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Database: UniProt
Entry: A0A1H9R116_9RHOB
LinkDB: A0A1H9R116_9RHOB
Original site: A0A1H9R116_9RHOB 
ID   A0A1H9R116_9RHOB        Unreviewed;       582 AA.
AC   A0A1H9R116;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN04490244_10280 {ECO:0000313|EMBL:SER66388.1};
OS   Tranquillimonas rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=641238 {ECO:0000313|EMBL:SER66388.1, ECO:0000313|Proteomes:UP000198885};
RN   [1] {ECO:0000313|EMBL:SER66388.1, ECO:0000313|Proteomes:UP000198885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23042 {ECO:0000313|EMBL:SER66388.1,
RC   ECO:0000313|Proteomes:UP000198885};
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; FOGU01000002; SER66388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9R116; -.
DR   STRING; 641238.SAMN04490244_10280; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000198885; 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; IPR022107; DNA_pol_III_gamma/tau_C.
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   Pfam; PF12362; DUF3646; 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:UP000198885};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          41..188
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          379..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  62593 MW;  EF3852DF681FECC6 CRC64;
     MSDTHAYQVL ARKYRPETFA DLVGQDAMVR TLKNAFESDR IAQAFIMTGI RGTGKTTTAR
     IIAKGMNCVG ADGEGGPTTT PCGRCEHCTA ISEGRHVDVY EMDAASNTSV NDIREIIDSV
     HYRAASARYK IYIIDEVHML STSAFNALLK TLEEPPEHVK FIFATTEIRK VPVTVLSRCQ
     RFDLRRIEPE VMLTLLRRIA DSETAQIADD ALALITRAAE GSARDATSLL DQAISHGAGE
     TTAEQVRAML GLADRGRVMD LFDMIMGGDP AGALGELSAQ YADGADPMAV LRDLAEITHW
     VSLVKITPET AEDPTIGPDE RSRGLAMAEK LPMRVLTRMW QMLLKALEEV AAAPNGMMAA
     EMAIIRLTHV ADLPSPEELV RKAQEAPAPT PPGGGGGATP APQNGGGGSA RGGTARASYG
     SGGAAQATAI ADDPEHALAR YASFDSVIEL IRNNRDVKLL VEIETCLRLA AYTPGRIEFQ
     PTDDAPRDLA ARLSDRLQNW TGARWAVSVV SEGGGATIAE ERDAEKLELE GRAKAHPLVQ
     AAFAAFPDAK IVEIRTPEAI AAEAEAEALP EVPDEWDPFE ED
//
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