ID A0A0S4L884_9BACT Unreviewed; 589 AA.
AC A0A0S4L884;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:CUS33022.1};
GN ORFNames=COMA1_10937 {ECO:0000313|EMBL:CUS33022.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS33022.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS33022.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS33022.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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; CZQA01000001; CUS33022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4L884; -.
DR STRING; 1742972.COMA1_10937; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000199032; 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; 3.40.50.300; 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; IPR045085; HLD_clamp_pol_III_gamma_tau.
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:CUS33022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199032};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:CUS33022.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 363..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 64449 MW; E02ECF5A04C36D75 CRC64;
MDYQVSARKY RPGTFDDVIG QSHVVQTLMN AVSTKRVAHA YLFSGTRGVG KTTVARIFAK
ALNCAQGPTS HPCDTCENCR EIALGSSVDV IEIDGASNTS VDDVREIREN VKFAPFHGQF
RVYIIDEVHM LSNSAFNALL KTLEEPPAHA VFIFATTEIH KIPVTILSRC QHYNFRRIAR
SEIIQRLQHV AAQDQLTLEE RSFLALARAS EGSMRDALSL LDQAIAYSGK AISHADLELL
LGAVPQELVQ ELIRAILTQN SPAALSSLAS LLDRGHDLRA FCADVVEHIR NLLVAAVVPS
ATELRSLIET SEEDLNQLSS DARAVTPEQL QELLAIFIQA EDSLRFSTHP RFVMETAAVR
ATRLLRPRPS DSLSPQQTSP SSSHKPLGDS EGHKTTPAPS PIRKPANQPP PPSKASKVER
PIPSPDPSPK PIVDRSAVSS ATEPAPLSPQ PSTLRWELVQ EEIAASFPNI APFLEAGRFV
GLEAGVVTIG FAKQATVARA RLEKEENTKV IAQLCERQMG PPIRVRIIEL TETHPQGPTM
AQARAAKEQE HRTALFEQAK TNPTVKQALE IFGVELADVR TIAQQEASE
//
