DPO3X_MYCPN
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 03-AUG-2022, entry version 111.
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) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
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; NC_000912.1.
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 OMA; RCQSFFF; -.
DR BioCyc; MPNE272634:G1GJ3-997-MON; -.
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: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; IPR012763; DNA_pol_III_sug/sutau_N.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR SMART; SM00382; AAA; 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; 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