ID A0A2L2BSN9_9MICO Unreviewed; 694 AA.
AC A0A2L2BSN9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=C3B54_111731 {ECO:0000313|EMBL:AVG24660.1};
OS Pontimonas salivibrio.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pontimonas.
OX NCBI_TaxID=1159327 {ECO:0000313|EMBL:AVG24660.1, ECO:0000313|Proteomes:UP000243077};
RN [1] {ECO:0000313|EMBL:AVG24660.1, ECO:0000313|Proteomes:UP000243077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-TW6 {ECO:0000313|EMBL:AVG24660.1,
RC ECO:0000313|Proteomes:UP000243077};
RA Cho B.C., Hardies S.C., Jang G.I., Hwang C.Y.;
RT "Complete genome of the streamlined marine actinobacterium Pontimonas
RT salivibrio CL-TW6 adapted to coastal planktonic lifestype.";
RL Submitted (FEB-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}.
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DR EMBL; CP026923; AVG24660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2BSN9; -.
DR KEGG; psai:C3B54_111731; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000243077; 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; 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 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:UP000243077};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 35..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 372..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 73037 MW; D1252F757C7517F8 CRC64;
MAALYRRYRP ETFQEVIGQI HVTGPLRHAL TSDRSHHAYL FSGPRGCGKT TSARILARCL
NCAKGPTDTP CGECPSCVEL SRDGGGSLDV VEIDAASHNG VDDARELRER AVFAPARDRY
KIYILDEAHM VTQQGFNALL KIVEEPPEHV KFIFATTDPD KVLPTIRSRT HHYPFRLVVP
AELLAYLQQV SESEGVTIEE GVLALVVRSG GGSVRDSLSL LDQLIAGSSD QAITLEGAQA
LLGYTPRVLL DEVVAAFASK DAPVAFQSLD SVMQSGQDPR RFVEDLLAHI RDIIVIQATG
TEAHELFPGV SQGDLGIWQE QASWFSPAQL ASMGREISDT LQHMSGVTAP RLQLELMVAK
LLVRADASVN GSAGRSVDVP AATPADRPAS ATNQPADQKA STAAPEAGPG SGPGPEHSST
APSVPEASIE PPTSDVASEE VFATPVEPLA EWTLEAVVER WSGIVETVGE QKRSLWVVLS
ETTPVALNAD VLTVGFAKRS DAEILKKPQG PGSPLPNADL LRDAIYQHTG HRVRFTIAEL
EPHQVPTPGA NATSQWPVVS KPGSDSSGSG DSGGNSDETA GVAASESETS AHASPAVSEE
DSMATTEGAG SAPENTEPAS LVEESPEEPG AESAEADSKS DPTASASATS QNAKGSSGPP
LATRGEPVLR QVLGGELIGE EILSEMSGQG EADV
//
