ID A0A2Z2NSJ8_9GAMM Unreviewed; 602 AA.
AC A0A2Z2NSJ8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:ASJ74482.1};
GN ORFNames=IMCC3135_22050 {ECO:0000313|EMBL:ASJ74482.1};
OS Granulosicoccus antarcticus IMCC3135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Granulosicoccaceae; Granulosicoccus.
OX NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ74482.1, ECO:0000313|Proteomes:UP000250079};
RN [1] {ECO:0000313|EMBL:ASJ74482.1, ECO:0000313|Proteomes:UP000250079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ74482.1,
RC ECO:0000313|Proteomes:UP000250079};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; CP018632; ASJ74482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2NSJ8; -.
DR KEGG; gai:IMCC3135_22050; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000250079; 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; 3.30.300.150; 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 ECO:0000313|EMBL:ASJ74482.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250079};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ASJ74482.1}.
FT DOMAIN 37..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 409..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 65086 MW; CD7502307F9AD30D CRC64;
MSYKVLARKW RPQHFRDMLG QEPVLRALVN ALDTNRLHHA YMFTGMRGVG KTTIARIFAK
CLNCETNGVS SNPCGECSAC RDIEAGRFFD LIEVDAASRT KVEETRELLE NVPYAPASGR
YKVYLIDEVH MFSNHSFNAL LKTLEEPPEH VKFLLATTDP QKVPVTVLSR CLQFNLKRMA
PGNLADYLSK ILDEESIEHE RPALDLIARA SEGSVRDSLS LVEQAAAFGE GAVRESDVET
MLGRASVDRL LGLVESLGRG DVAQLFERVE QLAEYAPDFS ELMGEILSLL HRIALLQMVP
GSVSEDTAGF ERLTQLATEL ADDEIQLYYQ IGTHARRDMP FAPDPREAFD MALLRMNTFR
PQGEPGQPSA PGSVPALAPV AAPVAPASTA ARGSVSAGAA LRDAALAAAR GETVPTKPTP
AAVEPAVRAP AAQTPPAQTA RPPAAPMPAA QAPAAPTPTA RAPASSASVD RSNIKIGDWR
SIVAELDISG MPKQLASNCE LVSVAGDAFN LRLESTSEHL HTPRFSERVQ TALSEWLGRP
AKLQISLVDD QLSTPSRIDE QVRADQMSAA RDSIGQDPVV RQLIDRVDAA VDEASIAPLG
ED
//
