ID A0A2P6F9X2_9MOLU Unreviewed; 691 AA.
AC A0A2P6F9X2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PQM30252.1};
GN Synonyms=dnaX {ECO:0000256|RuleBase:RU364063};
GN ORFNames=SMSRO_SF000080 {ECO:0000313|EMBL:PQM30252.1};
OS Spiroplasma poulsonii.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2138 {ECO:0000313|EMBL:PQM30252.1, ECO:0000313|Proteomes:UP000031565};
RN [1] {ECO:0000313|EMBL:PQM30252.1, ECO:0000313|Proteomes:UP000031565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSRO {ECO:0000313|EMBL:PQM30252.1,
RC ECO:0000313|Proteomes:UP000031565};
RX PubMed=25827421;
RA Paredes J.C., Herren J.K., Schupfer F., Marin R., Claverol S., Kuo C.H.,
RA Lemaitre B., Beven L.;
RT "Genome sequence of the Drosophila melanogaster male-killing Spiroplasma
RT strain MSRO endosymbiont.";
RL MBio 6:e02437-e02414(2015).
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:PQM30252.1}.
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DR EMBL; JTLV02000001; PQM30252.1; -; Genomic_DNA.
DR RefSeq; WP_040092404.1; NZ_PETG01000001.1.
DR AlphaFoldDB; A0A2P6F9X2; -.
DR STRING; 2138.SMSRO_v1c00070; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000031565; 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 ECO:0000313|EMBL:PQM30252.1};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:PQM30252.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 691 AA; 79343 MW; 8BBDF9AC94768761 CRC64;
MDYISLYRKY RPNIFDKIVG QVEIRKALKN AINNNNFSHA YLFSGPRGTG KTSIAKIFAK
AINCTNLNDG SPCNTCPSCN EINRGGAVDV FEIDAASNNG VDEIREIRNN VQLLPTMAKY
KVYIIDEIHM LTNSAFNALL KTLEEPPQHV VFILATTESH KIPATIISRC QQYNFRKIPK
VELENNIIEI LQKEEIKYDL VAIKEIAILA DGSARDSLSI LEQVIMFSDR NITLENVNII
FATVSKNIKL KLLKDILEFK TEAVLLTSKK IYEAGSDFEI LTLNLLDILK EVFEYKQTGN
LVFLNLLSEN QAKIFAAKLT VEELLTLLDL FTEASTKMRS SRTQEMYFEL ILLKALSMFE
RNVKSLDDLE LSDLTIVTKT EKNKDNKVDN SDIITKNIEI MENNSVYNEE NIEAVSNLQQ
VEEKNAEHLE LGTEKKIPNS EPLFRNFSLF DDEESNNVSL SQPLTTTSEK VTDDVVSEFD
VSKGSQQESS FPTELEQTPH GKELEGITDL QKYRDDMKNK INIYELSNIN YSINQIFNIL
IKANKEDREK FESKFMELIN EKGKVVQLDK LISFYDVKYA AASEQGLIIV TNTKPEANWI
SFEMCDWEFR NKIFHAFDFD FIIIALSESE WNNVRDDYAK IRQANKLPEV MLTDVEEFYQ
NLLVKQIDNY DDHKELLETG KQIFDNIKII D
//
