ID A0A3B0MJY2_9RHOB Unreviewed; 576 AA.
AC A0A3B0MJY2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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_1 {ECO:0000313|EMBL:SUZ31387.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=ROE7235_01128 {ECO:0000313|EMBL:SUZ31387.1};
OS Roseibaca ekhonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=254356 {ECO:0000313|EMBL:SUZ31387.1, ECO:0000313|Proteomes:UP000272908};
RN [1] {ECO:0000313|Proteomes:UP000272908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7235 {ECO:0000313|Proteomes:UP000272908};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (AUG-2018) 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; UIHC01000008; SUZ31387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0MJY2; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000272908; 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 ECO:0000313|EMBL:SUZ31387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272908};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:SUZ31387.1}.
FT DOMAIN 39..186
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 380..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 61949 MW; 7FCC8C79827609D0 CRC64;
MSEQYQVLAR KYRPESFADL IGQDAMVRTL RNAFAADRIH HAFIMTGIRG TGKTTTARII
AKGLNCIGAD GQGGPTTEPC GVCEHCRAII EGRHVDVMEM DAASRTGVGD IREIIDSVAY
RAASARYKIY IIDEVHMLSN NAFNALLKTL EEPPAHVKFI FATTEIRKVP VTVLSRCQRF
DLRRIEPEVM IAHLEKVAKA EGGQVAADAL ALITRAAEGS VRDAMSLLDQ AISHGAGETT
ADQVRAMLGL ADRARVLDLF DHIMRGDAAA ALSELAGQYA DGADPMAVLR DLAEITHWLS
VTQITPDAGA DPTISPEERD RGAAMAQALP MRVLTRTWQM LLKALEEVAA APNAMMAAEM
AIIRLTHMAD LPSPEEILRK WHDQTPPTGG SGAPAPRAPI SGGAAPRALS AGSAHGPQAA
LAGAAPALSD YPDFASVVAL IRAQRDMTLL VEVETNLRLV RYSPGRIEFQ PTDAAPIDLA
QCLGARLQGW TGARWAVSVA NTGGGATLAE RQAEQQNVDE EKAMQNSLVL AVLEVFPKAR
IAEIRLLTTP EDEAASAALP EVEDEFDPDW DPFEDT
//
