ID A0A1M4V3Q8_9FIRM Unreviewed; 507 AA.
AC A0A1M4V3Q8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN02746064_00908 {ECO:0000313|EMBL:SHE63616.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHE63616.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHE63616.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHE63616.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQTU01000004; SHE63616.1; -; Genomic_DNA.
DR RefSeq; WP_073269891.1; NZ_FQTU01000004.1.
DR AlphaFoldDB; A0A1M4V3Q8; -.
DR STRING; 1120975.SAMN02746064_00908; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000184251; 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; IPR012763; DNA_pol_III_sug/sutau_N.
DR InterPro; IPR048448; DnaX-like_C.
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; PF20964; DnaX_C; 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:UP000184251};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 370..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 56971 MW; 0508BA99E9CABB53 CRC64;
MEYVALYRKY RPKRFEDMIG QENVVSILKN QITMDKIAHA YLFSGTRGTG KTSAAKIFAR
AVNCPESETG EPCNNCKTCA DLETSSVMDI IEIDAASNRG VDEIRDLRDK VKYMPAVGRY
KVYIIDEVHM LTMEAFNALL KTLEEPPAHA IFILATTEPN KLPATILSRC QRFNFRRLTS
EEIIGRMAYI CKDTQIEIED AALKLIARNA DGAMRDALSI LDQCMSISKD DLIEYEEVKS
ILGITDNEIV YSMIEAVLDR DVKRALDNLD NAYNAGKEMV QLIHQLISGF RDVLIYGITK
NTNMLIEIKD ESSGLLAGSS METMERISSI IDVLTDRENK LKFTALPKIL MEVTLVRLCT
MEESTIKASS TQVEKPARQA PVAREQEAGY VRKDPQAHEK ISDGPKPGKD ADFASVVKYI
SKDKKVLGMS LGVGKAKADG DKIIIRYNQG DEFHSQKVEE EKAYIESTAK KILGRDVKIS
IQVKTRDDYL VNKLPLDLFG EDKVEFK
//
