DPO3X_BUCAP
ID DPO3X_BUCAP Reviewed; 363 AA.
AC Q8K983;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA polymerase III subunit gamma;
DE EC=2.7.7.7;
GN Name=dnaX; OrderedLocusNames=BUsg_466;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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 -!- 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 -!- 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 complex
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR EMBL; AE013218; AAM68009.1; -; Genomic_DNA.
DR RefSeq; WP_011053976.1; NC_004061.1.
DR AlphaFoldDB; Q8K983; -.
DR SMR; Q8K983; -.
DR STRING; 198804.BUsg_466; -.
DR EnsemblBacteria; AAM68009; AAM68009; BUsg_466.
DR KEGG; bas:BUsg_466; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_1_6; -.
DR OMA; IRENAKY; -.
DR OrthoDB; 556582at2; -.
DR Proteomes; UP000000416; 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: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; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF12169; DNA_pol3_gamma3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..363
FT /note="DNA polymerase III subunit gamma"
FT /id="PRO_0000105495"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 42186 MW; F22762B7493B091A CRC64;
MNYQILARKW RPQSFKKIIG QKYIVKAISN GFSLGKIHHA WLLSGTRGVG KTTIARLIAK
SLNCEIGITS LPCRKCTICQ EIEKGICLDF IEIDAASRTK VEEIREILDN IYYTPSKSRF
KVYLIDEVHM LSRHSFNALL KTLEEPPQHI KFILATTDVE KIPKTIRSRC LHFKLNILSE
EDIFNFLKHI LKKGGNNFDE EALKIISDYA NGSMRDALNL LEHAMHLSKN NINLKNTTEM
LGIPNKKHAF LLTKFLLEQD SKKMMCLLNK ISKIGLEWQN ILIEMMRFLH HIAMLKSYPK
IWNQIFIKNN ENEIKKIAEN NSKYNIQLCY KILLKGRKEL FFSPNHKMGV EMILLQAITE
IKR