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Database: UniProt
Entry: A0A1Y4SKA4_9FIRM
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ID   A0A1Y4SKA4_9FIRM        Unreviewed;       605 AA.
AC   A0A1Y4SKA4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=B5E79_05575 {ECO:0000313|EMBL:OUQ29850.1};
OS   Massilimicrobiota sp. An134.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Massilimicrobiota.
OX   NCBI_TaxID=1965557 {ECO:0000313|EMBL:OUQ29850.1, ECO:0000313|Proteomes:UP000195713};
RN   [1] {ECO:0000313|Proteomes:UP000195713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An134 {ECO:0000313|Proteomes:UP000195713};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUQ29850.1}.
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DR   EMBL; NFLH01000009; OUQ29850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4SKA4; -.
DR   Proteomes; UP000195713; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; 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; 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; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR004622; DNA_pol_HolB.
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   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   NCBIfam; TIGR00678; holB; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 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   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|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU364063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195713};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          37..177
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   605 AA;  69364 MW;  101A293E6526A5D2 CRC64;
     MAYKTLYRVY RPQKFEDVAG QEHIITTLKH AVDENKIAHA YLFCGPRGTG KTTIAKLLAK
     AVNCTGSPKP CDQCENCQQI TLGTHPDVIE IDAASNNGVD EVRNLIEKVK YAPTQGKYKV
     YIIDEFHMMS PGASNALLKT LEEPPTHVIF IFATTEPHKI LPTIISRCQR FDFTKLSIQD
     IVHRMKDIIN EEHYECDDEA LELIAKLADG GMRDALSILE QCLAYNDQHL TVKDVNQIYG
     IVSLENKIDF IKTILSKDMK KALSLLDDMK MNGTDIKRLT LDLVDILKDV VIYRNTHDES
     ILFVLSKYYL DLIVPYMGCE EALDFIDILM DASEKYAKVI NPSVYFELAI LKMCNQIKDE
     KVIHMETVKV PEQPIQQLKQ SDVIIEDHHD VEEDHHDMIE EEPVQEEIID ESIDDSSLES
     HENDDIPTFE FEQKQDIEPT VDDEIQVDEA DIMNILVQAK RTILESIQER WPIIKRYLAN
     LNMAKSASML CDGTAVAACE GGLIISFEYQ PSVNAVNYYK NYKQLSAFLS EVLGNEYRFI
     AIQQDEWLKM RSHFIELKRK GQLPQPHELT LKHIDSHDLD HVDMTEAQEF AIQLFGEDIV
     EFKED
//
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