ID A0A246AFH1_9SPHI Unreviewed; 596 AA.
AC A0A246AFH1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CBW18_04165 {ECO:0000313|EMBL:OWK71670.1};
OS Pedobacter sp. AJM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2003629 {ECO:0000313|EMBL:OWK71670.1, ECO:0000313|Proteomes:UP000198039};
RN [1] {ECO:0000313|Proteomes:UP000198039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJM {ECO:0000313|Proteomes:UP000198039};
RA Mcnett A.J., Newman J.D.;
RL Submitted (MAY-2017) 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:OWK71670.1}.
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DR EMBL; NHOT01000002; OWK71670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246AFH1; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000198039; 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; 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:UP000198039};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..186
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 395..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 67269 MW; 4A975E5106FB620B CRC64;
MENFIVSARK YRPATFETVV GQQHITGTLK NAIKNNQLAQ AFLFCGPRGV GKTTCARILA
KTINCTNPTA EMEACGQCDN CLSFQNGHSF NVHELDAASN NSVDDIRSLI EQVRIPPQAG
RYKIYIIDEV HMLSQSAFNA FLKTLEEPPS YAIFILATTE KHKILPTILS RCQIFDFNRI
QVEDISRHLA TIAQRENIAF ETDGLHIIAQ KADGGLRDAL SMFDQIASYA NKNITYKAVI
DNLNILDYDY FFKLTSYLTA AEVSQTLLLF DEILNNGFDG NNFINGLATH FRNLLVGKDA
ATIKLLEVSE NIKQKYLDQC RQTELSFLLT ALNLANNCDL NYKNSKNQRL QVELALIKMC
HIRSVVQLAQ QPLSPSNTAT DADQDKKKTD VIIEKAESPK IKAESENLPP KTETPVLPPV
EEKPKTSPPS SATSISINIP KKNVGTLIPS LNDLERLANG EEDNGPKKAT GEAREPFTYD
QLLEVWNKYI QILKSADKIN LFTILNNFAP KLISPVLIEI SVESKTQEQF VVQESVELMN
FLRNQLQNFA VDITFKQVER KIENRLYGNR EKYDYLVNKN PKLDELRKRF NLDINP
//
