ID A0A3T1CZA1_9BACL Unreviewed; 596 AA.
AC A0A3T1CZA1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:BBI31085.1};
GN ORFNames=KCTCHS21_04840 {ECO:0000313|EMBL:BBI31085.1};
OS Cohnella abietis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2507935 {ECO:0000313|EMBL:BBI31085.1, ECO:0000313|Proteomes:UP000289856};
RN [1] {ECO:0000313|EMBL:BBI31085.1, ECO:0000313|Proteomes:UP000289856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS21 {ECO:0000313|EMBL:BBI31085.1,
RC ECO:0000313|Proteomes:UP000289856};
RA Jiang L., Kang S.W., Kim S., Jung J., Kim C.Y., Kim D.H., Kim S.W., Lee J.;
RT "Complete genome sequence of Cohnella hallensis HS21 isolated from Korean
RT fir (Abies koreana) rhizospheric soil.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; AP019400; BBI31085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1CZA1; -.
DR KEGG; cohn:KCTCHS21_04840; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000289856; 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; IPR022754; DNA_pol_III_gamma-3.
DR InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR InterPro; IPR048448; DnaX-like_C.
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 Pfam; PF20964; DnaX_C; 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:UP000289856};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64963 MW; 5DEB04D946061D77 CRC64;
MAHLALYRAW RPQTFQDMVG QQHIVQTLQN AIREDRLSHA YLFSGPRGTG KTSAAKILAK
AVNCERGPAL EPCNECSQCE RITSGSVMDV VEIDAASNRG VEEIRDIRDK VKYSPTEVRR
KVYIIDEVHM LTTEAFNALL KTLEEPPGHV MFILATTEPH KLPPTIISRC QRFDFRRVSL
EEQTGRLQEI SDKEQITAEQ EALRYIARLS DGGMRDAVSL LDQISSFTGG QVTLEQAIEA
TGGLPSEQFA RLAMAIRESD AAKVLIEIDE MMKAGKSADK CLEQLMHYFR DLLLAQLAPD
AGDSSGRIAN PAELKEMSKA FSRERLFAII DLLNRYQNEM KYAAHPQTMF EIALLKLCSD
NPSVGAADAT SSNSAADTSH VRGELGQLRQ QLAALESKLG ALASGGFTPA SAGGGSSSQA
AGNRNARGSS PGNGGAGQAP RIAAIPKLKL NAYVEARTSA GQSLAKWPQI LQRVKEERVT
VHAWLVDGEP VSMAENTIVV AFRNTIHRET TERPANKGVI EGVLSSIFGN PTQLLTVMQK
DWQEAVAEST GSPKADSLVG EELLLVPDDE AAGKSEPWID EAVRLFGDQL VTIKDD
//
