ID A0A1Q9JHQ5_9FIRM Unreviewed; 619 AA.
AC A0A1Q9JHQ5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BHK98_06415 {ECO:0000313|EMBL:OLR55730.1};
OS Hornefia porci.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR55730.1, ECO:0000313|Proteomes:UP000187404};
RN [1] {ECO:0000313|EMBL:OLR55730.1, ECO:0000313|Proteomes:UP000187404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-3-10 {ECO:0000313|EMBL:OLR55730.1,
RC ECO:0000313|Proteomes:UP000187404};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR55730.1}.
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DR EMBL; MJIE01000001; OLR55730.1; -; Genomic_DNA.
DR RefSeq; WP_075712721.1; NZ_MJIE01000001.1.
DR AlphaFoldDB; A0A1Q9JHQ5; -.
DR STRING; 1261640.BHK98_06415; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000187404; 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 Reference proteome {ECO:0000313|Proteomes:UP000187404};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 93..244
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 67753 MW; F015FDFBB8848F35 CRC64;
MRLCDSTPAR QGEPCCGHPR RAESRGGSAG ENAGAGGQRG ERAGLYFVQK KKEGVMKQYL
ALYRENRPET FSQVLGQEHI VKILRHQIAT DTVAHAYLFC GTRGTGKTTM ARILAKAVNC
TGESGEKPCG VCDTCRDIAA GRYVDVVEID AASNNGVENV RDLRESVNYP PVVGRKKVYI
IDEVHMMSTN AFNAFLKTLE EPPADVIFIL ATTDPEKLPP TILSRCMRLD FKRVSGREIR
ENMRRICAAH GVEITEDALA LLAMNADGSV RDSLSLLEQC MSSGEPLLDR DVVLEFLGAA
SVEFYADLTE RALEHDVAGA LLLLEEALQE GKDIRQLMRG WMEHYRSLLI AKFVKEPQDM
LNMSLENIDL LKQQAGRIRL EALNRNIVTL ARTISDARYS TQARILMEVA IVTIAEDMEY
AGRAGTQTGG AAAQPRRAAE AGRTSGGAAA GHDMRSRGTK TGSPGRSASP RAPRQETPAA
ENSRLPKSAA ETAVGAGQAA ESVNTPAPVD SSDGLDEIWR DVCEADGLDQ LSAGATMRGA
RLAAMNDREF KLIVTGDMVR RMLERNSEQI CDLMEQRTGR RRKMVVREMN QTENRSKDER
LQQAASEAAS ILGTKVDIR
//