ID A0A2Y9B5A7_9RHOB Unreviewed; 573 AA.
AC A0A2Y9B5A7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BCF38_11724 {ECO:0000313|EMBL:PWJ12092.1}, SAMN05421539_11724
GN {ECO:0000313|EMBL:SSA51195.1};
OS Jannaschia seohaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=475081 {ECO:0000313|EMBL:SSA51195.1, ECO:0000313|Proteomes:UP000251571};
RN [1] {ECO:0000313|EMBL:SSA51195.1, ECO:0000313|Proteomes:UP000251571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:SSA51195.1,
RC ECO:0000313|Proteomes:UP000251571};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ12092.1, ECO:0000313|Proteomes:UP000245839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:PWJ12092.1,
RC ECO:0000313|Proteomes:UP000245839};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR EMBL; QGDJ01000017; PWJ12092.1; -; Genomic_DNA.
DR EMBL; UETC01000017; SSA51195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9B5A7; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000245839; Unassembled WGS sequence.
DR Proteomes; UP000251571; 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:UP000245839};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 44..191
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 390..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 61524 MW; FF65CEC4EBAA2F37 CRC64;
MQDQPADQAY QVLARKYRPA TFADLIGQDP MVRTLRNAFA QGRIAQAFIL TGIRGTGKTT
TARIVAKGLN CVGPDGAGGP TTDPCGQCEP CRAIAEGRHV DVLEMDAASN TGVGDMREII
DSVHYRAASA RYKIYIIDEV HMLSNSAFNA LLKTLEEPPA HVKFIFATTE IRKVPVTVLS
RCQRFDLRRI EPEVMIAHLR GVAEKEGAEI AEDALGLIAR AAEGSVRDAM SLLDQAISHG
AGETTADQVR AMLGLADRGR VLDLFELIMK GEAAAALMEL GAQYSDGADP MAVLRDLADV
THWVSVIQIT PDAAEDPTVG PDERARGQAM AQGLPMRSLT RMWQMLLKAL EEVSQAPNPM
MAAEMAVIRL THVADLPSPD ELIRKLRDAP APAAQAPTAP RPAPSGGGGG TPALRGGAAP
ALAADQEQAL ARFQTFPQVV ELIRANRDVK LLVEVETGVR LIRYAPGRIE MELAPDAAGD
LPQRLAGRLQ GWTGVRWVIT LGRGGAPTIA ETRDAARRET ETAALAHPLT QAVLAAFPGA
QLLEVRTRAE IEQAAAGEAL EEVEDEWDPF DED
//
