ID C1F0Z1_ACIC5 Unreviewed; 698 AA.
AC C1F0Z1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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:ACO32861.1};
GN OrderedLocusNames=ACP_0491 {ECO:0000313|EMBL:ACO32861.1};
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO32861.1, ECO:0000313|Proteomes:UP000002207};
RN [1] {ECO:0000313|EMBL:ACO32861.1, ECO:0000313|Proteomes:UP000002207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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|RuleBase:RU364063}.
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DR EMBL; CP001472; ACO32861.1; -; Genomic_DNA.
DR RefSeq; WP_012680882.1; NC_012483.1.
DR AlphaFoldDB; C1F0Z1; -.
DR STRING; 240015.ACP_0491; -.
DR KEGG; aca:ACP_0491; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_7_0; -.
DR InParanoid; C1F0Z1; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000002207; 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 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; IPR012763; DNA_pol_III_sug/sutau_N.
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 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:ACO32861.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002207};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ACO32861.1}.
FT DOMAIN 37..189
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 390..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..521
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 74931 MW; 67D740FE53A54DA7 CRC64;
MAYQVLARKY RPQRFSDVAG QEHVTRTLLN ALAQGRIAHG YIFSGHRGIG KTTIARILAM
ALNCRTPIGS TTGSPQRPTP EPCGVCESCE EIRLSNAVDV LEIDAATNRG IDEIRELREA
ARYRPSRDRY KIYILDEAHQ ITDAAFNALL KTLEEPPDHV VFMMATTEPE NIPQTIRSRC
QHFSFHAVKF DDILAQLRAI ATQENIVAED AALALLAEAG DGSMRDALSI MDQAIASARL
ENGQPHLDAE AIRELMGSVP NTVFERLLEA ISENQSAAVL EELNRLLNAG NSPVQLARQF
VRYLRNTIMA KIGGEQTDLL QISPDERARV GRSALLFSEE DLTRFLQIML RTFDELNYRQ
EQRFHLELGL IKLVHLQRLL PVEEFLSQLP PGTGAARSIS SATSSPAASR PSPAATAPPV
RATPPPRPAP AAPASTPEPS RPAFSPFEAD RQRKITSEDT APAPVAAPSA PSIEAATPAP
SVTTPSVNSV PVTSLPIAPP AEPVPAPMAA QPAPAAPSIP EPVAASRPLT PLEAASRAVE
AAPAKPSMRV GVAEPERTEG ALALASAPAA EADLDHIAQA VCSALEREGH GTASVLLSSG
NWTQQGDTIQ VEVAIKRMML SLTMNAEAEK ICKNAMRSIG ATQKLVFVPG EGNRAAGSKP
AIAITGSIQS AALENPLVQK AKELFRGEIR SVLDLRDK
//
