ID A0A1I5N8T4_9FIRM Unreviewed; 578 AA.
AC A0A1I5N8T4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=SAMN05216343_10419 {ECO:0000313|EMBL:SFP18259.1};
OS Oscillibacter sp. PC13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillibacter.
OX NCBI_TaxID=1855299 {ECO:0000313|EMBL:SFP18259.1, ECO:0000313|Proteomes:UP000198573};
RN [1] {ECO:0000313|EMBL:SFP18259.1, ECO:0000313|Proteomes:UP000198573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC13 {ECO:0000313|EMBL:SFP18259.1,
RC ECO:0000313|Proteomes:UP000198573};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOXE01000004; SFP18259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5N8T4; -.
DR STRING; 1855299.SAMN05216343_10419; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000198573; Unassembled WGS sequence.
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; 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 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:UP000198573};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 36..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 389..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 62472 MW; FCCEA77A70D27468 CRC64;
MYQALYRKWR PKTFSDVIGQ AHITETLQKQ VAEGRTSHAY LFTGTRGTGK TTCAKILAKA
VNCEHPVNGD PCNQCASCLG IENGSFLDVL ELDAASNNGV DQVRALRDEA IYSPANVKKR
VYIVDEVHML STPAFNALLK ILEEPPEHLM FILATTELHK VPATILSRCQ RFSFKRITPQ
DIAKRLTYVA GQEAIDLAAD GAELLSRLAD GALRDGLSLL DQCAAAGGTI DSTAVLEVLG
LAGNLQTAQL MEYVLQRDSK AALLLLNQLY ANGKDVGAVL SELSILVRDL LLRRTAPEGG
AALLSGGYDS AALDRLGKSA SASRLIYLAT TLQKTTADLY YSSNRRTDAE LCLLRLCDES
LSSDLTALEA RIQRLENAAA QAQAVRKAVQ KSMETAKPSV PQEKRTPRQE TVPAAEADLP
WEEEVPPLPL EEPPAPEDEG GRVFDAPESA PTPVSAPAGQ PVEEPPATTT VPAAGGNWWR
GLAESCKGRL PPMYRAFLDM CTGALDGDLL TVYGPDDITL GRLENDRVKT ALCEEAEKAA
GIPVRLAFRT GEPPKASPQE NLQNLLKFGS QFDNIKIK
//
