ID A0A1X7MQU3_9LACT Unreviewed; 625 AA.
AC A0A1X7MQU3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04488700_0513 {ECO:0000313|EMBL:SMH27190.1};
OS Carnobacterium iners.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1073423 {ECO:0000313|EMBL:SMH27190.1, ECO:0000313|Proteomes:UP000193435};
RN [1] {ECO:0000313|EMBL:SMH27190.1, ECO:0000313|Proteomes:UP000193435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG26642 {ECO:0000313|EMBL:SMH27190.1,
RC ECO:0000313|Proteomes:UP000193435};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXBJ01000002; SMH27190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7MQU3; -.
DR STRING; 1073423.SAMN04488700_0513; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000193435; 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:UP000193435};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 546..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 69993 MW; EDF5759E8FADFF38 CRC64;
MSYQALYRVW RPQKFQDVAG QKAITQTLRN ALIQQKTSHA YLFTGPRGTG KTSGAKIFAK
AINCHYLKDG EPCNECETCR AITKGQLNDV IEIDAASNNG VEEIRDIRDK AKYAPTSADY
KIYIIDEVHM LSTGAFNALL KTLEEPPKNV VFILATTEPH KIPLTIISRT QRFDFKRINV
RDISDRMRYI LTQEKIEFEE AALPIVARAA EGGMRDALSI LDQAISFGDD TVTIEDVMSV
TGSLTQELML TYFEAVVTHD TKKGLFLLQE ILADGKDAAR FVEDLILFSR DLLVYQQAPQ
MSELLDGAKV DAAFKKLSET ISADSLYQMI VILNGTQTEL RFTNHPDVYL EVATVRLTHL
DAITHLSESA TSNEQVLDQK ETSVPSDNKK IIELENELLK IKKQMESILV SGHSKVATKK
TKSVSKKAAN NQFKPNTSAI YSILKEATRE NLAQLKNVWP DLLNMLSVTQ RAMLKASTPV
AAGPSGLIVS FDYDILCQKA TNDSELMEAV KQFLERLIGN APQMIFVPGE QWPIIREQYV
KQLKNRSSDD KAVENTHVGQ VSKPDQSKEQ KGKSFEPVKK QLETVVDTSE WDSLEDFVPP
AQEDDKVVTE AMALFGEKMV EVKND
//
