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Database: UniProt
Entry: B0PF11_9FIRM
LinkDB: B0PF11_9FIRM
Original site: B0PF11_9FIRM 
ID   B0PF11_9FIRM            Unreviewed;       536 AA.
AC   B0PF11;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   ECO:0000313|EMBL:EDS09944.1};
GN   ORFNames=ANACOL_03390 {ECO:0000313|EMBL:EDS09944.1};
OS   Anaerotruncus colihominis DSM 17241.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS09944.1, ECO:0000313|Proteomes:UP000003803};
RN   [1] {ECO:0000313|EMBL:EDS09944.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09944.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS09944.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09944.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) 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:EDS09944.1}.
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DR   EMBL; ABGD02000025; EDS09944.1; -; Genomic_DNA.
DR   RefSeq; WP_006876252.1; NZ_DS544186.1.
DR   AlphaFoldDB; B0PF11; -.
DR   STRING; 169435.ERS852551_00330; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_0_5_9; -.
DR   Proteomes; UP000003803; Unassembled WGS sequence.
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; 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; 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-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   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:EDS09944.1};
KW   Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:EDS09944.1}.
FT   DOMAIN          36..187
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          382..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  57912 MW;  1341697CCEF3073C CRC64;
     MYQALYRKWR PKTFDDVVGQ EHITATLKNE VAAGKFSHAY LFTGSRGTGK TTCSKIVAKA
     VNCERPVDGN PCNECAACRG IDDGSVLDVV EIDAASNNGV DNIRQLREEA YFLPSVVKYR
     VYILDECHML SQGAVNALLK ILEEPPEHVV FILATTEIHK VLPTILSRCQ RFDFHRIRSR
     VIADRLLYIA EQESFSLADD AALLIARLSD GGMRDALSLL DLCASFGTDI TVQAVTQAAG
     LAGQSHLFEI ADAAIARDPA AALLVVGRLS EQSCDFSRLC EQMIGHYRNL MIVKTVREAD
     DLVQGTPEDL ERLRTQAGGI SLGAIMYALG VLQDAATSLT RTAFKRTELE MAIVRLCDER
     MGGGLEGVLD RLEKLEKAAR LGAAQAPAAP PAQPEASGAA TAPPKDSAKP VSAAAASKPK
     PAAGVAQVTP FGDWARVLEE LAKINAALRG AMNDSRAFVH GEMMLIDCQN ELFRTLLRTS
     IAAKESLRDA ILAVTGHKYN LGPYNPDKYA PAAAPSDPLE GMLKRASELD VPVELK
//
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