ID A0A1U7EDP2_9LACT Unreviewed; 608 AA.
AC A0A1U7EDP2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BW721_09215 {ECO:0000313|EMBL:APZ49795.1};
OS Jeotgalibaca sp. PTS2502.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=1903686 {ECO:0000313|EMBL:APZ49795.1, ECO:0000313|Proteomes:UP000187137};
RN [1] {ECO:0000313|EMBL:APZ49795.1, ECO:0000313|Proteomes:UP000187137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTS2502 {ECO:0000313|EMBL:APZ49795.1,
RC ECO:0000313|Proteomes:UP000187137};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; CP019433; APZ49795.1; -; Genomic_DNA.
DR RefSeq; WP_076768074.1; NZ_CP019433.1.
DR AlphaFoldDB; A0A1U7EDP2; -.
DR STRING; 1903686.BW721_09215; -.
DR KEGG; jep:BW721_09215; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000187137; Chromosome.
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; IPR001270; ClpA/B.
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; 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 PRINTS; PR00300; CLPPROTEASEA.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000187137};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 369..396
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 608 AA; 67720 MW; B4FCE97221B8CFA2 CRC64;
MSYQALYRVW RPQRFDDIAG QEAVTRTLKN ALIQGKNSHA YLFTGPRGTG KTSAAKIFAK
AINCPNQEDG EPCNHCDICQ SITEGRLNDV IEIDAASNNG VEEIRDIRDK ARYAPTQAEY
KIYIIDEVHM LSTGAFNALL KTLEEPPANV IFILATTEPH KIPLTIISRT QRFDFKRITY
QAIINRMAYI LEQEAIKYDS QALHVVARAA NGGMRDALSL LDQVISYDSD FVSFDHAIQV
SGSLTEEMML NFLSALSQSE AEEALHILHD ILEKGKEAGR FIEEMILFAR DLLVYKQAGQ
SDLEERYSQA FREFSQAVEP TFLYQAIEEF SQTQKDMRFS TQPDVYLEVL AVKLAKQKVK
PQTTNETAAP ADSAEVSRLE KELADLKKEL TTALAAMKNG AVAAEPVKPA SPRPAVAKNA
AGFKPNLGRV QAIMKTASKK ELVSIKDNWV DILDVLSVTQ RAVLRQAEPV AANSEACILS
FDYEILCQKA SEDMELQVAL EEAIGRMSNR PGEFVCVTAE QWASLRKSYV QELKSRQEAA
PAVTENEPQT AAQAVPLADY DDNDAPPLFD EDMAIEMSPA DEDEQKQQEV VEQAISMFGK
ENITVINE
//
