DPO3X_SALTY
ID DPO3X_SALTY Reviewed; 642 AA.
AC P74876; P74877;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DNA polymerase III subunit tau;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase III subunit gamma;
GN Name=dnaX; Synonyms=dnaZ, dnaZX; OrderedLocusNames=STM0484;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POSSIBLE RIBOSOMAL FRAMESHIFT.
RC STRAIN=DB9005;
RX PubMed=9209069; DOI=10.1128/jb.179.13.4438-4442.1997;
RA Blinkova A., Burkart M.F., Owens T.D., Walker J.R.;
RT "Conservation of the Escherichia coli dnaX programmed ribosomal frameshift
RT signal in Salmonella typhimurium.";
RL J. Bacteriol. 179:4438-4442(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: [Isoform tau]: Serves as a scaffold to help in the
CC dimerization of the core complex. {ECO:0000250}.
CC -!- FUNCTION: [Isoform gamma]: Seems to interact with the delta subunit to
CC transfer the beta subunit on the DNA. {ECO:0000250}.
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 -!- SUBUNIT: The DNA polymerase holoenzyme is a complex that contains 10
CC different types of subunits. These subunits are organized into 3
CC functionally essential subassemblies: the pol III core, the beta
CC sliding clamp processivity factor and the clamp-loading complex. The
CC pol III core (subunits alpha, epsilon and theta) contains the
CC polymerase and the 3'-5' exonuclease proofreading activities. The
CC polymerase is tethered to the template via the sliding clamp
CC processivity factor. The clamp-loading complex assembles the beta
CC processivity factor onto the primer template and plays a central role
CC in the organization and communication at the replication fork. This
CC complex contains delta, delta', psi and chi, and copies of either or
CC both of two different DnaX proteins, gamma and tau. The composition of
CC the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-
CC (isoform:gamma/tau)[3]-delta,delta', psi,chi-beta[4] (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The production of the two protein products from this region
CC is probably due to programmed ribosomal frameshifting.;
CC Name=tau;
CC IsoId=P74876-1; Sequence=Displayed;
CC Name=gamma;
CC IsoId=P74876-2; Sequence=VSP_042850;
CC -!- MISCELLANEOUS: [Isoform tau]: Produced by full-length translation of
CC the dnaX gene.
CC -!- MISCELLANEOUS: [Isoform gamma]: Probably formed by programmed ribosomal
CC frameshifting to a premature stop codon in the -1 frame at codon 430.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR EMBL; U66040; AAC97559.1; -; Genomic_DNA.
DR EMBL; U66040; AAC97558.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19438.1; -; Genomic_DNA.
DR RefSeq; NP_459479.1; NC_003197.2. [P74876-1]
DR RefSeq; WP_000121962.1; NC_003197.2.
DR AlphaFoldDB; P74876; -.
DR SMR; P74876; -.
DR STRING; 99287.STM0484; -.
DR PaxDb; P74876; -.
DR EnsemblBacteria; AAL19438; AAL19438; STM0484.
DR GeneID; 1252004; -.
DR KEGG; stm:STM0484; -.
DR PATRIC; fig|99287.12.peg.517; -.
DR HOGENOM; CLU_006229_6_0_6; -.
DR OMA; YALHQGN; -.
DR PhylomeDB; P74876; -.
DR BioCyc; SENT99287:STM0484-MON; -.
DR Proteomes; UP000001014; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 3.30.300.150; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Ribosomal frameshifting; Transferase.
FT CHAIN 1..642
FT /note="DNA polymerase III subunit tau"
FT /id="PRO_0000007362"
FT REGION 385..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 431..642
FT /note="Missing (in isoform gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_042850"
FT CONFLICT 225..226
FT /note="IA -> SS (in Ref. 1; AAC97559/AAC97558)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="A -> C (in Ref. 1; AAC97559/AAC97558)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="Y -> H (in Ref. 1; AAC97559/AAC97558)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> F (in Ref. 1; AAC97559/AAC97558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 70596 MW; 0C72400BA477CF26 CRC64;
MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK
GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF
KVYLIDEVHM LSRHSFNALL KTLEEPPAHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV
EQIRHQLEHI LNEEHIAHEP RALQLLSRAA DGSLRDALSL TDQAIASGDG QVSTQAVSAM
LGTLDDDQAL SLVEAVVDAN GERVMSLINE AAARGIEWEA LLVEMLSLLH RIAMVQLSPA
ALGSDMAAIE QRMRELARTV PPGDLQLYYQ TLLIGRKELP WAPDRRMGVE MTLLRALAFH
PRMPLPEPET PRQSFAPVAP TAVMTPPQLQ QPSAPAPQTS PAPLPASTSQ VLAARNQLQR
AQGVTKTKKS EPAAASRARP VNNSALERLA SVSERVQARP APSALETAPV KKEAYRWKAT
TPVVQTKEVV ATPKALKKAL EHEKTPELAA KLAAEAIERD PWAAQVSQLS LPKLVEQVAL
NAWKEQNGNA VCLHLRSTQR HLNSSGAQQK LAQALSDLTG TTVELTIVED DNPAVRTPLE
WRQAIYEEKL AQARESIIAD NNIQTLRRFF DAELDEESIR PI
