ID   HOLB_BUCAP              Reviewed;         328 AA.
AC   Q8K9J2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA polymerase III subunit delta';
DE            EC=2.7.7.7;
GN   Name=holB; OrderedLocusNames=BUsg_342;
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 (By similarity).
CC       {ECO:0000250}.
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}.
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DR   EMBL; AE013218; AAM67896.1; -; Genomic_DNA.
DR   RefSeq; WP_011053863.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9J2; -.
DR   SMR; Q8K9J2; -.
DR   STRING; 198804.BUsg_342; -.
DR   EnsemblBacteria; AAM67896; AAM67896; BUsg_342.
DR   KEGG; bas:BUsg_342; -.
DR   eggNOG; COG0470; Bacteria.
DR   HOGENOM; CLU_006229_4_3_6; -.
DR   OMA; YSRCQVW; -.
DR   OrthoDB; 1971388at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; 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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR015199; DNA_pol_III_delta_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF09115; DNApol3-delta_C; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..328
FT                   /note="DNA polymerase III subunit delta'"
FT                   /id="PRO_0000105511"
SQ   SEQUENCE   328 AA;  38927 MW;  160BA0FE21BAD08D CRC64;
     MKWYPWLIKP YKKIIRLHER KKAHHAILIK TQKGMGVFKL VWFISKWLLC LKPKGTNFCD
     NCHGCKLMSA NNHPDWHTII NEKNDVFDVD SIRVINEKIF KRAQQGNNKI IFLPNVHKLT
     ESAVNALLKI LEEPPEKNWF FLIDYNYLKL HSTLKSRCFL YRLPLPLEKE SLNWLKNNNK
     KDNISNLTSL RINQDSPISA KNFIESDLWD ERKNLYKSLS HSIKDKNLLK ILPVLCKKNT
     IMKIDWICLL LFDAVKTNFN ERKKLINCDQ IKLINFFSKK YNNILLNKSI RKWTKCRYIL
     SSVSSINSEL LLLEQLLLWE KILCFITP