ID K0D8J2_LEUCJ Unreviewed; 588 AA.
AC K0D8J2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 OrderedLocusNames=C270_01145 {ECO:0000313|EMBL:AFT81148.1};
OS Leuconostoc carnosum (strain JB16).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT81148.1, ECO:0000313|Proteomes:UP000006299};
RN [1] {ECO:0000313|EMBL:AFT81148.1, ECO:0000313|Proteomes:UP000006299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB16 {ECO:0000313|EMBL:AFT81148.1,
RC ECO:0000313|Proteomes:UP000006299};
RX PubMed=23144413; DOI=10.1128/JB.01805-12;
RA Jung J.Y., Lee S.H., Jeon C.O.;
RT "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT from Kimchi.";
RL J. Bacteriol. 194:6672-6673(2012).
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; CP003851; AFT81148.1; -; Genomic_DNA.
DR RefSeq; WP_014973762.1; NC_018673.1.
DR AlphaFoldDB; K0D8J2; -.
DR STRING; 1229758.C270_01145; -.
DR GeneID; 61186813; -.
DR KEGG; lcn:C270_01145; -.
DR PATRIC; fig|1229758.3.peg.227; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_3_9; -.
DR Proteomes; UP000006299; 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; 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 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:AFT81148.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006299};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:AFT81148.1}.
FT DOMAIN 37..166
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 369..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 64806 MW; 484D7B42801B6186 CRC64;
MAYQALYRVY RPRTFDDMVG QEVITQTLKN AIETHQTGHA YLFSGPRGTG KTSAAKIFAR
EVNGIDAATD DSQIPDIIEF DAASNSRVED IRDILTNVDY APLEAAFKIY IIDEVHMLSN
SAFNALLKTL EEPPVNVKFI LATTEPQKVP VTILSRTQRF EFKRIGSSTI QKRLAEILTK
QNVKYEEGAL RIIANVAEGG MRDALSILDQ VIAFGADIVT IDNALQVTGS TTTKRLLTYL
QQVSGFDTQA SLKTLHDILL EGKDAQRFVA DVLGLLRDVM LADVAPELIK STIALTELQA
LTQQLGTSRI QKMMMTLDDI QKQLMQTMQS DIYLELLTVK LSMNPTQSST IDNEPIPSSH
QAVKEVQQVD RKPEQQVEKV STTSSADKRT VSEEKISEPV PINDNSNGNV QTQTSSQKLI
ARTGQQAVFA VLKSAKRESL TRIKENWATL IGQFDVTQQA MLTIAEPVAA SDEAVVLAFD
YPALLVQALQ DTTLQSQLNS ALRDQSLPAE MVLISQDDWH QERAAYVKQL KAGTVPDVKL
ADVARVSGPL QKEATLSDVK LSDKITSEPT IVAEAKKLFG DDIVTVVD
//
