ID A0A094J0J8_9GAMM Unreviewed; 630 AA.
AC A0A094J0J8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=IDSA_02565 {ECO:0000313|EMBL:KFZ31604.1};
OS Pseudidiomarina salinarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=435908 {ECO:0000313|EMBL:KFZ31604.1, ECO:0000313|Proteomes:UP000054363};
RN [1] {ECO:0000313|EMBL:KFZ31604.1, ECO:0000313|Proteomes:UP000054363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISL-52 {ECO:0000313|EMBL:KFZ31604.1,
RC ECO:0000313|Proteomes:UP000054363};
RA Du J., Shao Z.;
RT "The draft genome sequence of Idiomarina salinarum ISL-52.";
RL Submitted (JUN-2014) 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:KFZ31604.1}.
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DR EMBL; JPER01000001; KFZ31604.1; -; Genomic_DNA.
DR RefSeq; WP_034773952.1; NZ_PIQD01000001.1.
DR AlphaFoldDB; A0A094J0J8; -.
DR STRING; 435908.IDSA_02565; -.
DR eggNOG; COG2812; Bacteria.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000054363; 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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
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; PF12170; DNA_pol3_tau_5; 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:UP000054363};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 373..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68619 MW; 4F34E5FB92FE0B01 CRC64;
MSYQVLARKW RPRNFTEVVG QQHVLKPLIN ALNSGRLHHA WLLTGTRGVG KTTIARILAK
SLNCEAGITA SPCGECGACT AIDQGRFVDL LEIDAASRTK VEDTRELLDN VQYRPTQGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPITVLSRC LQFNLKALSR
TEIAGHLQQV LQSENIAADD QALQLLARAA QGSLRDALSL TDQAIAQGDH AVTVAGVQQM
LGSVPGYELV ALLQQILTGE GEALLQTLDK VAGQVPDLAS LLSELQNLLH QIALYQAVPA
VADTLGLSDA EQRLAQQLPA ELIHVFYDIL VQGRRDLNFA SDTRSGVEIT LLRMMTFRPE
YLELIETEAA TVTQVRDEQQ GVPDVEAEVM PEAEPESEPE PESESKPEPV AEQPAAEQPQ
PTKSAGSNAD IEALIATRDA LQQKKNPEAP VTALSAAPEP EREPEPAPET EPEPEPESHF
ELAEPVAEEK PDVAPAPGVE KGVRTAAEVD SWAAIIDNSE LHGLARQLAR NSVLRKVDGD
YQLCLRSDWA HLLNDSAVEV ITGVLQDNLA MKLTGVVVEN ADQPTPTEIQ LQIDAQRLQQ
AHAELAADPL TRALADTFGA VLIEDSVKPN
//
