ID A0A7L9DF83_9GAMM Unreviewed; 164 AA. AC A0A7L9DF83; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 02-JUN-2021, entry version 2. DE RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063}; DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063}; DE Flags: Fragment; GN Name=dnaX {ECO:0000256|RuleBase:RU364063, GN ECO:0000313|EMBL:QOJ52648.1}; OS Pectobacterium sp. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium; unclassified Pectobacterium. OX NCBI_TaxID=1913084 {ECO:0000313|EMBL:QOJ52648.1}; RN [1] {ECO:0000313|EMBL:QOJ52648.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFBP797 {ECO:0000313|EMBL:QOJ52635.1}, CFBP8736 RC {ECO:0000313|EMBL:QOJ52646.1}, and CFBP8739 RC {ECO:0000313|EMBL:QOJ52648.1}; RX PubMed=32962307; RA Portier P., Pedron J., Taghouti G., Dutrieux C., Barny M.A.; RT "Updated Taxonomy of Pectobacterium Genus in the CIRM-CFBP Bacterial RT Collection: When Newly Described Species Reveal 'Old' Endemic Population."; RL Microorganisms 8:0-E1441(2020). 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:11130, CC Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:83828; EC=2.7.7.7; CC Evidence={ECO:0000256|ARBA:ARBA00001680, 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MT684042; QOJ52635.1; -; Genomic_DNA. DR EMBL; MT684053; QOJ52646.1; -; Genomic_DNA. DR EMBL; MT684055; QOJ52648.1; -; Genomic_DNA. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR027417; P-loop_NTPase. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02397; dnaX_nterm; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364063}; KW DNA replication {ECO:0000256|RuleBase:RU364063}; KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU364063}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063, KW ECO:0000313|EMBL:QOJ52648.1}; KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:QOJ52648.1}. FT DOMAIN 30..164 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QOJ52648.1" FT NON_TER 164 FT /evidence="ECO:0000313|EMBL:QOJ52648.1" SQ SEQUENCE 164 AA; 18329 MW; 30E7CAF271CB04F3 CRC64; RKWRPQTFTH VVGQEHVLTA LANGLSLGRI HHAYLFSGTR GVGKTSIARL LAKGLNCEQG VTATPCGQCD NCREIEQGRF VDLIEIDAAS RTKVEDTRDL LDNVQYAPAR GRFKVYLIDE VHMLSRHSFN ALLKTLEEPP PHVKFLLATT DPQKLPVTIL SRCL //