ID D3SBE1_THISK Unreviewed; 587 AA.
AC D3SBE1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 OrderedLocusNames=TK90_1855 {ECO:0000313|EMBL:ADC72346.1};
OS Thioalkalivibrio sp. (strain K90mix).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72346.1, ECO:0000313|Proteomes:UP000009099};
RN [1] {ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC72346.1, ECO:0000313|Proteomes:UP000009099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix {ECO:0000313|EMBL:ADC72346.1,
RC ECO:0000313|Proteomes:UP000009099};
RX PubMed=22675584; DOI=10.4056/sigs.2315092;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL Stand. Genomic Sci. 5:341-355(2011).
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; CP001905; ADC72346.1; -; Genomic_DNA.
DR RefSeq; WP_012983221.1; NC_013889.1.
DR AlphaFoldDB; D3SBE1; -.
DR STRING; 396595.TK90_1855; -.
DR KEGG; tkm:TK90_1855; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000009099; 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; 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:ADC72346.1};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ADC72346.1}.
FT DOMAIN 37..177
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 366..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 63579 MW; 55B5BD9DF580D422 CRC64;
MSHQVLARKW RPGRFEDLVG QPHVVRALAN ALSGDRLHHA YLFAGTRGVG KTTIARILAR
CLNCETGITA TPCGECRSCV EIAEGRHLDL IEVDAASRTR VDDTRELLDN VSYAPTAGRF
KVYLIDEVHM LSEKSFNALL KTLEEPPDHV KFLLATTDPQ KLPVTVLSRC LQFNLKPMPP
ALIAEHLTRI LEAEGLQAEP GALLRLGEAA EGSMRDALSL TDQAIAYGGD RLTESDACDM
LGLLPRTRLT GLLDAAFAGD GPGLMQGLQE LKGLGPDWSR LLDELAALVH RVAVEQLVRG
EGGAEDDDAA ERWARETAAR IDAETLQLTY QILIHGARDL PWAPDAQMGV EMTLLRLLAF
RPEGPGEGAV SVERQGGTPA TAPRTGPSAD PATARPDATM RSAPPPIPEP PRERAQERVR
EPDPGSDIGL NESAPRPRDA EPVRSPEPDS GPFDWHRFAE GLPTGTVREL ALHGELQQLD
DESVVIAVAP GTLYTDRTRT RLKEALETRL GHSVRLEIVD QTQPSQATPA ARLAADAAER
QASAETAMRE DPVVQALGEA FGAELGTVRI REDRAGDEPS ASQSIER
//
