ID C5BCZ8_EDWI9 Unreviewed; 652 AA.
AC C5BCZ8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=NT01EI_1108 {ECO:0000313|EMBL:ACR68319.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR68319.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR68319.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR68319.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
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; CP001600; ACR68319.1; -; Genomic_DNA.
DR RefSeq; WP_015870498.1; NC_012779.2.
DR AlphaFoldDB; C5BCZ8; -.
DR STRING; 67780.B6E78_15905; -.
DR GeneID; 69538141; -.
DR KEGG; eic:NT01EI_1108; -.
DR PATRIC; fig|634503.3.peg.1006; -.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000001485; 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 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; 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 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:ACR68319.1};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ACR68319.1}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 425..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 71473 MW; E8F22F1A95FC3A2D CRC64;
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK
GLNCETGITA TPCGVCDNCR EIEQGRFVDL LEIDAASRTK VEDTRDLLDN VQYAPARGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPPHV KFLLATTDPQ KLPVTILSRC LQFHLRALDH
EQIRAQLEKI AHAEALTAEP RALQLLARAA EGSMRDALSL MDQAIAMGQG QITADTVSQM
LGTLDDEQPL ALIEALTAAD GALVMARVEQ AAGRGVDWEN LLVEMLALLH RVAMLQLLPS
ALDSQFAAVE PRLRELARML PPADLQLFYQ IILNGRKELA FAPDRRMGAE MTLLRALAFH
PKAVIAELSS APSAVQGSDI LTVSAAAVQG VVSPAPEPTV MLQTVNVPAA GAVPESTAQL
LQARSRLRQK AAGGSEPKKS EPAALQRAQP ASSALERLAS ISERGQQKIA SAEQEQASAR
KEAYRWKAQN RPVEKKAPKT TPRALRSALE HEKTPELAER LAQESLTRDE WARELSQLRL
PKLVQQLALN AFREPAPEGS VLLHLRSAQR HLNSASAQQM LAQALSGHYG HPVALSIVED
DDPQRRTPLE WRQAIYEESL AQARASIAAD GNIQTLRRLF DAELDEESIR PV
//
