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Entry: A0A078KYE7_9GAMM
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ID   A0A078KYE7_9GAMM        Unreviewed;       577 AA.
AC   A0A078KYE7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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_1 {ECO:0000313|EMBL:CDZ77941.1};
GN   Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN   ORFNames=BN59_02237 {ECO:0000313|EMBL:CDZ77941.1};
OS   Legionella massiliensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ77941.1, ECO:0000313|Proteomes:UP000044071};
RN   [1] {ECO:0000313|EMBL:CDZ77941.1, ECO:0000313|Proteomes:UP000044071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUN-2014) 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; CCSB01000002; CDZ77941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078KYE7; -.
DR   STRING; 1034943.BN59_02237; -.
DR   eggNOG; COG2812; Bacteria.
DR   Proteomes; UP000044071; 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; IPR001270; ClpA/B.
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-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; PF12170; DNA_pol3_tau_5; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
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   Reference proteome {ECO:0000313|Proteomes:UP000044071};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          50..206
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          422..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  64531 MW;  38BFD87D94C3FB3A CRC64;
     MALRAAAQLV KVHMSYLALA RKWRPRTFSQ LVGQEHINKA LINSLNQQRL HHAYLFTGTR
     GVGKTSVARL LAKALNCEAG ISSEPCLRCE ACVAIEQGRF IDLIEIDGAS RTRVEDTREL
     LENVQYRPTN GRFKIYLIDE VHMLSQHSFN ALLKTLEEPP EHVKFLLATT DPQKLPVTVL
     SRCLQFSLKH LTTEIISHHL QHLLNEEQIA FEKEAIDLLA KAAKGSMRDA LSLLDQAIAS
     ADGKLVAQET KAILGYTQQD YAIQLLQALA KLDAQEIIHL SRQIASEGGH FRYVIDDLLE
     NLHQITIAQA LVSDNPLLSP RSEVKVLAQQ FSPEDTQLFY QIGIKGTEEM LLAPTIAIGF
     EMILLRMLTF RPAPKVDTPP LAYEKPGVKT TDLLAVSIEN CAKGNEQNPA PSIDIIERTE
     KHAEEKQVEP EPRPPSSAYM PEQNPVVPND EDWASILSRL NLAGLTLNAA ENAEFIEKSG
     REIRLRVAKG HQSLFTPSVT GRIEQALESY YKEPIKIALS SDEPVQSSPA LQKQIAQNLR
     QQDAEVNLQN DPFFQQLRQE FSAELVKNSI VPVKDEL
//
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