KU_CUPNH
ID KU_CUPNH Reviewed; 339 AA.
AC Q0JYN7;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Non-homologous end joining protein Ku {ECO:0000255|HAMAP-Rule:MF_01875};
GN Name=ku {ECO:0000255|HAMAP-Rule:MF_01875}; OrderedLocusNames=H16_B2355;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- FUNCTION: With LigD forms a non-homologous end joining (NHEJ) DNA
CC repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds
CC linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA
CC nor ssDNA. Recruits and stimulates the ligase activity of LigD.
CC {ECO:0000255|HAMAP-Rule:MF_01875}.
CC -!- SUBUNIT: Homodimer. Interacts with LigD. {ECO:0000255|HAMAP-
CC Rule:MF_01875}.
CC -!- SIMILARITY: Belongs to the prokaryotic Ku family. {ECO:0000255|HAMAP-
CC Rule:MF_01875}.
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DR EMBL; AM260480; CAJ97137.1; -; Genomic_DNA.
DR RefSeq; WP_010810674.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0JYN7; -.
DR SMR; Q0JYN7; -.
DR STRING; 381666.H16_B2355; -.
DR EnsemblBacteria; CAJ97137; CAJ97137; H16_B2355.
DR GeneID; 57648251; -.
DR KEGG; reh:H16_B2355; -.
DR eggNOG; COG1273; Bacteria.
DR HOGENOM; CLU_048975_2_0_4; -.
DR OMA; IRYRKVC; -.
DR OrthoDB; 1724780at2; -.
DR Proteomes; UP000008210; Chromosome 2.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:UniProtKB-UniRule.
DR CDD; cd00789; KU_like; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR HAMAP; MF_01875; Prokaryotic_Ku; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR009187; Prok_Ku.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR PANTHER; PTHR41251; PTHR41251; 1.
DR Pfam; PF02735; Ku; 1.
DR PIRSF; PIRSF006493; Prok_Ku; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR TIGRFAMs; TIGR02772; Ku_bact; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Reference proteome.
FT CHAIN 1..339
FT /note="Non-homologous end joining protein Ku"
FT /id="PRO_0000389193"
FT DOMAIN 10..187
FT /note="Ku"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01875"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37947 MW; A42FF431F685A312 CRC64;
MSRIIWKGAI TFGLVNIPVV LRPASRSQTL DLDLLDVRDM APVGYQRINK STGKPVDKEY
IVKGYQYAKD EYVLLNEEDF RQANVEATQT VDIVSFVDAQ SIPPYYFDTP YYLEPDKRGE
RGYALLHETM RRTGRAALAL VVLRARQHLA AMLVHGDALV LNTMRFADEV LPISELRLPK
ATTGKPTGAH AREIEMATKL VEDMSEDWEP EQYRDSYRDD LMARIEEKID SGKTHQLTPP
AEEEEAPRQG AKVIDMVALL RQSLGQRGKE DKEDATPARR KAPARHAAAR KQPAAKRAAT
PPAKRASTAA KTKRAPAKRE SHAPAARKSS STTRRKHAA
