ID F3LEM1_9GAMM Unreviewed; 740 AA.
AC F3LEM1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=IMCC1989_2508 {ECO:0000313|EMBL:EGG94663.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG94663.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG94663.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG94663.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(2011).
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:EGG94663.1}.
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DR EMBL; AEVK01000064; EGG94663.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LEM1; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000010300; 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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
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; PF12170; DNA_pol3_tau_5; 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:UP000010300};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 433..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 81537 MW; DDBD8CBB52E32073 CRC64;
MSYQVLARKW RPRTFREMVG QEHVLQALIN ALDHDRLHHA YLFTGTRGVG KTTIARILAK
CLNCEVGVSS VPCNECSSCI EINEGRFVDL IEVDAASRTK VEDTRELLEN VQYAPTRGRY
KVYLIDEVHM LSNSSFNALL KTLEEPPPHV KFLLATTDPQ KLPVTILSRC LQFNLKNMNP
EKIVSHLQFV LEKEMVPFED AGLWQLARSA DGSMRDALSL TDQSIAFGDG KITDVDVRTM
LGTIDQSLVY DVLKGLIAED IKQLLSAVAN LSEHSPDYSA ALAELIATLH RIAIAQALPE
AVDNSQGDRQ QIYEFAQAIT AEDIQLYYQT ALLGRRDLPL VPDPRSGFEM VLLRMLAFKP
QGVNHLPKAT LSANAAISDT AIATPVEADK APVEIAPEAI VETVVENIAE ATSEAVSETV
SEAPTVAAVA ENQVSDPVSQ PMVESSQEVL SEPESETTVS VPTANTEDNH SASQTEHHDS
AIPSEYEAFA NMPNTEEDPS VKKSDAATEV AVDTEENAGA IKDEPYLSPA LAAFDAPVIE
DSISDNTEEN HSERNRTEKI HTEKERVDES IETATESVVE AAVETSEETV EQTAANDSAA
TVKKRIPKIP FNELNASTWF TVYNGIDTGG LLQSTVANCA LINWESLHLQ FILDHQQSTL
YDTKHQQYLA DLLTEYFGHP IEATITLGDV PYETPSQIVI RQRQERQIQA EEAIANDPVV
QQLQEMFDGK VVPESIKPID
//
