ID A0A0B0HCQ6_SOVGS Unreviewed; 546 AA.
AC A0A0B0HCQ6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=JV46_18700 {ECO:0000313|EMBL:KHF25694.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF25694.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF25694.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF25694.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
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:KHF25694.1}.
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DR EMBL; JRAA01000001; KHF25694.1; -; Genomic_DNA.
DR RefSeq; WP_043115368.1; NZ_JRAA01000001.1.
DR AlphaFoldDB; A0A0B0HCQ6; -.
DR STRING; 2340.JV46_18700; -.
DR PATRIC; fig|2340.3.peg.209; -.
DR eggNOG; COG2812; Bacteria.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000030856; 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; 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; 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 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 ECO:0000313|EMBL:KHF25694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KHF25694.1}.
FT DOMAIN 37..177
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 364..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 60467 MW; FC1D7D0B0070F221 CRC64;
MSYEVLARKW RPHGFAELVG QEHVVQALSN ALDQDRLHHA YLFTGTRGVG KTTLARIFAK
SLNCEEGVSS TPCGVCSTCR EVDEGRFVDL LEVDAASRTK VEQTRELLEN VPYAPAKGRY
KVYLIDEVHM FSDSSFNALL KTLEEPPPHV KFLLATTDPQ KLPMTVLSRC LQFGLKRLTL
EQIAGQLRHI LDVEKVGHDD TAVTLLAYGA DGSMRDGLSL LDQAINFGGG EVVEEKVASM
LGTVSRDYVF GLVEALVARD GKLLMQKIDA LADRSPDFRS VLDELLRMLH RVAVLQTVPD
LNVENEVDHE RYAWMVETVP ADEVQLYYQI GITGKRDMPM APDLRSGFEM VMLRMLAFQP
GAVSQPAEAP RQAQKKSPEP VAAPAARQAE AATEAEAETK KKVQQQAVPA APVSQDAELP
QSVDWNQLQK ELKLGGISGQ LAMNCAFDSV DGNLFRLVLP EEHQALQSDM AVKRMEEELR
KHFGCAALKL EIALGKPQVD TPAQRKLRLE NQRLAEAKAG MVNDPFVKEL QQQLGARVID
ETIKPV
//
