ID A0A371RVM9_9BACI Unreviewed; 563 AA.
AC A0A371RVM9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DZB84_24180 {ECO:0000313|EMBL:RFB09470.1};
OS Bacillus sp. HNG.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2293325 {ECO:0000313|EMBL:RFB09470.1, ECO:0000313|Proteomes:UP000263943};
RN [1] {ECO:0000313|EMBL:RFB09470.1, ECO:0000313|Proteomes:UP000263943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNG {ECO:0000313|EMBL:RFB09470.1,
RC ECO:0000313|Proteomes:UP000263943};
RA Gagnon H.N., Maines B.A., Sevigny J.L.;
RT "Genome Assembly of Bacillus sp. HNG.";
RL Submitted (AUG-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:RFB09470.1}.
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DR EMBL; QUQV01000032; RFB09470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371RVM9; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000263943; 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; 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 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:RFB09470.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000263943};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RFB09470.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 563 AA; 63714 MW; 9E9136055B59FE7C CRC64;
MAYQALYRVF RPQAFHDVVG QEHITKTLQN ALLQEKFSHA YLFSGPRGTG KTSAAKIFAK
AVNCEHSPTA EPCNECAACK GITDGSIADV IEIDAASNNG VDEIRDIRDK VKYAPSAVRY
KVYIIDEVHM LSIGAFNALL KTLEEPPRHV IFILATTEPH KIPLTIISRC QRFDFRRITT
QAIVGRMKTI IAEQDVKVDE QALYVIARAA EGGMRDALSL LDQAISFSDE EVKLEDVLTI
TGAVSQSFLT NVVRAIRDRD VRTALKTLDE MMDHGKDPMR FIEDIIFYYR DMLLYQTAPQ
LEEVLERVLV DEDFTELAKS IQGSEIYETI DILNQAQQEM KWTNHPRIFL EVAIVKLTQM
EQQQSLESLP QIEGLMNKIN RLESELTAIK EKGVVAHPQD AKLAEKRPQK SSRNGYRTPV
GRINEVLKSA TRQNLDLLKG KWGDMLDQLR TQNKVSHAAL LIESEPVAAS TNAFVLKFKY
EIHCKMASEN PEVKENLENI LSGLTGHRFE MIGVPDDEWG KIREEFIRGQ RTDDDDERPE
DTEDPLIAEA MKIVGSELIE IKE
//
