KU_BPMOM
ID KU_BPMOM Reviewed; 282 AA.
AC Q853W0;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein Ku;
DE AltName: Full=Gp206;
DE AltName: Full=Omega-Ku;
GN Name=206;
OS Mycobacterium phage Omega (Mycobacteriophage Omega).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Omegavirus.
OX NCBI_TaxID=205879;
OH NCBI_TaxID=1772; Mycolicibacterium smegmatis (Mycobacterium smegmatis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12705866; DOI=10.1016/s0092-8674(03)00233-2;
RA Pedulla M.L., Ford M.E., Houtz J.M., Karthikeyan T., Wadsworth C.,
RA Lewis J.A., Jacobs-Sera D., Falbo J., Gross J., Pannunzio N.R., Brucker W.,
RA Kumar V., Kandasamy J., Keenan L., Bardarov S., Kriakov J., Lawrence J.G.,
RA Jacobs W.R. Jr., Hendrix R.W., Hatfull G.F.;
RT "Origins of highly mosaic mycobacteriophage genomes.";
RL Cell 113:171-182(2003).
RN [2]
RP FUNCTION, SUBUNIT, PROBABLE INTERACTION WITH HOST LIGD, AND DNA-BINDING.
RX PubMed=16949369; DOI=10.1016/j.molcel.2006.07.009;
RA Pitcher R.S., Tonkin L.M., Daley J.M., Palmbos P.L., Green A.J.,
RA Velting T.L., Brzostek A., Korycka-Machala M., Cresawn S., Dziadek J.,
RA Hatfull G.F., Wilson T.E., Doherty A.J.;
RT "Mycobacteriophage exploit NHEJ to facilitate genome circularization.";
RL Mol. Cell 23:743-748(2006).
CC -!- FUNCTION: Required for replication of viruses with short cos ends (4
CC bases). Stimulates dsDNA end-joining by host LigD; in conjunction with
CC M.smegmatis or M.tuberculosis LigD can reconstitute NHEJ in
CC S.cerevisiae. Binds dsDNA with either blunt, 5'- or 3-overhangs,
CC protecting it from host exonuclease degradation.
CC {ECO:0000269|PubMed:16949369}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with host LigD, maybe via the
CC LigD Pol domain. {ECO:0000269|PubMed:16949369, ECO:0000305}.
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DR EMBL; AY129338; AAN12848.1; -; Genomic_DNA.
DR RefSeq; NP_818506.1; NC_004688.1.
DR SMR; Q853W0; -.
DR GeneID; 1260006; -.
DR KEGG; vg:1260006; -.
DR Proteomes; UP000000963; Genome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0099016; P:evasion by virus of DNA end degradation; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099009; P:viral genome circularization; IEA:UniProtKB-KW.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR HAMAP; MF_01875; Prokaryotic_Ku; 1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024412; Lsr2.
DR InterPro; IPR009187; Prok_Ku.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR PANTHER; PTHR41251; PTHR41251; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF11774; Lsr2; 1.
DR PIRSF; PIRSF006493; Prok_Ku; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR TIGRFAMs; TIGR02772; Ku_bact; 1.
PE 1: Evidence at protein level;
KW DNA end degradation evasion by virus; DNA-binding; Host-virus interaction;
KW Reference proteome; Viral genome circularization;
KW Virus entry into host cell.
FT CHAIN 1..282
FT /note="Protein Ku"
FT /id="PRO_0000425948"
FT DOMAIN 9..189
FT /note="Ku"
SQ SEQUENCE 282 AA; 31279 MW; 3760306B66ADBB83 CRC64;
MRAVWTGAVN FGLVNVPVKM YAATEEHDLK GHLAHVQDGG RIRYHKVCET CGEQVHTADL
GKVFEVDGQT ALLTDEDLAE LPSENNKVID VVEFVPAGEV DPILLDKPYY LNAEGSVRPY
ALLARTLSDA DKVAIVRVTL RSKEHLAVLR VTGKNEVLTL QTLRWPDEVR EPDFPKLDNK
PELSEAELKV AAMLVDELSA PFNPDKHQDT YKVELRALVE SKLEPVEVPE DVSGLLAKLE
ASVKPKQAKP DIRTWAKAQG FKISARGRIP KDIVDKYEGA MA