ID Q7MUS1_PORGI Unreviewed; 602 AA.
AC Q7MUS1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN Name=dnaX {ECO:0000256|RuleBase:RU364063,
GN ECO:0000313|EMBL:AAQ66472.1};
GN OrderedLocusNames=PG_1418 {ECO:0000313|EMBL:AAQ66472.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66472.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66472.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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 {ECO:0000256|RuleBase:RU364063}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU364063};
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
CC complex. {ECO:0000256|RuleBase:RU364063}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR EMBL; AE015924; AAQ66472.1; -; Genomic_DNA.
DR RefSeq; WP_005873407.1; NC_002950.2.
DR AlphaFoldDB; Q7MUS1; -.
DR STRING; 242619.PG_1418; -.
DR EnsemblBacteria; AAQ66472; AAQ66472; PG_1418.
DR KEGG; pgi:PG_1418; -.
DR PATRIC; fig|242619.8.peg.1319; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_2_10; -.
DR BioCyc; PGIN242619:G1G02-1321-MONOMER; -.
DR Proteomes; UP000000588; 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: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; cd00009; AAA; 1.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
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 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 Pfam; PF12169; DNA_pol3_gamma3; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364063};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|RuleBase:RU364063};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU364063};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000000588};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 39..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 371..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 399..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 67418 MW; A00EC88FFA1E0679 CRC64;
METKYIVSAL KYRPDSFASM VGQEALSATL KSSIVQQKTA HAYLFCGPRG VGKTSCARIF
ARAINCLERL PDGEACGRCE SCKAFDEQRS MNIYELDAAS NNSVDDIRLL IEQANVPPQI
GKYKIYIIDE VHMLSQQAFN AFLKTLEEPP SYVIFILATT EKHKILPTIL SRCQIFDFKR
IPPARIEQHL RYVADSEGIK AEAEALAIIA TKADGGMRDA LSLFDRIARF SEGNITYANT
IENLNILDYD YYFRLTDFFL QGDYRSVLIV LDELLAKGFD GQVIVSGLAS FFRDLMMAQD
ASTLPLLEQS EVVIQRYVDM AARCPTSFLY QSLKILNACD QQYRQSNGKR LLLELSLMNI
AALFSKGLTA PPPTHGAQHA NPVVSGSVSP RPAPAKEQPS VAPSQSSVPP QPSIGEQRRQ
PETTAPTITE DKPEQTKVVP PTRPMATSTV GSEGRFTLRG IRNKQEQLQN NIQEVRTEMT
ESFDEEQLQL AWIEFAETKL SEEIHLKETM ANCLPKLRPG TSAFEVEVLN SRQEEEINNV
SARLLSFLAD KLCNTTIRMN VRVSESTSLN RVPVSLDEKI ERLNQENPLF DELRMRLGLS
LV
//
