ID A0A0D5YP20_9FLAO Unreviewed; 612 AA.
AC A0A0D5YP20;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=VC82_301 {ECO:0000313|EMBL:AKA33987.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA33987.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA33987.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA33987.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-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}.
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DR EMBL; CP011071; AKA33987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D5YP20; -.
DR STRING; 516051.VC82_301; -.
DR KEGG; mlt:VC82_301; -.
DR PATRIC; fig|516051.4.peg.313; -.
DR HOGENOM; CLU_006229_0_2_10; -.
DR Proteomes; UP000032726; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000032726};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 61..191
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 410..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 69450 MW; 1185C51F02446E58 CRC64;
MRAVSDRNIT PIPIFVDSYN HTILEPFIVS ARKYRPQTFK DVVGQEAITN TLENAIANNH
LAQALLFCGP RGVGKTTCAR ILAKKINQDG TESEHEDFAF NIFELDAASN NSVDDIRSLI
DQVRIPPQVG KYKVYIIDEV HMLSQSAFNA FLKTLEEPPK HAIFILATTE KHKIIPTILS
RCQIFDFKRI TVKDTAKYLQ YIAQEQGIEA DGDALHIIAQ KADGAMRDAL SIFDRVVSFS
GKNLTRKAVS ENLNVLDYET YFETVDLILK NDIPGLLVLF NKTVALGFDG HHFISGLATH
LRDLMVCKNE STIELLEVGE AAKKQYQEQA QKTSKAFLLK ALEIANDCDL KYKTSRNQRL
LVELALMKLA SISFDGEKKK SDSIIPASYF KKDARKEATP PPENVVVEHQ KNAPQHQTAE
TPHPIDIDSP IEHTKKDVPS EEEGRPSTAP PKIKLEKPQK RVSGLSLSSI KVKKEFQSSK
ETVPVDENEL PKDPFTEADM RKHWNDFTND LIRKGKRILG SNLQTDEPKL VNGHIIRIEL
PNHTMKKEVE REKKPLLDHL KQKLNNYSIR LQVSVNEEVE KKFAFTPEEK YEKLKEKNPA
IELLRKEFDL DL
//
