ID A0A0L6Z953_9CLOT Unreviewed; 545 AA.
AC A0A0L6Z953;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_1 {ECO:0000313|EMBL:KOA19506.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=CLHOM_21140 {ECO:0000313|EMBL:KOA19506.1};
OS Clostridium homopropionicum DSM 5847.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA19506.1, ECO:0000313|Proteomes:UP000037043};
RN [1] {ECO:0000313|Proteomes:UP000037043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA Duerre P.;
RT "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT (DSM 5847T).";
RL Submitted (AUG-2015) 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:KOA19506.1}.
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DR EMBL; LHUR01000023; KOA19506.1; -; Genomic_DNA.
DR RefSeq; WP_052221651.1; NZ_LHUR01000023.1.
DR AlphaFoldDB; A0A0L6Z953; -.
DR STRING; 36844.SAMN04488501_1243; -.
DR PATRIC; fig|1121318.3.peg.2131; -.
DR Proteomes; UP000037043; 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; 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 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:KOA19506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037043};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KOA19506.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 545 AA; 62939 MW; F6D6D474EF1C442E CRC64;
MSYTALYREW RPKTFEEVVG QSHVTTTLKN QIKNNRVAHA YLLCGTRGTG KTSTAKIFAK
AVNCLEPKDG EPCNECEMCK KINAGLAIDV SEMDAASHNK VDDIRDLIEE VKYPPRESRY
KVYIMDEVHM LTQGAVNAFL KTLEEPPEKT IFVLATTDPQ KLPITILSRC QRFDFKRIKS
DDIFERLVKI IKEQGNYADN KSLRLIARIS DGAMRDALSI LDQAISMGNG NVDYDKLINM
LGLITNEYLF KLTDSIIKRD IEEAISVIDE VVYTGKDVNL FTKDMILHLR NLMISKVSEN
PEEVLDMSEE NIYIVKEQAS KLRVEEIMRC IRILQESEEQ SKWSNQGRIY LEMAVIKMCK
FEYDTSKEVL LARINKLENI IKEGNFNIKQ NISDNNAVKT VENRNPKKVF EKKQDNKEKS
NDLNIKIEEN IESKLTLEDV KKSWKDILEV LKARRLMVLY ASLVTGKVES CINGIIEIKY
EPEYAFNISR LKKEENRRTV DEIFSEALKE KVRIKYIVEE KEEPINPVDI LKETFGEDLV
EIIDE
//
