ID A0A1M4ZY42_9BURK Unreviewed; 633 AA.
AC A0A1M4ZY42;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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 {ECO:0000256|RuleBase:RU364063};
GN ORFNames=SAMN02745117_01543 {ECO:0000313|EMBL:SHF22938.1};
OS Lampropedia hyalina DSM 16112.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1122156 {ECO:0000313|EMBL:SHF22938.1, ECO:0000313|Proteomes:UP000184327};
RN [1] {ECO:0000313|EMBL:SHF22938.1, ECO:0000313|Proteomes:UP000184327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16112 {ECO:0000313|EMBL:SHF22938.1,
RC ECO:0000313|Proteomes:UP000184327};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQUZ01000016; SHF22938.1; -; Genomic_DNA.
DR RefSeq; WP_073356123.1; NZ_FQUZ01000016.1.
DR AlphaFoldDB; A0A1M4ZY42; -.
DR STRING; 1122156.SAMN02745117_01543; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000184327; 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; 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:UP000184327};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 444..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 68393 MW; CE9D7AC462FFBCC7 CRC64;
MSYLVLARKY RPRNFDEMVG QEHVVKALSN ALEQQRLHHA YLFTGTRGVG KTTVSRILAK
SLNCQGADGQ GGITAHPCGV CQACRDIDAG RFVDYTELDA ASNRTVDEVQ SLLEQAIYKP
VQGRFKVFMI DEVHMLTGHA FNAMLKTLEE PPEYLKFVLA TTDPQKVPVT VLSRCLQFNL
RPMVPETIAE HLQKVLSLES VACELPAVRL ISRAARGSMR DALSLTDQAI AFGGGALHEA
QVRQMLGVVD KQYIYQIIEA LAQGQGKAVL DVCDTLRRAG TPAVSVLEDM SLALQQMALY
QSVPEHARQA ETGDTDEQRL LHYAAQLPPD ETQLLYSFCL KGREELGLAP DEYSGLVMVL
LRILAFKAPP APLSARASPV PLPAVATVAD APPAAPAPAP VEAAVAPVEV EAVEPPPAPI
PDAFAPVEEP VEQPPRYAEV LPWEDEAAPP PPTPAPVATV ATEPAPPAPP QAEPEPLLAD
AAPLPEPAPE TSIALPPEDL PPAQWWIALI HTLVQTGRLT ALARELAVQS ELLARDAQAL
RLRLNNQTLD NQSLRQKLAS VLLAVGVTQR LDIAVGEAVS TPAAHATEQK NRQMDVARHI
VENDPQVQML QQRFGGQIVP GSIQPLDIVL PPA
//
