ID A0A366XP89_9BACI Unreviewed; 564 AA.
AC A0A366XP89;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DS031_22765 {ECO:0000313|EMBL:RBW67328.1};
OS Bacillus taeanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW67328.1, ECO:0000313|Proteomes:UP000253314};
RN [1] {ECO:0000313|EMBL:RBW67328.1, ECO:0000313|Proteomes:UP000253314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030017 {ECO:0000313|EMBL:RBW67328.1,
RC ECO:0000313|Proteomes:UP000253314};
RA Liu R., Huang Z.;
RT "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT intestinal tract of a marine limpet and the reclassification of B.
RT taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT genus Lottiidibacillus.";
RL Submitted (JUL-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:RBW67328.1}.
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DR EMBL; QOCW01000041; RBW67328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366XP89; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000253314; 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; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
DR InterPro; IPR048448; DnaX-like_C.
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; PF20964; DnaX_C; 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 ECO:0000313|EMBL:RBW67328.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253314};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RBW67328.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 373..400
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 564 AA; 64215 MW; 9C7646B08026C62C CRC64;
MSYQALYRVW RPQQFKDVVG QEHITKTLQN AIMQQKLSHA YLFTGPRGTG KTSAAKIIAK
AINCEKAPIE EPCNECDACR GIKDGSLSDV IEIDAASNNG VDEIRDIRDK VKYAPSSVPY
KVYIIDEVHM LTTGAFNALL KTLEEPPPHV IFILATTEPH KIPLTIISRC QRFDFRRITI
EAIVSRMEHI INAQEVVVER EALYMVARAA EGGMRDALSI LDQVISYSEQ SVTVDDVLAV
TGMVSQQFLS RVAKAFLDQD VITALKAVEQ LMEHGKDPTR FLEDLIYYYR DILLYQTAPK
LEEVMDRAKV DEQFQEIANT ISKEWIYYII EILNRSQQEM KWTNHPRIFL ELSLVKICQG
EGAPKQQGNI GTDAALLDRI NNLEKEIASL KENGVSVREE TTAEPKPQRA FNPAIKKQQS
SGRIREMLKK ATKQDLNRLR SVWGDVMERI RQEKVSAHAW LKDSQPVACS DDTFVLSFQY
ELHSQMALKD NIRSTLENVL TNVLGKQLAM LTILEEDWQA VKSSYIKNQH DSEESEQILT
EKQEDPLISE AKKLFGEELI EIQD
//
