ID K9VRY7_9CYAN Unreviewed; 471 AA.
AC K9VRY7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=Osc7112_6564 {ECO:0000313|EMBL:AFZ10696.1};
OS Oscillatoria nigro-viridis PCC 7112.
OG Plasmid pOSC7112.02 {ECO:0000313|EMBL:AFZ10696.1,
OG ECO:0000313|Proteomes:UP000010478}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ10696.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ10696.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ10696.1,
RC ECO:0000313|Proteomes:UP000010478};
RC PLASMID=pOSC7112.02 {ECO:0000313|EMBL:AFZ10696.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished plasmid 2 of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) 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|RuleBase:RU364063}.
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DR EMBL; CP003616; AFZ10696.1; -; Genomic_DNA.
DR RefSeq; WP_015179669.1; NC_019730.1.
DR AlphaFoldDB; K9VRY7; -.
DR KEGG; oni:Osc7112_6564; -.
DR PATRIC; fig|179408.3.peg.7855; -.
DR HOGENOM; CLU_006229_0_8_3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000010478; Plasmid pOSC7112.02.
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 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; 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 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 Plasmid {ECO:0000313|EMBL:AFZ10696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 36..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 471 AA; 51224 MW; 27FC661B6AA67D42 CRC64;
MYQPLHLKYR PKNLQELVGQ DTIKTTLTNA ITSDKIAQAY LFTGPRGTGK TSTARILAKS
LNCLNSKKPT ATPCGECSSC KTIDSCSSLD VTEIDAASHN GVDDARELIQ HSNFAPALSR
YRIWILDECH QLSTSAQNAL LKCLEEPPAH VVFILCTTEA HKVLPTIISR CQTFNFRALS
VDAIVGQLHK ISSAESIEIA SEAMRAIART CDGGLRDALQ LLSQLSLLNS EITLTQVAEV
SGSISEQDSI ALLKAIHSGD TLSVLQSSRT LIDSGKTPKL ILSSLLAAMR DLLIVKSTRH
CQNLIAGPVG YSQLRSLALH LDFETIDAAC TQLQKSEFQL RTSTNAATWL EVCLLNLMLS
SKPAAKETRL PATFPSNQPD NFDKTPPKIE ADSPDFETTW AQVVAAAKPG NRSLLNRAQI
AELSADSCVL AVERKYANKF QSHLESVQRI VTKALGRSVT VTVKQQEELA A
//
