ID Q1NAS7_SPHSS Unreviewed; 538 AA.
AC Q1NAS7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=SKA58_07990 {ECO:0000313|EMBL:EAT08141.1};
OS Sphingomonas sp. (strain SKA58).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT08141.1, ECO:0000313|Proteomes:UP000005395};
RN [1] {ECO:0000313|EMBL:EAT08141.1, ECO:0000313|Proteomes:UP000005395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT08141.1,
RC ECO:0000313|Proteomes:UP000005395};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) 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}.
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:EAT08141.1}.
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DR EMBL; AAQG01000012; EAT08141.1; -; Genomic_DNA.
DR RefSeq; WP_009821368.1; NZ_CH959306.1.
DR AlphaFoldDB; Q1NAS7; -.
DR STRING; 314266.SKA58_07990; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_7_5; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000005395; 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; 3.40.50.300; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000005395};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 42..189
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 390..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 57890 MW; 4FB63F1E1F3E8BD5 CRC64;
MSDSPQPYRV LARKYRPRSF SELIGQDAMV QTLGNAIRRG RLAHAFLMTG VRGVGKTSTA
RLIAKALNCV GPDGQGGPTI DPCGQCEPCK AIAEGRHIDV VEMDAASHTG VDDVREIIEA
VRYAAVSARY KIYIIDEVHM LSKNAFNALL KTLEEPPAHV KFLFATTEVN KVPVTVLSRC
QRFDLRRIPA ELLATHFTHV VEAESVAAEP EALALIAQAA EGSARDGLSI LDQAIAHAEM
DDGPSLVTAA QVREMLGLSD RGSVRRLLAL LLEGETASLI AAVREQYALG VEPLALMRGL
MELVHAVTLM KAGRDIASPG QPAEEREMLA DWAAQLGFAP LHRLWQLLLK GHDEVANAVL
PIESCEMALL RVMHAATMPD PAEVARLLRE GGASSSASTE GSSAGAASSA PASARLPATY
ADLIEAFWQG GKGQLAQELH DCVGVIRYAP PQFDYRPTPQ LPADFLARLL PALREVTGTA
WQVAAGEGPA EPTLLEQEQR QAADTRARIL ETPVVKAAMA AFPDAELDDR LERWSAEA
//
