ID   KU_MYCTU                Reviewed;         273 AA.
AC   P9WKD9; L7N5V9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Non-homologous end joining protein Ku {ECO:0000255|HAMAP-Rule:MF_01875};
DE   AltName: Full=Mt-Ku;
GN   Name=mku; OrderedLocusNames=Rv0937c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, INTERACTION WITH LIGD, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12215643; DOI=10.1126/science.1074584;
RA   Weller G.R., Kysela B., Roy R., Tonkin L.M., Scanlan E., Della M.,
RA   Devine S.K., Day J.P., Wilkinson A., d'Adda di Fagagna F., Devine K.M.,
RA   Bowater R.P., Jeggo P.A., Jackson S.P., Doherty A.J.;
RT   "Identification of a DNA nonhomologous end-joining complex in bacteria.";
RL   Science 297:1686-1689(2002).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15499016; DOI=10.1126/science.1099824;
RA   Della M., Palmbos P.L., Tseng H.M., Tonkin L.M., Daley J.M., Topper L.M.,
RA   Pitcher R.S., Tomkinson A.E., Wilson T.E., Doherty A.J.;
RT   "Mycobacterial Ku and ligase proteins constitute a two-component NHEJ
RT   repair machine.";
RL   Science 306:683-685(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH LIGD, AND DOMAIN.
RX   PubMed=15778718; DOI=10.1038/nsmb915;
RA   Gong C., Bongiorno P., Martins A., Stephanou N.C., Zhu H., Shuman S.,
RA   Glickman M.S.;
RT   "Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity
RT   repair system driven by Ku, ligase D and ligase C.";
RL   Nat. Struct. Mol. Biol. 12:304-312(2005).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH LIGD.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16023671; DOI=10.1016/j.jmb.2005.06.038;
RA   Pitcher R.S., Tonkin L.M., Green A.J., Doherty A.J.;
RT   "Domain structure of a NHEJ DNA repair ligase from Mycobacterium
RT   tuberculosis.";
RL   J. Mol. Biol. 351:531-544(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [7]
RP   INTERACTION WITH SIR2, AND SUBUNIT.
RX   PubMed=21637345; DOI=10.1371/journal.pone.0020045;
RA   Li Z., Wen J., Lin Y., Wang S., Xue P., Zhang Z., Zhou Y., Wang X., Sui L.,
RA   Bi L.J., Zhang X.E.;
RT   "A Sir2-like protein participates in mycobacterial NHEJ.";
RL   PLoS ONE 6:E20045-E20045(2011).
CC   -!- FUNCTION: With LigD forms a non-homologous end joining (NHEJ) repair
CC       enzyme. Binds linear dsDNA with 5'- and 3'-overhangs but not closed
CC       circular dsDNA nor ssDNA. One dimer binds for every 30 bp. Recruits and
CC       stimulates the ligase activity of LigD but not of T4 ligase or a human
CC       ligase complex (LIG4/XRCC4). Attenuates the 3'- to 5'-exonuclease
CC       activity of LigD. Stimulates the template-directed addition of dNTPs by
CC       LigD on 5'-overhangs and nuclease activity on 3'-overhangs.
CC       {ECO:0000269|PubMed:12215643, ECO:0000269|PubMed:15499016,
CC       ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:16023671}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with LigD in the absence of
CC       DSBs, and with the isolated Pol domain of LigD in the presence of DNA.
CC       Interacts with Sir2, possibly in a trimeric complex with LigD.
CC       {ECO:0000255|HAMAP-Rule:MF_01875, ECO:0000269|PubMed:12215643,
CC       ECO:0000269|PubMed:15778718, ECO:0000269|PubMed:16023671,
CC       ECO:0000269|PubMed:21637345, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the prokaryotic Ku family. {ECO:0000255|HAMAP-
CC       Rule:MF_01875}.
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DR   EMBL; AL123456; CCP43685.1; -; Genomic_DNA.
DR   PIR; A70585; A70585.
DR   RefSeq; NP_215452.1; NC_000962.3.
DR   RefSeq; WP_003404795.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WKD9; -.
DR   SMR; P9WKD9; -.
DR   STRING; 83332.Rv0937c; -.
DR   PaxDb; P9WKD9; -.
DR   DNASU; 885050; -.
DR   GeneID; 885050; -.
DR   KEGG; mtu:Rv0937c; -.
DR   TubercuList; Rv0937c; -.
DR   eggNOG; COG1273; Bacteria.
DR   OMA; IRYRKVC; -.
DR   PhylomeDB; P9WKD9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0033202; C:DNA helicase complex; IDA:MTBBASE.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR   GO; GO:0051351; P:positive regulation of ligase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding; Reference proteome.
FT   CHAIN           1..273
FT                   /note="Non-homologous end joining protein Ku"
FT                   /id="PRO_0000425945"
FT   DOMAIN          10..193
FT                   /note="Ku"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01875"
FT   REGION          111..273
FT                   /note="Sufficient for interaction with LigD"
SQ   SEQUENCE   273 AA;  30904 MW;  DE11166BC1C52519 CRC64;
     MRAIWTGSIA FGLVNVPVKV YSATADHDIR FHQVHAKDNG RIRYKRVCEA CGEVVDYRDL
     ARAYESGDGQ MVAITDDDIA SLPEERSREI EVLEFVPAAD VDPMMFDRSY FLEPDSKSSK
     SYVLLAKTLA ETDRMAIVHF TLRNKTRLAA LRVKDFGKRE VMMVHTLLWP DEIRDPDFPV
     LDQKVEIKPA ELKMAGQVVD SMADDFNPDR YHDTYQEQLQ ELIDTKLEGG QAFTAEDQPR
     LLDEPEDVSD LLAKLEASVK ARSKANSNVP TPP