ID J3DJL8_9BURK Unreviewed; 675 AA.
AC J3DJL8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=PMI16_00644 {ECO:0000313|EMBL:EJL93321.1};
OS Herbaspirillum sp. CF444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL93321.1, ECO:0000313|Proteomes:UP000007296};
RN [1] {ECO:0000313|EMBL:EJL93321.1, ECO:0000313|Proteomes:UP000007296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF444 {ECO:0000313|EMBL:EJL93321.1,
RC ECO:0000313|Proteomes:UP000007296};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL93321.1}.
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DR EMBL; AKJW01000016; EJL93321.1; -; Genomic_DNA.
DR RefSeq; WP_007876325.1; NZ_AKJW01000016.1.
DR AlphaFoldDB; J3DJL8; -.
DR STRING; 1144319.PMI16_00644; -.
DR PATRIC; fig|1144319.3.peg.644; -.
DR eggNOG; COG2812; Bacteria.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000007296; 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; 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 Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..184
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 461..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 71126 MW; 0948ACB9E6E6C204 CRC64;
MSYQVLARKY RPRSFDTLVG QEHVVRALTH ALDQQRLHHA YLFTGTRGVG KTTLSRILAK
SLNCQGPDGN GGITAQPCGV CEACVAIDAG RFVDYIEMDA ASNRGVDEMA QLLEQAIYAP
SNARFKVYMI DEVHMLTNHA FNSMLKTLEE PPEHVKFILA TTDPQKIPVT VLSRCLQFNL
KQMPPGHIIS HLDNILGQEN IEFEAPALRL LAQGAHGSMR DALSLTDQAI AYAAGKVTLE
AVQGMLGALD QSYLIRVLDA LAAQDGAALL SVADEMATRS LSYNAALQDL ATLLHQIALA
QTVPAALAED VPQREDIVRL ASQFNPEEAQ LFYQIAVHGR NELGLAPDEY AGFSMTLLRM
LAFRPVAAGA AGAVGSAPAA PVARPTAAPA RSTPAAAPLS AAPQVATASA PVSRPPASSV
PAAGPANSAR AAALEAARAA SGKSAPRPAA VASAPMPVQA APVAAPTPAP AAMSDDTPPP
WDEEPAGADA QKKTEQYSAD SVNAAASVAI YTAADNAEDA IVLAPPVAPA STITPAMQAQ
TAQVAAELGW DGNWPHLAAD LPLRGMVQQM AQQSELVRCE LTGNTVCFHL RIPVETLRAS
GNVDKLASAL GERFGKSVRV ETEIGLVAHT ANAKAEADRA DRQREAEKTV QNDPFVQVMM
REFGASIVPG SIRPL
//
