ID A0A428MDB4_9BACT Unreviewed; 671 AA.
AC A0A428MDB4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=EDE15_0366 {ECO:0000313|EMBL:RSL14898.1};
OS Edaphobacter aggregans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Edaphobacter.
OX NCBI_TaxID=570835 {ECO:0000313|EMBL:RSL14898.1, ECO:0000313|Proteomes:UP000269669};
RN [1] {ECO:0000313|EMBL:RSL14898.1, ECO:0000313|Proteomes:UP000269669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB153 {ECO:0000313|EMBL:RSL14898.1,
RC ECO:0000313|Proteomes:UP000269669};
RA Deangelis K.;
RT "Sequencing of bacterial isolates from soil warming experiment in Harvard
RT Forest, Massachusetts, USA.";
RL Submitted (DEC-2018) 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|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:RSL14898.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RSDW01000001; RSL14898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428MDB4; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000269669; 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 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; 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 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:UP000269669};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..185
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 398..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 71888 MW; 54120E43C9758050 CRC64;
MGYQVLARKY RPQRFADVAG QDHVTVTLMN ALTQGRIAHG YIFSGHRGIG KTTIARILAM
ALNCRNAIGS AQRATAEPCE VCDSCVEIRA GNAVDVIEID AATNRGIDEI RELRDAARYR
PARDKYKIYI LDEAHQITDA AFNALLKTLE EPPDHIVFMM ATTQPEDIPQ TVRSRCQHFS
FHAVKLVDIL GELRGIAERE GVVADEAALA LLAEAGDGSM RDALSIMDQA IASAPTEDGR
PRLDASQIRE LMGTVPNTVF EKILEAVDGN NSAEVITVAN QLLDAGNSPA QLARQFVRYL
RNCVIAKIAG IGADGSGLDG TATELLQISA DEQRRTGRSA ALFGEEELTR FLQVMLRTFD
ELGYRQEQRF HFELGLLKLV HLRRLLPVEE VLSQFPVGGG SGQVTPRTTG ATSASAQPAT
VRAGAPVSSS APAVTTAKPA FSPFEADRSR KRFEGDAIVS APAKGEIPAP VKAEAAVVPK
NVDPVRVTEA VVVEPEPVDE ASVTTITAEI LGTGAVPAAA LEPEIPLVVE SSNLQTSSPP
SASAEEFQRV ATEALMNAKS QGSAADAMAD SEWKIEGGEI RVQTELSKIM LPMVVNPEAD
KIVRAALREA GAGALKLVLL PGTAAATEKK KPRAAKTGSA QAKAMEHPVV QQAQRLFNAE
IRNVIDLRDN D
//