ID I1YFV1_METFJ Unreviewed; 570 AA.
AC I1YFV1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
DE Flags: Precursor;
GN Name=dnaX {ECO:0000256|RuleBase:RU364063};
GN OrderedLocusNames=Q7C_623 {ECO:0000313|EMBL:AFJ01794.1};
OS Methylophaga frappieri (strain ATCC BAA-2434 / DSM 25690 / JAM7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754477 {ECO:0000313|EMBL:AFJ01794.1, ECO:0000313|Proteomes:UP000009145};
RN [1] {ECO:0000313|EMBL:AFJ01794.1, ECO:0000313|Proteomes:UP000009145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM7 {ECO:0000313|EMBL:AFJ01794.1,
RC ECO:0000313|Proteomes:UP000009145};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003380; AFJ01794.1; -; Genomic_DNA.
DR RefSeq; WP_014703216.1; NC_017856.1.
DR AlphaFoldDB; I1YFV1; -.
DR STRING; 754477.Q7C_623; -.
DR KEGG; mec:Q7C_623; -.
DR PATRIC; fig|754477.3.peg.615; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000009145; Chromosome.
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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
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; PF12170; DNA_pol3_tau_5; 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 ECO:0000313|EMBL:AFJ01794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009145};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:AFJ01794.1}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 570 AA; 62627 MW; EEE5A36DBDA422E0 CRC64;
MSYLVLARKW RPTSFAEVVG QQHVLQALIN GLTQNRLHHA FLFAGTRGVG KTTLARILAK
SLNCETGVTA TPCGQCSACV EVDSGRFVDL IEVDAASRTK VDDTRELLDN VQYAPSRGRY
KVYLIDEVHM LSTSSFNALL KTLEEPPAHV KFLFATTDPQ KLPVTILSRC LQFNLRRLTL
AQISDHLGYI LTQENIPFES AALKQLAQAA DGSMRDALSL LDQAIGFGDG EVRNEAVERM
LGNISGTQLM ALLSALAEHN SSQLLSQVAE LNALGREATA ILDGLMQLLQ QMAILQAVPE
HQLEDATTQP FLSALANQLS PETVQLMYQI ALHGKRDLPY APTPQSGLEM TLIRMLHFQP
DHTSDSLQPI ANQTMEMPPK KPQAKPDPVS EQTRAAAATV EHDTDSAPVK NNAANLVSDS
KITTPETQQI QADPVSDTNA TVDAKNWTQL IAELKLSALT RQLADNCAFI RSEENIIYLQ
LAPELAHLAT DNAQKRLAAA INKQLDKTLT LRFENQVDSS VPQTLAAERA QDMADRQQHA
ETAIQNDPTV EMLKNTFNAR IIDQTIKPLK
//
