ID Q6LTE8_PHOPR Unreviewed; 753 AA.
AC Q6LTE8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=PBPRA1017 {ECO:0000313|EMBL:CAG19428.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG19428.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378666; CAG19428.1; -; Genomic_DNA.
DR RefSeq; WP_011217762.1; NC_006370.1.
DR AlphaFoldDB; Q6LTE8; -.
DR STRING; 298386.PBPRA1017; -.
DR KEGG; ppr:PBPRA1017; -.
DR eggNOG; COG2812; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR Proteomes; UP000000593; Chromosome 1.
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; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR022001; DNA_pol3_tau_IV.
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; PF12168; DNA_pol3_tau_4; 1.
DR Pfam; PF12170; DNA_pol3_tau_5; 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 Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 418..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 82449 MW; D7854B28150420CB CRC64;
MSYQVLARKW RPYQFSDVVG QSHVLTALSN ALTHNRLHHA YLFSGTRGVG KTTIARIFAK
GLNCEQGITA TPCGQCGTCK EIDEGRFVDL LEIDAASRTK VEDTRELLDN VQYKPARGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPEYV KFILATTDPQ KLPVTILSRC LQFHLKHLDN
DQIQSQLSNV LTQENVDFEP KALSLLSRAA EGSMRDALSL TDQAIALGNG QVHADSVSMM
LGTLNTDQAL FLLEAVSGGQ ANTAMGGLEE LASVGVEWDS LLRELAAQLH RVAMHQALPA
ALDMSAPDAD RIITLSSVMT PQDVQLCYQI ALQGRQDLAF APDGRIGLEM VLLRMLAFRP
VSGSGITPQS INVPASEPAA PQQGMQRVQA LKAQMGSQPQ AATSQVTIPQ VVAPHAVAPQ
HSDQQLAASP SSIQESAGTV PAEQQYQQHQ QVPTSQEAFR QEPSRQEPTP PPAQYQQQAP
HSEQSAAPQN IPPAQPRSAA SGLLAARNKL RSQSKRGNEE QPVKKGEPAP AKKVAMNVLD
RIANKHAGMR VPTTGNTATN SAMPASMIAT QANGTQANVP EKKDEYQWKP MQPVAPEEDT
KLEVAPRKLK QALEHEKTPE MAKLLVNEAA NQDSWSDLVT KLNVGRLVQQ LALNSAFEQD
NNQVTLYLRQ SQSHLDNPKA REQLAQAIGE LQSVDIDLKI ELSGKGQTPL EWREGLYQQK
LGQAKESLES DANVTFIRQR FAAVLDEDSI RPL
//
