ID   DPO3X_MYCTO             Reviewed;         578 AA.
AC   P9WNT8; 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 36.
DE   RecName: Full=DNA polymerase III subunit gamma/tau;
DE            EC=2.7.7.7;
GN   Name=dnaX; Synonyms=dnaZX; OrderedLocusNames=MT3824;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 (By similarity).
CC       {ECO:0000250}.
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: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48193.1; -; Genomic_DNA.
DR   PIR; B70796; B70796.
DR   RefSeq; WP_003420417.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNT8; -.
DR   SMR; P9WNT8; -.
DR   EnsemblBacteria; AAK48193; AAK48193; MT3824.
DR   KEGG; mtc:MT3824; -.
DR   PATRIC; fig|83331.31.peg.4117; -.
DR   HOGENOM; CLU_006229_3_5_11; -.
DR   Proteomes; UP000001020; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..578
FT                   /note="DNA polymerase III subunit gamma/tau"
FT                   /id="PRO_0000427069"
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