutagenesisi596 – 5961D → N: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi599 – 5991E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication
Mutagenesisi602 – 6021E → Q: Almost no effect on both the DNA cleavage and joining activities without bloing tetramer assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663DDE-recombinase APRO_0000077584Add
BLAST

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

Homotetramer. Part of the transpososome complex composed of a DDE-recombinase A tetramer synapsing the ends of the viral genome and the enhancer element. Interacts with target DNA activator B; this interaction brings DDE-recombinase A to the transposition target site. Interacts with host ClpX; this interaction remodels the transpososome for replication and is required for the flaps endonuclease activity of DDE-recombinase A. Binds (via N-terminus) three distinct recognition sites in the AttR and AttL regions of the viral genome ends: R1, R2, and R3 on the right end and L1, L2, and L3 on the left, not all of which are essential for transposition. The active transpososome is formed by three DDE-recombinase A subunits tightly bound to R1, R2, L1 plus a fourth subunit tightly bound in the complex but weakly bound to the L2 recognition site. Only two subunits out of the four involved are responsible for catalysis. Each subunit performs the cleavage and joining reactions for one DNA end and acts in trans, ensuring the reaction is only initiated when both viral genome ends are paired.4 Publications

Protein-protein interaction databases

DIPiDIP-59984N.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Beta strandi14 – 163Combined sources
Helixi20 – 289Combined sources
Beta strandi40 – 434Combined sources
Turni50 – 523Combined sources
Helixi55 – 6410Combined sources
Beta strandi69 – 724Combined sources
Helixi90 – 989Combined sources
Helixi101 – 12222Combined sources
Helixi127 – 13711Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 15312Combined sources
Helixi157 – 1659Combined sources
Helixi182 – 19211Combined sources
Helixi200 – 21415Combined sources
Helixi221 – 23111Combined sources
Helixi233 – 2408Combined sources
Turni262 – 2643Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi288 – 2947Combined sources
Turni295 – 2973Combined sources
Beta strandi300 – 3089Combined sources
Helixi311 – 32515Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi338 – 3403Combined sources
Turni341 – 3466Combined sources
Turni351 – 3544Combined sources
Helixi363 – 3708Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi377 – 3793Combined sources
Turni381 – 3833Combined sources
Helixi393 – 3953Combined sources
Helixi397 – 4026Combined sources
Turni403 – 4064Combined sources
Helixi408 – 4103Combined sources
Turni411 – 4133Combined sources
Helixi424 – 4263Combined sources
Turni427 – 4293Combined sources
Helixi433 – 44917Combined sources
Turni456 – 4616Combined sources
Helixi464 – 4729Combined sources
Helixi482 – 4876Combined sources
Beta strandi489 – 4924Combined sources
Beta strandi501 – 5077Combined sources
Beta strandi514 – 5196Combined sources
Helixi521 – 5233Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi529 – 5357Combined sources
Helixi537 – 5393Combined sources
Turni540 – 5423Combined sources
Beta strandi543 – 5475Combined sources
Beta strandi553 – 5597Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCMX-ray2.80A/B248-574[»]
1BCOX-ray2.40A248-574[»]
1TNSNMR-A1-76[»]
1TNTNMR-A1-76[»]
2EZHNMR-A174-247[»]
2EZINMR-A174-247[»]
2EZKNMR-A77-174[»]
2EZLNMR-A77-174[»]
4FCYX-ray3.71A/B77-605[»]
ProteinModelPortaliP07636.
SMRiP07636. Positions 1-247, 257-560.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6969HTH Mu-type; 1-alpha, viral IAS bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 174981-beta, viral genome ends bindingAdd
BLAST
Regioni175 – 247731-gamma, viral genome ends bindingAdd
BLAST
Regioni249 – 490242CatalyticAdd
BLAST
Regioni491 – 605115Target DNA capture and bendingAdd
BLAST
Regioni575 – 5795Involved in flaps endonuclease activity
Regioni605 – 66359Interaction with MuBAdd
BLAST
Regioni656 – 6638Interaction with and host ClpX

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi269 – 392124DDEAdd
BLAST

Domaini

The catalytic domain contains two distinct activities, the cleavage and strand transfer activity and the flaps endonuclease activity. The N-terminal HTH Mu-type domain 1-alpha is responsible for sequence-specific DNA binding to the IAS. Two adjacent regions 1-beta and 1-gamma bind to the ends of the viral genome.
Contains a D-x(n)-D-x(35)-E motif, named for the conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. These residues coordinate the metal ions required for nucleophile activation. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities (By similarity).By similarity

Sequence similaritiesi

Contains 1 HTH Mu-type domain.Curated

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 2 hits.
2.30.30.130. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR009057. Homeodomain-like.
IPR003314. Mu-type_HTH.
IPR015126. Mu_I-gamma.
IPR004189. Phage_Mu_transposase.
IPR012337. RNaseH-like_dom.
IPR015378. Transposase-like_Mu_C.
IPR009004. Transposase_Mu_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02914. DDE_2. 1 hit.
PF02316. HTH_Tnp_Mu_1. 1 hit.
PF09039. HTH_Tnp_Mu_2. 1 hit.
PF09299. Mu-transpos_C. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF46955. SSF46955. 1 hit.
SSF50610. SSF50610. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS51702. HTH_MU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELWVSPKEC ANLPGLPKTS AGVIYVAKKQ GWQNRTRAGV KGGKAIEYNA
60 70 80 90 100
NSLPVEAKAA LLLRQGEIET SLGYFEIARP TLEAHDYDRE ALWSKWDNAS
110 120 130 140 150
DSQRRLAEKW LPAVQAADEM LNQGISTKTA FATVAGHYQV SASTLRDKYY
160 170 180 190 200
QVQKFAKPDW AAALVDGRGA SRRNVHKSEF DEDAWQFLIA DYLRPEKPAF
210 220 230 240 250
RKCYERLELA AREHGWSIPS RATAFRRIQQ LDEAMVVACR EGEHALMHLI
260 270 280 290 300
PAQQRTVEHL DAMQWINGDG YLHNVFVRWF NGDVIRPKTW FWQDVKTRKI
310 320 330 340 350
LGWRCDVSEN IDSIRLSFMD VVTRYGIPED FHITIDNTRG AANKWLTGGA
360 370 380 390 400
PNRYRFKVKE DDPKGLFLLM GAKMHWTSVV AGKGWGQAKP VERAFGVGGL
410 420 430 440 450
EEYVDKHPAL AGAYTGPNPQ AKPDNYGDRA VDAELFLKTL AEGVAMFNAR
460 470 480 490 500
TGRETEMCGG KLSFDDVFER EYARTIVRKP TEEQKRMLLL PAEAVNVSRK
510 520 530 540 550
GEFTLKVGGS LKGAKNVYYN MALMNAGVKK VVVRFDPQQL HSTVYCYTLD
560 570 580 590 600
GRFICEAECL APVAFNDAAA GREYRRRQKQ LKSATKAAIK AQKQMDALEV
610 620 630 640 650
AELLPQIAEP AAPESRIVGI FRPSGNTERV KNQERDDEYE TERDEYLNHS
660
LDILEQNRRK KAI
Length:663
Mass (Da):75,003
Last modified:February 1, 1996 - v2
Checksum:iB882CFDCBFC0B2E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661G → R in CAA24236 (PubMed:6222246).Curated
Sequence conflicti408 – 4081P → S in AAA32379 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11195 Genomic DNA. Translation: AAA32369.1.
M64097 Genomic DNA. Translation: AAA32379.1.
AF083977 Genomic DNA. Translation: AAF01083.1.
V01464 Genomic DNA. Translation: CAA24713.1.
V00868 Genomic DNA. Translation: CAA24236.1.
PIRiA24746. TQBPU.
RefSeqiNP_050607.1. NC_000929.1.

Genome annotation databases

GeneIDi2636292.
KEGGivg:2636292.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11195 Genomic DNA. Translation: AAA32369.1.
M64097 Genomic DNA. Translation: AAA32379.1.
AF083977 Genomic DNA. Translation: AAF01083.1.
V01464 Genomic DNA. Translation: CAA24713.1.
V00868 Genomic DNA. Translation: CAA24236.1.
PIRiA24746. TQBPU.
RefSeqiNP_050607.1. NC_000929.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCMX-ray2.80A/B248-574[»]
1BCOX-ray2.40A248-574[»]
1TNSNMR-A1-76[»]
1TNTNMR-A1-76[»]
2EZHNMR-A174-247[»]
2EZINMR-A174-247[»]
2EZKNMR-A77-174[»]
2EZLNMR-A77-174[»]
4FCYX-ray3.71A/B77-605[»]
ProteinModelPortaliP07636.
SMRiP07636. Positions 1-247, 257-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59984N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2636292.
KEGGivg:2636292.

Miscellaneous databases

EvolutionaryTraceiP07636.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.10.60. 2 hits.
2.30.30.130. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR009057. Homeodomain-like.
IPR003314. Mu-type_HTH.
IPR015126. Mu_I-gamma.
IPR004189. Phage_Mu_transposase.
IPR012337. RNaseH-like_dom.
IPR015378. Transposase-like_Mu_C.
IPR009004. Transposase_Mu_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02914. DDE_2. 1 hit.
PF02316. HTH_Tnp_Mu_1. 1 hit.
PF09039. HTH_Tnp_Mu_2. 1 hit.
PF09299. Mu-transpos_C. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF46955. SSF46955. 1 hit.
SSF50610. SSF50610. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS51702. HTH_MU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of phage mu transposase: homology to mu repressor."
    Harshey R.M., Getzoff E.D., Baldwin D.L., Miller J.L., Chaconas G.
    Proc. Natl. Acad. Sci. U.S.A. 82:7676-7680(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Sequence of the left end of Mu."
    Priess H., Brauer B., Schmidt C., Kamp D.
    (In) Symonds N., Toussaint A., van de Putte P., Howe M.M. (eds.); Phage Mu, pp.277-296, Cold Spring Harbor Laboratory Press, New York (1987)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like prophages in Haemophilus, Neisseria and Deinococcus."
    Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.
    J. Mol. Biol. 317:337-359(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Nucleotide sequence of the immunity region of bacteriophage Mu."
    Priess H., Kamp D., Kahmann R., Braeuer B., Delius H.
    Mol. Gen. Genet. 186:315-321(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
  5. "The products of gene A of the related phages Mu and D108 differ in their specificities."
    Toussaint A., Faelen M., Desmet L., Allet B.
    Mol. Gen. Genet. 190:70-79(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84.
  6. "Action at a distance in Mu DNA transposition: an enhancer-like element is the site of action of supercoiling relief activity by integration host factor (IHF)."
    Surette M.G., Lavoie B.D., Chaconas G.
    EMBO J. 8:3483-3489(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Localization and regulation of bacteriophage Mu promoters."
    Stoddard S.F., Howe M.M.
    J. Bacteriol. 171:3440-3448(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome."
    Lavoie B.D., Chan B.S., Allison R.G., Chaconas G.
    EMBO J. 10:3051-3059(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION IN THE TRANSPOSOSOME COMPLEX.
  9. "Identification of residues in the Mu transposase essential for catalysis."
    Baker T.A., Luo L.
    Proc. Natl. Acad. Sci. U.S.A. 91:6654-6658(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, MUTAGENESIS OF ASP-269; ASP-294; GLU-392; ASP-550; GLU-556; GLU-558; ASP-567; GLU-573; ASP-596; GLU-599 AND GLU-602.
  10. "Step-arrest mutants of phage Mu transposase. Implications in DNA-protein assembly, Mu end cleavage, and strand transfer."
    Kim K., Namgoong S.Y., Jayaram M., Harshey R.M.
    J. Biol. Chem. 270:1472-1479(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-269; ASP-294; GLY-348 AND GLU-392.
  11. "A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage."
    Wu Z., Chaconas G.
    EMBO J. 14:3835-3843(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF C-TERMINAL REGION.
  12. "The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition."
    Clubb R.T., Mizuuchi M., Huth J.R., Omichinski J.G., Savilahti H., Mizuuchi K., Clore G.M., Gronenborn A.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:1146-1150(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  13. "ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway."
    Levchenko I., Yamauchi M., Baker T.A.
    Genes Dev. 11:1561-1572(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUB AND HOST CLPX.
  14. "The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition."
    Namgoong S.Y., Harshey R.M.
    EMBO J. 17:3775-3785(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  15. "Differential role of the Mu B protein in phage Mu integration vs. replication: mechanistic insights into two transposition pathways."
    Roldan L.A., Baker T.A.
    Mol. Microbiol. 40:141-155(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "DNA recognition sites activate MuA transposase to perform transposition of non-Mu DNA."
    Goldhaber-Gordon I., Williams T.L., Baker T.A.
    J. Biol. Chem. 277:7694-7702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Sequence and positional requirements for DNA sites in a mu transpososome."
    Goldhaber-Gordon I., Early M.H., Gray M.K., Baker T.A.
    J. Biol. Chem. 277:7703-7712(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Path of DNA within the Mu transpososome. Transposase interactions bridging two Mu ends and the enhancer trap five DNA supercoils."
    Pathania S., Jayaram M., Harshey R.M.
    Cell 109:425-436(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "MuA transposase separates DNA sequence recognition from catalysis."
    Goldhaber-Gordon I., Early M.H., Baker T.A.
    Biochemistry 42:14633-14642(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, COFACTOR.
  20. "Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase."
    Burton B.M., Baker T.A.
    Protein Sci. 14:1945-1954(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. "Interactions of phage Mu enhancer and termini that specify the assembly of a topologically unique interwrapped transpososome."
    Yin Z., Suzuki A., Lou Z., Jayaram M., Harshey R.M.
    J. Mol. Biol. 372:382-396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  22. "Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX."
    Abdelhakim A.H., Oakes E.C., Sauer R.T., Baker T.A.
    Mol. Cell 30:39-50(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST CLPX.
  23. "DNA repair by the cryptic endonuclease activity of Mu transposase."
    Choi W., Harshey R.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:10014-10019(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS FLAPS ENDONUCLEASE, MUTAGENESIS OF 575-ARG--LYS-579.
  24. "The AAA+ ClpX machine unfolds a keystone subunit to remodel the Mu transpososome."
    Abdelhakim A.H., Sauer R.T., Baker T.A.
    Proc. Natl. Acad. Sci. U.S.A. 107:2437-2442(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Mu insertions are repaired by the double-strand break repair pathway of Escherichia coli."
    Jang S., Sandler S.J., Harshey R.M.
    PLoS Genet. 8:E1002642-E1002642(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase."
    Clubb R.T., Omichinski J.G., Savilahti H., Mizuuchi K., Gronenborn A.M., Clore G.M.
    Structure 2:1041-1048(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-76.
  27. "Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains."
    Schumacher S., Clubb R.T., Cai M., Mizuuchi K., Clore G.M., Gronenborn A.M.
    EMBO J. 16:7532-7541(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 76-174.
  28. "Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase."
    Clubb R.T., Schumacher S., Mizuuchi K., Gronenborn A.M., Clore G.M.
    J. Mol. Biol. 273:19-25(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 173-247.
  29. "Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration."
    Rice P., Mizuuchi K.
    Cell 82:209-220(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 248-574, METAL-BINDING.
  30. "The mu transpososome structure sheds light on DDE recombinase evolution."
    Montano S.P., Pigli Y.Z., Rice P.A.
    Nature 491:413-417(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.71 ANGSTROMS) OF 77-605, FUNCTION.

Entry informationi

Entry nameiTNPA_BPMU
AccessioniPrimary (citable) accession number: P07636
Secondary accession number(s): P06021
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This enzyme is structurally similar to and performs the same endonucleotidic reaction as retroviral integrases, RNase H, RuvC holliday resolvases and RAG proteins.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.