ID D5ETG0_PRER2 Unreviewed; 601 AA.
AC D5ETG0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ADE82662.1};
GN OrderedLocusNames=PRU_1618 {ECO:0000313|EMBL:ADE82662.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82662.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82662.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
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; CP002006; ADE82662.1; -; Genomic_DNA.
DR RefSeq; WP_013064648.1; NC_014033.1.
DR AlphaFoldDB; D5ETG0; -.
DR STRING; 264731.PRU_1618; -.
DR KEGG; pru:PRU_1618; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_2_10; -.
DR Proteomes; UP000000927; 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; 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; 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 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 ECO:0000313|EMBL:ADE82662.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ADE82662.1}.
FT DOMAIN 37..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 414..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 66788 MW; F1DA81A90E4C5358 CRC64;
MEYIVSARKY RPLSFDTVVG QAALTTTLKN AVKSGKLAHA YLFCGPRGVG KTTCARIFAK
AINCQHPTAE GEACNECESC QSFNEQRSLN IFELDAASNN SVEHIKTLME QTRIPPQLGR
YKVFIIDEVH MLSTAAFNAF LKTLEEPPAH VIFILATTEK HKILPTILSR CQIYDFERMT
IRNTIDHLKH VAEQEGITYE EQALAVIAEK ADGGMRDALS IFDQAASFCQ GNITYEKVIE
DLNVLDSENY FKIIDLAIDN KVSDIMVLLN GVINKGFDGG LLIQGLAKHV RNVLMARDPQ
TLPLLEVSDQ MRARYEEQAK KCQITFLYDA LKLMNQCDIN YRQSSNKRLL VELTLIEIAQ
ITQPAEDGAS AGRKPRRLKS LFKNMIQQQK PKNAAPQVAA AKVAVSAAAA VTAEATGESQ
TAGTTASEAS TTSNAKPKLS LGGIGFSWKK LRQQDNGPQK GGMQIIPGSI NMPTGQDAVT
DAQFTQTDLE FQWMAMCNRM PQKLSGIATR MKNMNPEITE FPTVEVVVDN ELIKQEIEDI
QKSIAKTLQV YLHNNQIQIT VRVAEQTEHV KILSRREQFE QMAEKNAAVA KLQQAFDLEL
A
//
