ID A0A078LRM6_9PSED Unreviewed; 668 AA.
AC A0A078LRM6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ECO:0000313|EMBL:CDZ93910.1};
GN ORFNames=BN1079_01215 {ECO:0000313|EMBL:CDZ93910.1};
OS Pseudomonas saudiphocaensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ93910.1, ECO:0000313|Proteomes:UP000053902};
RN [1] {ECO:0000313|EMBL:CDZ93910.1, ECO:0000313|Proteomes:UP000053902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ93910.1,
RC ECO:0000313|Proteomes:UP000053902};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) 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|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR EMBL; CCSF01000001; CDZ93910.1; -; Genomic_DNA.
DR RefSeq; WP_037023001.1; NZ_CCSF01000001.1.
DR AlphaFoldDB; A0A078LRM6; -.
DR STRING; 1499686.BN1079_01215; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000053902; 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; 3.30.300.150; 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 Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72344 MW; 8410BC0CE34DD4BA CRC64;
MSYQVLARKW RPRSFGEMVG QTHVLKALIN ALDSQRLHHA YLFTGTRGVG KTTIARIIAK
CLNCETGVSS TPCGQCSVCR EIDEGRFVDL IEVDAASRTK VEDTRELLDN VQYAPSRGRF
KVYLIDEVHM LSSHSFNALL KTLEEPPPHV KFLLATTDPQ KLPVTILSRC LQFSLKNMPP
ERVVEHLTHV LSVENVPFEE DALWLLGRAA DGSMRDAMSL TDQAIAFGEG KVLAEDVRSM
LGTLDHGQVY GVLQALLEGD ARALLEAVRH LAEQGPDWGG VLAEILNVLH RVAIAQALPE
AVDNGQGDRD RVLALAQALP AEDVQFYYQV GLIGRRDLPL APDPRSGFEM VLLRMLAFRP
AGSENTPRTP LKIEGISPAT TDPQAAPVAA TKVAAAPVAP AAVAEPASIA AEPEVSPQPV
VEAISEPAPI EPAAPAQAPV VEKPADQPAS AAVPVDLPWE ERPDPPVSEP LAESAPTEVA
SEPVAVVAPV EDVDDDEPPL SDEDYFEVET QAEAYLHTLD ALEPAPAEVE PALAMAPATG
LAAEWQSIYL KLGLSGLTGS IASNCTLVSV EDDCWVMHLD PAQSALFNAT QQRRLNEALD
QYHGRPLKLV IELQKPEQET PAQAAARYRA QRQQAAEQSI QSDPLVQQLM QQFAAVIREG
TIEPLEQP
//
