ID A6Q505_NITSB Unreviewed; 512 AA.
AC A6Q505;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=NIS_1457 {ECO:0000313|EMBL:BAF70564.1};
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor.
OX NCBI_TaxID=387092 {ECO:0000313|EMBL:BAF70564.1, ECO:0000313|Proteomes:UP000001118};
RN [1] {ECO:0000313|EMBL:BAF70564.1, ECO:0000313|Proteomes:UP000001118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2 {ECO:0000313|EMBL:BAF70564.1,
RC ECO:0000313|Proteomes:UP000001118};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF70564.1; -; Genomic_DNA.
DR RefSeq; WP_012082827.1; NC_009662.1.
DR AlphaFoldDB; A6Q505; -.
DR STRING; 387092.NIS_1457; -.
DR KEGG; nis:NIS_1457; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_8_7; -.
DR InParanoid; A6Q505; -.
DR Proteomes; UP000001118; 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: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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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.
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:BAF70564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001118};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:BAF70564.1}.
FT DOMAIN 34..176
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 58441 MW; F13890DB2C5BB14F CRC64;
MALALKYRPK RFEDLIGQEA VTQTLQRALD TKNLSHAYLF SGLRGSGKTS TARIFSKALI
CDGGPTSSPC ETCENCQAAN EGRHIDIIEM DAASNRKIDD IRDLIEHTKY KPSSARYKIF
IIDEVHMLTK EAFNALLKTL EEPPEFVKFI LATTDPLKLP ATILSRTQHF RFKKIAQRDI
VHHLEHILNL ENVEYEPEAL QILARSGSGS LRDTLTLLDQ AITFGKNRVS VEAVTNMLGL
VDPKKIEALF DMILRQDKEA ILQTVQELRD YEAQMVLDEM LIFLKNQLFS KNSTFSMMLY
ERFFKILSDG KNLLFVSGDD EFVLMITLMK LMEATKIKSV EELIEEFESK ETPTISHTPP
PIQTNEQTKT SQPVQKDPFQ RLIDKLYERN YELGECFEKS VKFIDFSDNV LRWESNPPAE
CKEKLKHSYP TIRHFVQEVF GIDTKIVKVD PPKSCDEPSS MIEEAEFGGS CIQKEAGLSA
KEMDGTNILE DPFVRKAKEL FKAKKVVIKP KI
//
