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Database: UniProt
Entry: A0A1K1MYJ5_RUMFL
LinkDB: A0A1K1MYJ5_RUMFL
Original site: A0A1K1MYJ5_RUMFL 
ID   A0A1K1MYJ5_RUMFL        Unreviewed;       536 AA.
AC   A0A1K1MYJ5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=SAMN02910280_1413 {ECO:0000313|EMBL:SFW27086.1};
OS   Ruminococcus flavefaciens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265 {ECO:0000313|EMBL:SFW27086.1, ECO:0000313|Proteomes:UP000183461};
RN   [1] {ECO:0000313|EMBL:SFW27086.1, ECO:0000313|Proteomes:UP000183461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL228 {ECO:0000313|EMBL:SFW27086.1,
RC   ECO:0000313|Proteomes:UP000183461};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FPIP01000003; SFW27086.1; -; Genomic_DNA.
DR   RefSeq; WP_072299762.1; NZ_FPIP01000003.1.
DR   AlphaFoldDB; A0A1K1MYJ5; -.
DR   Proteomes; UP000183461; 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   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; 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   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   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          36..178
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   536 AA;  59325 MW;  D46F46852E1E155B CRC64;
     MYKALYRKWR PMTFDDVISQ QYTTEALKNQ IISGKTAHAY LFTGSRGTGK TTCARILAKA
     VNCRNMKNGN PCLECDICRD ADSGALTDIV EIDAASNNGV DNIRDLRDAA VYTPERGAYK
     IYIIDEVHML SAGAFNALLK IMEEPPPYVK FILATTEIHK VPATIVSRCQ RYDFRRIKAE
     DIAARISYIA QQEELNLTED GAAMIAKLAD GGMRDAVSLL DQCSVCAEVI NAEAVSNAAG
     IAGRDYLYDM LDAVSDSDTP KALSITADLY DMSKDLTRLC EELITQLRNV MLIKASPDTA
     DKLIVCMPDE LERLKAIAEK SDLPTVMDRL SALQECRERM QRAMNKRVEF EMSLIKLCGN
     VKNTTESIDN SEIYDKIKQL EDKINTVPRA VPAAGKPAEE KPEVLEASAV PADEKIVPTI
     DIKKLKPEDI IPCERWNEVL DEFRNINPAV AGSLDGSFAG TAGNYIFITA QNRFFMELFK
     VKENANSLGA AIANVLGQRF IIKARCATTV AEQKNLAESL IKKAMDSQIE TAVENQ
//
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