ID   DPO3X_MYCPN             Reviewed;         681 AA.
AC   P75177;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=DNA polymerase III subunit gamma/tau;
DE            EC=2.7.7.7;
GN   Name=dnaX; OrderedLocusNames=MPN_618; ORFNames=MP224;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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: 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; U00089; AAB95872.1; -; Genomic_DNA.
DR   PIR; S73550; S73550.
DR   RefSeq; NP_110307.1; NC_000912.1.
DR   RefSeq; WP_010874975.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75177; -.
DR   SMR; P75177; -.
DR   IntAct; P75177; 5.
DR   STRING; 272634.MPN_618; -.
DR   EnsemblBacteria; AAB95872; AAB95872; MPN_618.
DR   KEGG; mpn:MPN_618; -.
DR   PATRIC; fig|272634.6.peg.682; -.
DR   HOGENOM; CLU_006229_0_3_14; -.
DR   OrthoDB; 9810148at2; -.
DR   BioCyc; MPNE272634:G1GJ3-997-MONOMER; -.
DR   Proteomes; UP000000808; 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:0016887; F:ATP hydrolysis activity; 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; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..681
FT                   /note="DNA polymerase III subunit gamma/tau"
FT                   /id="PRO_0000105499"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   681 AA;  76213 MW;  E3DDC6A580FFCBCC CRC64;
     MRKVLYQKYR PTKFSDTVGQ DSIKRIIVNA ITQDQLPHGY IFAGERGTGK TTFAKIIAKA
     INCLNWNGDV CNQCEACQAI NSNSAIDVFE IDAASKNGIN DIRELAENVF NLPFKFKKKV
     YILDEAHMLT PQSWSGLLKT LEEAPDYVLF IFATTEFNKI PITILSRCQS FFFKQITNDL
     IQQRLAEVAA KESIKITTDA LVKLADLAQG SLRDGLSLLD QISNFSESKT ISLADVEKTF
     NLLDKEQKFG FIEAVLSGDL KQSFHLIDNF ESQGINFVHF LRELFALTVD LYGYVKTGQI
     AVVKPSDQTM AAKLRFHPKQ YALLVQAIEA NTGYGPSQLS LSDQIKAIVI HYNNAVSKEP
     HIPAYTPVVQ TQSPAKEHVP SKTVEEAKPQ LPAKEPVLYK VIEEPKVSSF VKDPVASKLI
     EQPQTIVQPE AQQEITEVEQ PTETSPAPAT DLFGLAIKPE VVRKRGRRPL SVENTDFFQP
     AVKKLIQPVS KPAPIKLIEP SDNNPVSIPI KLNRAVIAVS VYGHNDPKLV AHFQQLLDSF
     KREFTQAEKT KDSSYLKQFS DKFTASDLSK VIKVLAASPF GLVLIFEDKE IATRLWKEAL
     TEATAQATLL EIFQQNLFLS SFTLSEYETK VLAKVEQLTH KPQVLQLQQL EQLSSTVVKK
     AQKTAAQEIA DTFFKGLYEE K
//