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Database: UniProt
Entry: A0A428MDB4_9BACT
LinkDB: A0A428MDB4_9BACT
Original site: A0A428MDB4_9BACT 
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}.
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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
//
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