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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
 
 
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