ID A0A327LWY7_9RHOB Unreviewed; 586 AA.
AC A0A327LWY7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DOO74_09375 {ECO:0000313|EMBL:RAI54425.1};
OS Rhodobacteraceae bacterium AsT-22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2230886 {ECO:0000313|EMBL:RAI54425.1, ECO:0000313|Proteomes:UP000249713};
RN [1] {ECO:0000313|EMBL:RAI54425.1, ECO:0000313|Proteomes:UP000249713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AsT-22 {ECO:0000313|EMBL:RAI54425.1,
RC ECO:0000313|Proteomes:UP000249713};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) 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:RAI54425.1}.
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DR EMBL; QLIW01000004; RAI54425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327LWY7; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000249713; 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; IPR022107; DNA_pol_III_gamma/tau_C.
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 Pfam; PF12362; DUF3646; 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:RAI54425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249713};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RAI54425.1}.
FT DOMAIN 43..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 382..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 63553 MW; 4AFBFD78D83007C5 CRC64;
MSEHTTKGYQ VLARKYRPET FADLVGQDAM VRTLKNAFMA DRIAQAFIMT GIRGTGKTTT
ARIIAKGMNC IGPDGTGGPT TDPCGVCEHC TAIMEGRHVD VMEMDAASRT GVGDIREIIE
SVHYRAASAR YKIYIIDEVH MLSTSAFNAL LKTLEEPPEH VKFIFATTEI RKVPVTVLSR
CQRFDLRRIE PEDMIAMLRR IATAEEAQIA DDALALITRA AEGSARDATS LLDQAISHGA
GETTATQVRA MLGLADRGRV LDLFDMIMKG DAAGALAELA AEYAEGADPL AVLRDLAEIT
HWVSVVKITP DAAEDPTISP DERSRGQAMA GALPLRVLAR MWQMLLKALD EVAQAPNAMM
AAEMAIIRLT HVADLPTPED LVKRLNDETP PPPPPTRGAP LPPQGSGGGN GQANTPLSSG
RSTSGRSGGP SAALAQDSAQ ALARYPTFDH VLELIRANRD GKLLMDVEAD LRLVSYQPGR
ITFQPTPDAP SDLASRLGAA LQRWTGNRWA VTVTSENGTP SIVETRNAER VSRESEARDH
PLVQAVFDVF PNARIVDIKT RRDITAEAQA EALPEVEEEW DPFEEE
//
