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Database: UniProt
Entry: Q1QQZ5_NITHX
LinkDB: Q1QQZ5_NITHX
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ID   Q1QQZ5_NITHX            Unreviewed;       615 AA.
AC   Q1QQZ5;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 103.
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=Nham_0462 {ECO:0000313|EMBL:ABE61352.1};
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE61352.1, ECO:0000313|Proteomes:UP000001953};
RN   [1] {ECO:0000313|EMBL:ABE61352.1, ECO:0000313|Proteomes:UP000001953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14
RC   {ECO:0000313|Proteomes:UP000001953};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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; CP000319; ABE61352.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1QQZ5; -.
DR   STRING; 323097.Nham_0462; -.
DR   KEGG; nha:Nham_0462; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_0_7_5; -.
DR   OMA; HVDVMEM; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000001953; 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; 3.40.50.300; 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; IPR022107; DNA_pol_III_gamma/tau_C.
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-LIKE 2; 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; PF12362; DUF3646; 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:ABE61352.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001953};
KW   Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ABE61352.1}.
FT   DOMAIN          67..215
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  66615 MW;  1AC96295A07E57C4 CRC64;
     MTDAGNPATS TDGAAGQSGF DLGVGPSESG AAYRVLARKY RPASFDDLIG QEALVRTVSN
     AFETGRIPQA WILTGVRGVG KTTTARILAR ALNYELPDGS VKGPTIRMPK LGVHCQAIME
     SRHIDVLEMD AASHTGVDDV RQINDSVRYA PSSARYKVYI IDEVHMLSTA AFNAFLKTLE
     EPPEHAKFVF ATTEIRKVPV TVLSRCQRFD LKRVDADVLV THLGNIAAKE NVEVEPEALG
     IVARAAEGSV RDSLSLFDQA IAHAAGVVRA DAVRQMLGLA DRTRVIDLFY SLARGDIASA
     FREFRDQYDT GADPVVVLSD LAEFVNFVTR IKIVPALADN IAFGETERLR ARDFAAKLSM
     RVLSRMWQML LKGITEVQGA TRPAAAAEMV LVRIAYVADL PTPDEAIRML DRNGGESPVV
     PNNAAPQRPA PGSMSSAQSS AARTLSAPRA AAEPASRPQA ITPMVDPTGA VPAVRLESFT
     ELVALAGEKR DLIIKAALEA DMRLVRMEDG RLEVALERSA ARTLVNELAR KLEQWTGRRW
     TVIVSNEPGQ PTLRSQALLQ KNERERAAEA DPRVKDVLAR FPGAKVVEVR KLALSPPDSD
     TVPDDQADGF DGGDE
//
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