ID   Q9CDM5_LACLA            Unreviewed;       552 AA.
AC   Q9CDM5;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaH {ECO:0000313|EMBL:AAK06292.1};
GN   Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN   ORFNames=L0279 {ECO:0000313|EMBL:AAK06292.1};
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK06292.1, ECO:0000313|Proteomes:UP000002196};
RN   [1] {ECO:0000313|EMBL:AAK06292.1, ECO:0000313|Proteomes:UP000002196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403 {ECO:0000313|EMBL:AAK06292.1,
RC   ECO:0000313|Proteomes:UP000002196};
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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       {ECO:0000256|RuleBase:RU364063}.
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         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU364063};
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
CC       complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; AE005176; AAK06292.1; -; Genomic_DNA.
DR   PIR; B86899; B86899.
DR   RefSeq; NP_268351.1; NC_002662.1.
DR   RefSeq; WP_010906374.1; NC_002662.1.
DR   AlphaFoldDB; Q9CDM5; -.
DR   PaxDb; 272623-L0279; -.
DR   EnsemblBacteria; AAK06292; AAK06292; L0279.
DR   KEGG; lla:L0279; -.
DR   PATRIC; fig|272623.7.peg.2356; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_0_3_9; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000002196; 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:0016887; F:ATP hydrolysis activity; 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   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
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   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:AAK06292.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002196};
KW   Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:AAK06292.1}.
FT   DOMAIN          37..184
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   552 AA;  60766 MW;  CC0438E81C6C2D3B CRC64;
     MAYQALYRKY RSQRFDEMVG QEVVATTLKN AIVNHQISHA YLFSGPRGTG KTSAAKIFAK
     AINCPNQVDG EPCNNCFICD SITKGSLDDV IELDAASNNG VDEIREIRDK STYAASQATY
     KVYIIDEVHM LSTGAFNALL KTLEEPTENV VFVLATTELQ KIPATIISRV QRFAFKSITT
     GDIRTYLAKI MADEGLEFDG KALDVIAKAA EGGMRDALSL LDQALSFSSG KLEENDALLV
     TGSIAADALV TYVAALFEHD EAKAMTELDK IFAEGKNMLR FTEDLLAYLR DLLLDKNSQY
     DRGQIFSWID VAIESLKTIK ETTQTKIAAD VMTMRLAEIG QNNLLTASQG EIPNQLTAEI
     ATLKTEINQL KAQISAGQIQ VNSDSQNNLL TENVKASPKP IASKKRQINK DLIYKALAEA
     TNEARKAALS AWPELVASVT KPADRALLNN TAPVAASENF LVVTFPHENL AKRVSENEEL
     QLFCGNLLSS IVGFAPEIIS LAEQDWQEVR AEYVSNLKSE NVQEDEEDEK EPDETVNLAK
     ELFGEKVVEI ND
//