ID A0A3M8G109_9BACT Unreviewed; 603 AA.
AC A0A3M8G109;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:RNC84003.1};
GN ORFNames=ED557_09545 {ECO:0000313|EMBL:RNC84003.1};
OS Balneola sp.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=2024824 {ECO:0000313|EMBL:RNC84003.1, ECO:0000313|Proteomes:UP000280416};
RN [1] {ECO:0000313|EMBL:RNC84003.1, ECO:0000313|Proteomes:UP000280416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin6 {ECO:0000313|EMBL:RNC84003.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-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:RNC84003.1}.
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DR EMBL; RHLJ01000003; RNC84003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8G109; -.
DR Proteomes; UP000280416; 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; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:RNC84003.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280416};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RNC84003.1}.
FT DOMAIN 39..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 407..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 68215 MW; AD378069C30FA387 CRC64;
MSEHYRALTR KYRPNSFEDI VSQDHVSSTL LNAIKQKRLS HAYMFCGPRG VGKTTMARVL
ARVINEIDTS VDGEALNQTL NIIEMDAASN NKVEDVHHLR ESVRIPPQNG RYKVFIVDEV
HMLSKAAFNA LLKTLEEPPE HAIFIFATTE PHKVLPTILS RVQRFDFKRI SVEEIVARLR
KISLDEQIAI DEESLHVIAK KADGALRDAL GLMDQAIAFC GDTITHNELL LALNVVGTDR
LFQFMDCVKE HDANAGLDLI NTLLQEGYDI QEFLIGLTEH LRNLYIAHHS PQLYLVEASD
ETRKKYQATA PGFSRDDLMR MMHIVSEAQI KLKDASQPRV QFEITLLKLI HMERSESLKQ
LLSDLEEVKK KFKSGASSSS SSIKQEAHQQ IIESQKPVQE ALNGIHKEEE APENPIVQEK
PVSYSPKPDE QEPVPVLDEY DLGQPALVTE VTQKAKVLHF KNGNGAIEKK EQSPVPAQET
VVKLTLEKVH EIWSDFLSSL ENNVPKTLEL QVQRVTLSSL SGNELTIECE NAFAAKMMNE
QAHDLCVKLK EHVGTMLRFK TVVKKGEVQK TSSLSNYDRF KEIQQKDPIV RELVTRLGAE
LEF
//
