ID   DPO3X_BUCAI             Reviewed;         361 AA.
AC   P57553; Q9F453;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, 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=BU481;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13178.1; -; Genomic_DNA.
DR   RefSeq; NP_240292.1; NC_002528.1.
DR   RefSeq; WP_009874434.1; NC_002528.1.
DR   AlphaFoldDB; P57553; -.
DR   SMR; P57553; -.
DR   STRING; 107806.10039144; -.
DR   EnsemblBacteria; BAB13178; BAB13178; BAB13178.
DR   KEGG; buc:BU481; -.
DR   PATRIC; fig|107806.10.peg.490; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_0_1_6; -.
DR   OMA; IRENAKY; -.
DR   Proteomes; UP000001806; 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..361
FT                   /note="DNA polymerase III subunit gamma"
FT                   /id="PRO_0000105494"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   361 AA;  41607 MW;  8771F5A74EAB415E CRC64;
     MNYQILARKW RPQYFRDIIG QKHIVTAISN GLSLGRIHHA WLLSGTRGIG KTTIARLLAK
     SLNCQNGITS DPCRQCIICK EIEKGLCLDV IEIDGASRTK VEEMREILDS IYYSPIKSRF
     KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFVLATTDVD RIPKTIISRC LYFKLQIISE
     EKIFKFLKYI LIKESIDTDE YSLKKIAYHA HGSIRDALNL LEHAINLGNG HVNIKNVTDM
     LGLLPEKYSF LLTDAVLKKD SKKTMLLLNK ISSIGVEWEE ILIEMLRFLY HISTSQSFPL
     VWEKIFTEKY KNQIQKIAQN NKKTNIQLCY QILLNGRKEL KFAPSQKIGV EMSLLRVISA
     I