ID   DPO3X_MYCTU             Reviewed;         578 AA.
AC   P9WNT9; L0TF21; O69688; P63975;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=DNA polymerase III subunit gamma/tau;
DE            EC=2.7.7.7;
GN   Name=dnaX; Synonyms=dnaZX; OrderedLocusNames=Rv3721c; ORFNames=MTV025.069c;
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   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [3]
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   [4]
RP   INTERACTION WITH DNAN, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=H37Rv;
RX   PubMed=22545130; DOI=10.1371/journal.pone.0035702;
RA   Kukshal V., Khanam T., Chopra D., Singh N., Sanyal S., Ramachandran R.;
RT   "M. tuberculosis sliding beta-clamp does not interact directly with the
RT   NAD+-dependent DNA ligase.";
RL   PLoS ONE 7:E35702-E35702(2012).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- SUBUNIT: Interacts with the beta sliding-clamp (dnaN)
CC       (PubMed:22545130). DNA polymerase III contains a core (composed of
CC       alpha, epsilon and theta chains) that associates with a tau subunit.
CC       This core dimerizes to form the POLIII' complex. PolIII' associates
CC       with the gamma complex (composed of gamma, delta, delta', psi and chi
CC       chains) and with the beta chain to form the complete DNA polymerase III
CC       complex (By similarity). {ECO:0000250, ECO:0000269|PubMed:22545130}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46547.1; -; Genomic_DNA.
DR   PIR; B70796; B70796.
DR   RefSeq; NP_218238.1; NC_000962.3.
DR   RefSeq; WP_003420417.1; NZ_NVQJ01000009.1.
DR   AlphaFoldDB; P9WNT9; -.
DR   SMR; P9WNT9; -.
DR   STRING; 83332.Rv3721c; -.
DR   PaxDb; P9WNT9; -.
DR   DNASU; 885361; -.
DR   GeneID; 885361; -.
DR   KEGG; mtu:Rv3721c; -.
DR   TubercuList; Rv3721c; -.
DR   eggNOG; COG2812; Bacteria.
DR   OMA; HVDVMEM; -.
DR   PhylomeDB; P9WNT9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..578
FT                   /note="DNA polymerase III subunit gamma/tau"
FT                   /id="PRO_0000105500"
FT   REGION          389..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   578 AA;  61923 MW;  3AF4CD7959B3C965 CRC64;
     MALYRKYRPA SFAEVVGQEH VTAPLSVALD AGRINHAYLF SGPRGCGKTS SARILARSLN
     CAQGPTANPC GVCESCVSLA PNAPGSIDVV ELDAASHGGV DDTRELRDRA FYAPVQSRYR
     VFIVDEAHMV TTAGFNALLK IVEEPPEHLI FIFATTEPEK VLPTIRSRTH HYPFRLLPPR
     TMRALLARIC EQEGVVVDDA VYPLVIRAGG GSPRDTLSVL DQLLAGAADT HVTYTRALGL
     LGVTDVALID DAVDALAACD AAALFGAIES VIDGGHDPRR FATDLLERFR DLIVLQSVPD
     AASRGVVDAP EDALDRMREQ AARIGRATLT RYAEVVQAGL GEMRGATAPR LLLEVVCARL
     LLPSASDAES ALLQRVERIE TRLDMSIPAP QAVPRPSAAA AEPKHQPARE PRPVLAPTPA
     SSEPTVAAVR SMWPTVRDKV RLRSRTTEVM LAGATVRALE DNTLVLTHES APLARRLSEQ
     RNADVLAEAL KDALGVNWRV RCETGEPAAA ASPVGGGANV ATAKAVNPAP TANSTQRDEE
     EHMLAEAGRG DPSPRRDPEE VALELLQNEL GARRIDNA