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Database: UniProt
Entry: A0A1D9P5Q3_9FIRM
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ID   A0A1D9P5Q3_9FIRM        Unreviewed;       552 AA.
AC   A0A1D9P5Q3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=dnaX {ECO:0000256|RuleBase:RU364063};
GN   ORFNames=bhn_II070 {ECO:0000313|EMBL:AOZ97869.1};
OS   Butyrivibrio hungatei.
OG   Plasmid pnp144 {ECO:0000313|Proteomes:UP000179284}.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ97869.1, ECO:0000313|Proteomes:UP000179284};
RN   [1] {ECO:0000313|Proteomes:UP000179284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RC   PLASMID=Plasmid pnp144 {ECO:0000313|Proteomes:UP000179284};
RA   Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA   Attwood G.T.;
RT   "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT   MB2003.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364063}.
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DR   EMBL; CP017832; AOZ97869.1; -; Genomic_DNA.
DR   RefSeq; WP_071177628.1; NZ_CP017832.1.
DR   AlphaFoldDB; A0A1D9P5Q3; -.
DR   KEGG; bhu:bhn_II070; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000179284; Plasmid pnp144.
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   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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   Pfam; PF12169; DNA_pol3_gamma3; 1.
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   Plasmid {ECO:0000313|EMBL:AOZ97869.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179284};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          34..174
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   552 AA;  59893 MW;  623780EB19AB897C CRC64;
     MSLYNELRPK SLSEVQGQDT IKAQLKGMFL SKKVPNAMLF NGPRGTGKTT VARIVARTLN
     CESGGMEPCG ECQQCKDILN GSSLDVIELD AASNNKVEDV RGIIEKAQYI SSSNYKVFIL
     DEVHMFSQGA WNALLKLIEE PPKNVVFIMC TTEEHKVPKT IISRARRFNF ETISLDVISD
     YLMQVCNEHG KAYDVDAIRL IAAASDGGMR DALSILEPFY DDDCITTSVV TETLGITPEK
     AIFDLLFSIE KGDVASAISV VRDAVTKGKN LQVMLKSIIN TLTDALFVMT GASVETLVNT
     DSYRELLLSY VEKVDVDSIL KLSKSLSDVY GVLAKVPDSE FLIETALIRA VNDMASQISL
     KEIERRVSDL EKGVSSMPVD VKPVDVQVDN VVNIATKEVS SNDTNEEPAD GFAPISESDE
     LPFVLDEIPD ELPIDGDLSV AAVSEMQVNE PVPQSVSESV VDVPSDSSTA VAATSNTIPD
     ELLSHLPAGT KVLGEAISST VETPCESDSE DTNVVNDLAG EVKEEAEETA MFKADEEIPA
     FGFANSFSGW LQ
//
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