ID A0A0F7KT09_9SPHN Unreviewed; 600 AA.
AC A0A0F7KT09;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_2 {ECO:0000313|EMBL:AKH41915.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=WYH_00864 {ECO:0000313|EMBL:AKH41915.1};
OS Croceibacterium atlanticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH41915.1, ECO:0000313|Proteomes:UP000034392};
RN [1] {ECO:0000313|EMBL:AKH41915.1, ECO:0000313|Proteomes:UP000034392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH41915.1,
RC ECO:0000313|Proteomes:UP000034392};
RA Wu Y.-H., Cheng H., Wu X.-W.;
RT "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL Submitted (MAY-2015) 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; CP011452; AKH41915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7KT09; -.
DR STRING; 1267766.WYH_00864; -.
DR KEGG; aay:WYH_00864; -.
DR PATRIC; fig|1267766.3.peg.871; -.
DR Proteomes; UP000034392; 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 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; IPR022107; DNA_pol_III_gamma/tau_C.
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 Pfam; PF12362; DUF3646; 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 ECO:0000313|EMBL:AKH41915.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034392};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:AKH41915.1}.
FT DOMAIN 97..244
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 65149 MW; 7E5A401BB509FB74 CRC64;
MSGETPPWDE GEEEQPSAAE LEAAGQSAMF GDAPQPPVPA PTPAPVSEQP QMDAPPTDAA
QPYRVLARKY RPQTFSELIG QDAMVTTLAH AIQRDRLAHA FLMTGVRGVG KTSTARLIAK
ALNCVGPDGQ GGPTIDPCGV CEPCRAIAEG RHIDVIEMDA ASHTGVDDVR EIIEAVRYSA
VSARYKIYII DEVHMLSRNA FNALLKTLEE PPAHVKFLFA TTEVDKLPVT VLSRTQRFDL
RRIPTPMLKE HFAGICRKER VDAQDEALAM VAAAAEGSVR DGLSILDQAI AHADLETGSD
EKALVTADRV RDMLGLADKS AQRRLFDALL NGDPQAMLAD VDRQYSLGVE PLALLRGMME
LTHRIAITQV SNSPSESVTE EERQAVEEWA GRLSAGQVHR LWQLLLKGHD EVRSAPDPLV
AAQMALLRVL HAADMPDPGR LAKQLQDIAA NGVASAPAAT GEGGAAPVAQ GPRMDWRELC
DRVDQAGRLL VASTMRDWIR VIELAPGRLI FSLRPGLAED PVSGIRDALY EVTGQRWQVE
RGEGEGAPSL REQEDAARQA EADRIRKSPL VEAALAAFPG AEFVEEDEAP RGDRNWSRRA
//
