ID A0A0F0CFN1_9CLOT Unreviewed; 539 AA.
AC A0A0F0CFN1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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_2 {ECO:0000313|EMBL:KJJ74731.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=CLFS41_11220 {ECO:0000313|EMBL:KJJ74731.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ74731.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ74731.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ74731.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-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:KJJ74731.1}.
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DR EMBL; JYHN01000039; KJJ74731.1; -; Genomic_DNA.
DR RefSeq; WP_045091704.1; NZ_JYHN01000039.1.
DR AlphaFoldDB; A0A0F0CFN1; -.
DR PATRIC; fig|1609975.3.peg.1202; -.
DR Proteomes; UP000033604; 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:KJJ74731.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KJJ74731.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 539 AA; 60162 MW; FCD3FDB336721447 CRC64;
MSYTALYRKW RPVSFEDVKG QDPIVQTLKN QITSERIGHA YLFCGTRGTG KTSIAKIFAR
AVNCEHPVDG SPCNECPTCK AIQTGSSMNV VEIDAASNNG VENIRDIRDQ VQYPPTEGRY
RVYIIDEVHM LSIGAFNALL KTLEEPPSYV IFILATTEVH KIPITILSRC QRYDFKRISL
DTIADRLREL TQAEQIEVED KALMYIAKAA DGSLRDGLSL LDQCVAFHYG KVLTYDNALE
VLGAVDAGVF SQMFGAIVDG RTKDCICALE EIVIQGRELG QFVTDFIWYM RNLLLIQSAD
DAEGLLDMSE ENLKQLKADG EKADGPTLMR YIRVFSELSN QLRYATQKRV LVEVALIKLT
RPAMEPNLDS ILQRLGDLEM LMEDLEAGRM TIQAAAPAYA AAGTAGQAAR PAAASAEPEI
PAERVSLPKA QLEDLKLVRN EWARIVRSMG GGAKSYLRDT VVEPGGEGCL TIVFMDPMNY
DMGKRPTVIG ELERYVETNY GKSIYFKTRL AGRGERLNTI YVTEEELEDK IHMDITYED
//
