ID A0A3R9UJ39_9RHOB Unreviewed; 582 AA.
AC A0A3R9UJ39;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EJA01_10905 {ECO:0000313|EMBL:RSK32835.1};
OS Rhodovulum robiginosum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK32835.1, ECO:0000313|Proteomes:UP000275159};
RN [1] {ECO:0000313|EMBL:RSK32835.1, ECO:0000313|Proteomes:UP000275159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK32835.1,
RC ECO:0000313|Proteomes:UP000275159};
RA Gupta D., Guzman M.S., Bose A.;
RT "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT robiginosum.";
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|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:RSK32835.1}.
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DR EMBL; RWGU01000048; RSK32835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9UJ39; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000275159; 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 ECO:0000313|EMBL:RSK32835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275159};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RSK32835.1}.
FT DOMAIN 43..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 383..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 62471 MW; B68A6F4F19965687 CRC64;
MPDTPGTGYQ VLARKYRPAT FADLIGQDAM VRTLKNAFAA DRIAQAFIMT GIRGTGKTTT
ARIIAKGMNC IGPDGESGPT TEPCGHCEHC VAIAEGRHVD VMEMDAASRT GVGDIREIID
SVAYRAASAR YKIYIIDEVH MLSTSAFNAL LKTLEEPPAH VKFIFATTEI RKVPVTVLSR
CQRFDLRRIE PEVMIAHLKQ IAGLESAPIS DEALGLITRA AEGSVRDAMS LLDQAISQGA
GETTADEVRA MLGLADRGRV LDLFELIVKG DTAGALTELS AQYADGADPM AVLRDLAEIT
HWLSVILITP EAADDPTVSP DERTRGQTMA KALHMRVLTR MWQMLLKALE EVAMAPNAMM
AAEMAVIRLT HVSTLPTPED LVRRLQDAPP PQPGGGGGAH RPAGGSPPTG AQGHAALRAP
RGGGGPATAL ATQPETALAH YASFDHVVEL IRANREPKLL IDVETGVRLV SYSPGRIAFE
PTSDAPRDLA ARLSDRLKAW TGYRWAVSVE ATGGGPTIAE TRDAERLSLE AEAKEHPLVR
AVFDAFPKAR ITDIKTPDAL TQAAAAEALP EVEDEWDPFE DS
//
