ID   DPO3X_BUCBP             Reviewed;         370 AA.
AC   Q89A95;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA polymerase III subunit gamma;
DE            EC=2.7.7.7;
GN   Name=dnaX; OrderedLocusNames=bbp_425;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27135.1; -; Genomic_DNA.
DR   RefSeq; WP_011091536.1; NC_004545.1.
DR   AlphaFoldDB; Q89A95; -.
DR   SMR; Q89A95; -.
DR   STRING; 224915.bbp_425; -.
DR   EnsemblBacteria; AAO27135; AAO27135; bbp_425.
DR   GeneID; 56470960; -.
DR   KEGG; bab:bbp_425; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_0_1_6; -.
DR   OMA; IRENAKY; -.
DR   OrthoDB; 556582at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..370
FT                   /note="DNA polymerase III subunit gamma"
FT                   /id="PRO_0000105496"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   370 AA;  42722 MW;  4E352CC0173850ED CRC64;
     MNYHILAKKW RPQTFNDVIG QQYIVSAISN SLLLGRIHHA WLFFGIRGTG KTTIARILAK
     SLNCKLGISP NPCRKCSNCV EVEQGNFIDL YEVDAASRTK VEDMKELLDN IRYLPSKGRF
     KIYLIDEVHM LSRYSFNFLL KNIEEPPQHI KFILATTNLE KIPDTILSRC LQFQLKPINL
     NEIVACISNI LHKENITYEI KALSLISQKS EGSLRDAITL TEQMISMGKG NITEKIVRKT
     LGMLYEDQIL YILTTLLNKD LKNLVLCFKY ISDTHINFEN ILVEILQLLH QISIIKIIPS
     IKLNDTKYSK NMQHAIQKIA ELSNYNDIYL YYQTALLGKK ELHIAPDQKI SIEMTLLRMF
     NLNTKPIYIK