ID A0A0Q7Q7W2_9ACTN Unreviewed; 671 AA.
AC A0A0Q7Q7W2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASD11_17580 {ECO:0000313|EMBL:KQY55354.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY55354.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY55354.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY55354.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY55354.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY55354.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY55354.1}.
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DR EMBL; LMFJ01000003; KQY55354.1; -; Genomic_DNA.
DR RefSeq; WP_056290763.1; NZ_LMFJ01000003.1.
DR AlphaFoldDB; A0A0Q7Q7W2; -.
DR STRING; 1736550.ASD11_17580; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000051970; 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; 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; 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; PR01217; PRICHEXTENSN.
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:UP000051970};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..186
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 391..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 70653 MW; 6475CB45D3E97D3E CRC64;
MDAPLALYRR YRPETFAEVI GQDHVTTPLR HALAANKVNH AYLFSGPRGC GKTTSARILA
RALNCEQAPI SDPCGECQSC RDLARGGPGS VDVIEIDAAS HGGVDDARDL RERAFFSPVS
SRYKVYIIDE AHMVSPQGFN ALLKLVEEPP PHLKFIFATT EPDKVIGTIR SRTHHYPFRL
VPPKVLGDYL LQLCQSEGVV LEPTALPLVV RAGAGSVRDT LSVLDQLLGG AGPEGVTYSL
AVQLLGYTPD SLLDEAIDAF AAHDGSTVFG VVDKIIESGQ DPRRFAEDLL QRLRDLIVVT
AVPDALRTGL LEVPGDRAER LLSQAKGFGP SQLTRAADIV NTALVEFRGA TAPRLLLELM
CARILVPGAD DTTQGFAARL DRIEKRLAVA GGEPTPAPAQ PVDTRPVQPA APEPTPTPQP
PAPEPAPAPQ VSAPEPTPAP RAPAAEPAPA PQPSAGPGVP PASPASGGAP DERREAAVAA
PPQSVQPPAP APPAAQAPGQ LGTADVRRLW PEVLEVVKGL RRFSWIMLSQ NAQVAQLEGS
TLTIALVNTG ARDSFLGSGS VEVVQQALQQ VVGVSWKIEA IVDPSADPSG ASAPALVQQA
PEPSSSQPAR PKGVKAPESV RQAMAAPAGE RVPDDPDAGA HPDDPILDQG DDPEQLLSRE
LGAKVIGEHR E
//
