ID A0A2A7UU58_COMTR Unreviewed; 726 AA.
AC A0A2A7UU58;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CRM82_09800 {ECO:0000313|EMBL:PEH88845.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH88845.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) 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:PEH88845.1}.
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DR EMBL; PDEA01000001; PEH88845.1; -; Genomic_DNA.
DR RefSeq; WP_066535791.1; NZ_UIGV01000001.1.
DR AlphaFoldDB; A0A2A7UU58; -.
DR STRING; 1219032.GCA_001515545_01746; -.
DR GeneID; 80800897; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000220246; 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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
DR NCBIfam; TIGR02397; dnaX_nterm; 1.
DR PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 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; PF12170; DNA_pol3_tau_5; 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 Reference proteome {ECO:0000313|Proteomes:UP000220246};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..184
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 486..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 75986 MW; 48F131C1B3551F0F CRC64;
MSYLVLARKY RPRNFSEMVG QEHVVQALTN ALTQQRLHHA YLFTGTRGVG KTTVSRILAK
SLNCVGPDGQ GGITATPCGV CPACKEIDSG RFPDYTELDA ASNRGVDEVQ SLLEQAVYKP
VQGRFKVFMI DEVHMLTNTA FNAMLKTLEE PPEYLKFVLA TTDPQKVPVT VLSRCLQFNL
RPMAPDTVLE HLTSVLGTES VPAEPQALKL LARAARGSMR DALSLTDQAI AFGSGQLQEA
TVRQMLGSVD RSYVFRLIGA LAQGDGRTVV ETVDSLRTNG VSASATLEDM CAVLQRMAVL
QAVPQMADAA DPSDPEAAEM AALAQQMPAD ETQLLYSISL HGRTELGLAP DEYAALTMAL
LRLLAFKPQG TADAATVEKK TLAKPVTQAE AARIQAPAPA QASAQAVTVV AAEPVPAAPA
VPEVAPVVPA AAPVQPPASV APVQAPAVAP AVQYTASPIA APAPAGEPAA RATPAAADVV
QAPAPVAPPA APKATAVQSH AAPQPAPQPA VVPPAGVPAV SNEVPPWEDI PEVAVEESDS
SDDADSAPPA WEGPMDGEPM DLPDDPLDAM EPVDAAPAPR SAPAVQDYAP APAPLEVPTT
PLGDVWHGVV TQLVQAEAVT ALVRELALQS QLVAQEGDSW TLRVERTSLN QATAKERLRK
ALADAGHCQT LVVENGAAAD TPAKRNTAAA QRHQKLAEAI VLNDPQVQTL MRAYGAKIVP
GSIRPA
//