ID A0A167HU96_9FLAO Unreviewed; 620 AA.
AC A0A167HU96;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ULVI_10360 {ECO:0000313|EMBL:OAB78968.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB78968.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB78968.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB78968.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-2016) 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:OAB78968.1}.
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DR EMBL; LRXL01000037; OAB78968.1; -; Genomic_DNA.
DR RefSeq; WP_068592476.1; NZ_LRXL01000037.1.
DR AlphaFoldDB; A0A167HU96; -.
DR STRING; 1763537.ULVI_10360; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000077013; 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; 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; 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 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:UP000077013};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 380..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70179 MW; 08A5CABBE523549B CRC64;
MEHFIVSARK YRPTVFKDVV GQQAITNTLE NAIKNDHLAQ ALLFTGPRGV GKTTCARILA
KKINQDGTEK EDEDFAFNIF ELDAASNNSV DDIRNLIDQV RIPPQVGNYK VYIIDEVHML
SSAAFNAFLK TLEEPPKHAI FILATTEKHK IIPTILSRCQ IFDFRRITVQ DIKGHLAEVA
RSEGIEAEDD ALHVIAQKAD GALRDALSIF DRVVSFSGKT MTREAVTENL NVLDYTYYFK
ITDLLLSNNI PQVLIAYNEI LAKGFDGHHF IMGIASHFRD LLVCKNQETI SLLEVGEQVK
TMYFEQSQKT STEFLLEAIQ IANSCDLTYK NSRNQRLLVE LCLLQLASLT AKGEKKNSNS
FLLAGKDRFV LPPSHFKKQA TEPVFSETTS ENQVNNSTSE IKLDGPSEAS LNNNASQSTE
TIQKTEDATI EEASESSNVA MVSTFKKPSE EKKEKVIDRP QLLAERNAKK VSGLSLKSIQ
KKKELQEELV AKQPDQKNLP TKEFTEEAMI ATWNEYTKKV ESDGKYNLLS HLTMGVPRLE
GSLIHLEFPN QTIKTEVERA KYDLLGFIRE QLENYDIDLS IEVNETAVKR YAYTPIEKFQ
KLKEKNPLIE QLRKEFDLDI
//