ID A0A316U2X3_9BACT Unreviewed; 637 AA.
AC A0A316U2X3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DDZ15_01230 {ECO:0000313|EMBL:PWN07676.1};
OS Rhodohalobacter mucosus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2079485 {ECO:0000313|EMBL:PWN07676.1, ECO:0000313|Proteomes:UP000245533};
RN [1] {ECO:0000313|EMBL:PWN07676.1, ECO:0000313|Proteomes:UP000245533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8A47 {ECO:0000313|EMBL:PWN07676.1,
RC ECO:0000313|Proteomes:UP000245533};
RA Liu Z.-W.;
RT "Rhodohalobacter halophilus gen. nov., sp. nov., a moderately halophilic
RT member of the family Balneolaceae.";
RL Submitted (MAY-2018) 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:PWN07676.1}.
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DR EMBL; QGGB01000002; PWN07676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316U2X3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000245533; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000245533};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 39..171
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 372..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71791 MW; FD03B30497C0F222 CRC64;
MAQHYRALTR TYRPQTFDDI VSQEHVTSTL KNAIRQKRIS HAYMFCGPRG VGKTTMARVL
ARAVNEIPEN VDGEALNQTL NIVEMDAASN RKIEDVRQLK DVIRVPPQSG NYKIFIIDEV
HMLTKEAFNA LLKTLEEPPA HAIFIFATTE PHKVLPTILS RVQRFDFKRI SVDEIVSRLK
NISEKEDISI DEESLHIIAK KADGALRDAL GLMDQAIAFC GTTIHYDELL KALNVIGHDS
LFEFTQAVEK RDTAEGLRLI DQLMKEGADI QEYLVSLTEH IRNLYVASQG NQMHLVEATP
DTKQRYKEGA KPFSEEDLMR MLHMVSEAQV KIKDVQQPRV HFEILMLKMI HMGRTPELRK
ILQGLDDIKK NGASHSHSVN GSILPQNREQ EKATANDHGN AAQSEPNPEP ARKQSPSSGD
ETAGESSYES IKPQVNGDAE SEEEPPADTD SSEYVKSGLP SSPNPEESDS VSDNDFLMVK
PSLGYAQGIS SASVSEQGDA TSVAEQTEDD KDLRHTISGI GDVEKHWKQF LNNIKENAPQ
MLYFQLLRVE IKELKGTDLI VSADNEFATR LLEENQQMLS SMFREVSGTF LRMKCIVERS
EKKKSESLSP YERFKELQKK DPNLRTIVEL FGAELEY
//
