ID B7JZ29_RIPO1 Unreviewed; 648 AA.
AC B7JZ29;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=PCC8801_2074 {ECO:0000313|EMBL:ACK66106.1};
OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS 8801)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK66106.1, ECO:0000313|Proteomes:UP000008204};
RN [1] {ECO:0000313|Proteomes:UP000008204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001287; ACK66106.1; -; Genomic_DNA.
DR RefSeq; WP_012595374.1; NC_011726.1.
DR AlphaFoldDB; B7JZ29; -.
DR STRING; 41431.PCC8801_2074; -.
DR KEGG; cyp:PCC8801_2074; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_2_2_3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000008204; 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 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 PRINTS; PR01217; PRICHEXTENSN.
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:ACK66106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008204};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ACK66106.1}.
FT DOMAIN 38..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 372..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70931 MW; ECB040FB356399D4 CRC64;
MSSYEPLHHK YRPQTFADLV GQEAIATTLT NAIAAKRIAP AYLFTGPRGT GKTSSARILA
KSLNCLAFSD PTATPCGKCE VCRAITRGSA LDVIEIDAAS NTGVDNIREI IERAQFAPVQ
CRYKVYVIDE CHMLSVAAFN ALLKTLEEPP DRVIFVLATT DPQRVLPTII SRCQRFDYRR
IPLAAMVSHL GKIAQQETID IAQDALILVA QIANGGLRDA ESLLDQLSLL SGTITTDKVW
ELVGAVPEQD LLLLLQAIAS NNAELVIDRC RHLMNRGREP LVVLQNLAGF YLNLLIAKTA
PNRPDMVAVT APTWQALCNE AHQWNLETIL QGQQRLKDSE FQLKNTTQPR LWLEVTLLSL
LPSAFMKSEV TSQKSEVIPT PTPPLTPSPP PSPSPHPSPP PLTPSPPLSQ NPVINDVNGI
WPAILAKLQP FSQGLVNSHC YFLNLEESAA YIGVRSQGLL KLVQGKIPDL EAAFAAVCQR
PIKVHLKVAS PSSNAVSTSP QPVNPSPSPV PISNSETEKP VIAQPVINSD KETISNTPKT
EIKAFSHKQN NLPESEINLK DISENLDDED LKKVAENFAK IFEGEIVDLA PSFNSKIPSL
SVGSEEQKIK HKTQPNSQLS DSIKLDINNS IRVKGRPEII EDEDDLDF
//
