ID DPO3X_ECOLI Reviewed; 643 AA. AC P06710; A0A385XJC4; Q2MBV7; Q47721; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 212. 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=b0470, JW0459; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / JM109 / ATCC 53323; RX PubMed=3534795; DOI=10.1093/nar/14.20.8091; RA Flower A.M., McHenry C.S.; RT "The adjacent dnaZ and dnaX genes of Escherichia coli are contained within RT one continuous open reading frame."; RL Nucleic Acids Res. 14:8091-8101(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3018672; DOI=10.1093/nar/14.16.6541; RA Yin K.-C., Blinkowa A.L., Walker J.R.; RT "Nucleotide sequence of the Escherichia coli replication gene dnaZX."; RL Nucleic Acids Res. 14:6541-6549(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PROTEIN SEQUENCE OF 1-13. RC STRAIN=ATCC 33694 / HB101; RX PubMed=3283125; DOI=10.1016/s0021-9258(18)68676-4; RA Maki S., Kornberg A.; RT "DNA polymerase III holoenzyme of Escherichia coli. I. Purification and RT distinctive functions of subunits tau and gamma, the dnaZX gene products."; RL J. Biol. Chem. 263:6547-6554(1988). RN [7] RP PROBABLE FUNCTION OF TAU IN DIMERIZATION OF DNA POLYMERASE. RC STRAIN=HMS 83; RX PubMed=7037770; DOI=10.1016/s0021-9258(18)34974-3; RA McHenry C.S.; RT "Purification and characterization of DNA polymerase III'. Identification RT of tau as a subunit of the DNA polymerase III holoenzyme."; RL J. Biol. Chem. 257:2657-2663(1982). RN [8] RP RIBOSOMAL FRAMESHIFT, ISOFORMS TAU AND GAMMA, AND PROTEIN SEQUENCE OF RP 428-431 (ISOFORM GAMMA). RX PubMed=2181440; DOI=10.1073/pnas.87.7.2516; RA Tsuchihashi Z., Kornberg A.; RT "Translational frameshifting generates the gamma subunit of DNA polymerase RT III holoenzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2516-2520(1990). RN [9] RP RIBOSOMAL FRAMESHIFT, AND ISOFORMS TAU AND GAMMA. RC STRAIN=K12 / JM103Y; RX PubMed=2186364; DOI=10.1093/nar/18.7.1725; RA Blinkowa A.L., Walker J.R.; RT "Programmed ribosomal frameshifting generates the Escherichia coli DNA RT polymerase III gamma subunit from within the tau subunit reading frame."; RL Nucleic Acids Res. 18:1725-1729(1990). RN [10] RP RIBOSOMAL FRAMESHIFT, AND ISOFORMS TAU AND GAMMA. RC STRAIN=K12; RX PubMed=2187190; DOI=10.1073/pnas.87.10.3713; RA Flower A.M., McHenry C.S.; RT "The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is RT produced by ribosomal frameshifting."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3713-3717(1990). RN [11] RP FUNCTION, AND SUBUNIT. RX PubMed=2040637; DOI=10.1016/s0021-9258(18)99166-0; RA Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M.; RT "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme."; RL J. Biol. Chem. 266:11328-11334(1991). RN [12] RP REVIEW. RX PubMed=1575709; DOI=10.1002/bies.950140206; RA O'Donnell M.; RT "Accessory protein function in the DNA polymerase III holoenzyme from E. RT coli."; RL Bioessays 14:105-111(1992). RN [13] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [14] RP IDENTIFICATION OF TEMPERATURE-SENSITIVE ALLELES, FUNCTION, AND MUTAGENESIS RP OF GLY-118 AND GLU-601. RC STRAIN=K12; RX PubMed=8376347; DOI=10.1128/jb.175.18.6018-6027.1993; RA Blinkova A., Hervas C., Stukenberg P.T., Onrust R., O'Donnell M.E., RA Walker J.R.; RT "The Escherichia coli DNA polymerase III holoenzyme contains both products RT of the dnaX gene, tau and gamma, but only tau is essential."; RL J. Bacteriol. 175:6018-6027(1993). RN [15] RP FUNCTION OF GAMMA, AND SUBUNIT. RX PubMed=9927437; DOI=10.1093/emboj/18.3.771; RA Turner J., Hingorani M.M., Kelman Z., O'Donnell M.; RT "The internal workings of a DNA polymerase clamp-loading machine."; RL EMBO J. 18:771-783(1999). RN [16] RP REPLISOME COMPLEX, AND SUBUNIT. RX PubMed=20413500; DOI=10.1126/science.1185757; RA Reyes-Lamothe R., Sherratt D.J., Leake M.C.; RT "Stoichiometry and architecture of active DNA replication machinery in RT Escherichia coli."; RL Science 328:498-501(2010). RN [17] RP REPLISOME COMPLEX, AND SUBUNIT. RX PubMed=22157955; DOI=10.1038/nsmb.2179; RA Georgescu R.E., Kurth I., O'Donnell M.E.; RT "Single-molecule studies reveal the function of a third polymerase in the RT replisome."; RL Nat. Struct. Mol. Biol. 19:113-116(2011). RN [18] {ECO:0007744|PDB:1JR3} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-373 (GAMMA) IN COMPLEX WITH RP HOLA AND HOLB. RX PubMed=11525729; DOI=10.1016/s0092-8674(01)00463-9; RA Jeruzalmi D., O'Donnell M., Kuriyan J.; RT "Crystal structure of the processivity clamp loader gamma (gamma) complex RT of E. coli DNA polymerase III."; RL Cell 106:429-441(2001). RN [19] {ECO:0007744|PDB:5FKU, ECO:0007744|PDB:5FKV} RP STRUCTURE BY ELECTRON MICROSCOPY (8.00 ANGSTROMS) OF 500-643 OF DNAE; DNAN; RP DNAQ; DNAX WITH AND WITHOUT DNA, AND SUBUNIT. RX PubMed=26499492; DOI=10.7554/elife.11134; RA Fernandez-Leiro R., Conrad J., Scheres S.H., Lamers M.H.; RT "cryo-EM structures of the E. coli replicative DNA polymerase reveal its RT dynamic interactions with the DNA sliding clamp, exonuclease and tau."; RL Elife 4:0-0(2015). CC -!- FUNCTION: Part of the beta sliding clamp loading complex, which CC hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA CC replication pre-initiation complex (PubMed:2040637). DNA polymerase III CC is a complex, multichain enzyme responsible for most of the replicative CC synthesis in bacteria. This DNA polymerase also exhibits 3'-5' CC exonuclease activity. The gamma complex (gamma(3),delta,delta') is CC thought to load beta dimers onto DNA by binding ATP which alters the CC complex's conformation so it can bind beta sliding clamp dimers and CC open them at one interface. Primed DNA is recognized, ATP is hydrolyzed CC releasing the gamma complex and closing the beta sliding clamp ring CC around the primed DNA (PubMed:9927437). {ECO:0000269|PubMed:2040637}. CC -!- FUNCTION: [Isoform tau]: Serves as a scaffold to trimerize the core CC complex (PubMed:7037770). {ECO:0000305|PubMed:7037770}. CC -!- FUNCTION: [Isoform gamma]: Interacts with the delta and delta' subunits CC to transfer the beta subunit on the DNA (PubMed:9927437). Interacts CC with ATP, drives ATP-induced conformational changes in the gamma CC complex that opens the beta sliding clamp ring. After loading of primed CC DNA ATP is hydrolyzed and the beta sliding clamp ring closes CC (PubMed:9927437). {ECO:0000269|PubMed:9927437}. 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 III holoenzyme complex contains at least 10 CC different subunits organized into 3 functionally essential CC subassemblies: the Pol III core, the beta sliding clamp processivity CC factor and the clamp-loading complex. The Pol III core (subunits alpha, CC epsilon and theta) contains the polymerase and the 3'-5' exonuclease CC proofreading activities (PubMed:2040637). The polymerase is tethered to CC the template via the dimeric beta sliding clamp processivity factor. CC The clamp-loading complex (also called gamma complex) assembles the CC beta sliding clamp onto the primed template and plays a central role in CC the organization and communication at the replication fork. The clamp- CC loading complex contains delta, delta', psi and chi, and 3 copies of CC either or both of two different DnaX proteins, gamma and tau. The DNA CC replisome complex has a single clamp loader (3 tau and 1 each of delta, CC delta', psi and chi subunits) which binds 3 Pol III cores (1 core on CC the leading strand and 2 on the lagging strand) each with a beta CC sliding clamp dimer. Additional proteins in the replisome are other CC copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase CC (PubMed:20413500, PubMed:22157955). The clamp loader hydrolyzes ATP to CC assemble the beta processivity factor onto the primed template CC (PubMed:2040637, PubMed:9927437) and plays a central role in the CC organization and communication at the replication fork; the minimal CC complex to load the beta sliding clamp on DNA is delta, delta', gamma CC (PubMed:9927437). {ECO:0000269|PubMed:11525729, CC ECO:0000269|PubMed:2040637, ECO:0000269|PubMed:20413500, CC ECO:0000269|PubMed:22157955, ECO:0000269|PubMed:9927437}. CC -!- INTERACTION: CC P06710; P11989: bglG; NbExp=3; IntAct=EBI-549140, EBI-545674; CC P06710; P0ACB0: dnaB; NbExp=2; IntAct=EBI-549140, EBI-548978; CC P06710; P10443: dnaE; NbExp=12; IntAct=EBI-549140, EBI-549111; CC P06710; P0A988: dnaN; NbExp=4; IntAct=EBI-549140, EBI-542385; CC P06710; P03007: dnaQ; NbExp=6; IntAct=EBI-549140, EBI-549131; CC P06710; P06710: dnaX; NbExp=9; IntAct=EBI-549140, EBI-549140; CC P06710; P20605: fic; NbExp=2; IntAct=EBI-549140, EBI-1132602; CC P06710; P28630: holA; NbExp=19; IntAct=EBI-549140, EBI-549153; CC P06710; P28631: holB; NbExp=26; IntAct=EBI-549140, EBI-549161; CC P06710; P28905: holC; NbExp=20; IntAct=EBI-549140, EBI-549169; CC P06710; P28632: holD; NbExp=26; IntAct=EBI-549140, EBI-549176; CC P06710; P0A7L0: rplA; NbExp=2; IntAct=EBI-549140, EBI-543771; CC P06710; P0AGE0: ssb; NbExp=2; IntAct=EBI-549140, EBI-1118620; CC P06710-1; P28630: holA; NbExp=5; IntAct=EBI-6464728, EBI-549153; CC P06710-1; P28631: holB; NbExp=6; IntAct=EBI-6464728, EBI-549161; CC P06710-2; P06710-2: dnaX; NbExp=2; IntAct=EBI-2604194, EBI-2604194; CC P06710-2; P28630: holA; NbExp=6; IntAct=EBI-2604194, EBI-549153; CC P06710-2; P28632: holD; NbExp=2; IntAct=EBI-2604194, EBI-549176; CC P06710-2; P23367: mutL; NbExp=2; IntAct=EBI-2604194, EBI-554913; CC -!- ALTERNATIVE PRODUCTS: CC Event=Ribosomal frameshifting; Named isoforms=2; CC Comment=The production of the two protein products from this region CC is due to programmed ribosomal frameshifting. Frameshifting is about CC 40% efficient. {ECO:0000269|PubMed:2181440, CC ECO:0000269|PubMed:2186364, ECO:0000269|PubMed:2187190}; CC Name=tau; CC IsoId=P06710-1; Sequence=Displayed; CC Name=gamma; CC IsoId=P06710-2; Sequence=VSP_042848, VSP_042849; CC -!- MISCELLANEOUS: [Isoform tau]: Produced by full-length translation of CC the dnaX gene. This isoform is essential, constructs that express only CC the gamma isoform are not viable (PubMed:8376347). CC {ECO:0000269|PubMed:8376347}. CC -!- MISCELLANEOUS: [Isoform gamma]: Formed by programmed ribosomal CC frameshifting to a premature stop codon in the -1 frame at codon 430, CC the last residue is thus Glu and not Ser. Mutants which remove the CC frameshift are viable, suggesting strongly that gamma is not essential CC for viability (PubMed:8376347). {ECO:0000269|PubMed:2181440, CC ECO:0000269|PubMed:2186364, ECO:0000269|PubMed:2187190, CC ECO:0000269|PubMed:8376347}. CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA28175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04487; CAA28174.1; -; Genomic_DNA. DR EMBL; X04487; CAA28175.1; ALT_INIT; Genomic_DNA. DR EMBL; X04275; CAA27827.1; -; Genomic_DNA. DR EMBL; U82664; AAB40224.1; -; Genomic_DNA. DR EMBL; U00096; AAC73572.1; -; Genomic_DNA. DR EMBL; U00096; AYC08179.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76249.1; -; Genomic_DNA. DR EMBL; M38777; AAA23457.1; -; Genomic_DNA. DR PIR; A25549; DJEC3G. DR RefSeq; NP_415003.1; NC_000913.3. DR RefSeq; WP_000122013.1; NZ_SSUW01000008.1. DR PDB; 1JR3; X-ray; 2.70 A; A/B/C=1-373. DR PDB; 1NJF; X-ray; 2.30 A; A/B/C/D=1-243. DR PDB; 1NJG; X-ray; 2.20 A; A/B=1-243. DR PDB; 1XXH; X-ray; 3.45 A; B/C/D/G/H/I=1-373. DR PDB; 1XXI; X-ray; 4.10 A; B/C/D/G/H/I=1-368. DR PDB; 2AYA; NMR; -; A=499-625. DR PDB; 3GLF; X-ray; 3.39 A; B/C/D/G/H/I=1-373. DR PDB; 3GLG; X-ray; 3.25 A; B/C/D/G/H/I=1-373. DR PDB; 3GLH; X-ray; 3.89 A; B/C/D/G/H/I/L/M/N=1-373. DR PDB; 3GLI; X-ray; 3.50 A; B/C/D/G/H/I=1-373. DR PDB; 5FKU; EM; 8.34 A; E=500-643. DR PDB; 5FKV; EM; 8.00 A; E=500-643. DR PDBsum; 1JR3; -. DR PDBsum; 1NJF; -. DR PDBsum; 1NJG; -. DR PDBsum; 1XXH; -. DR PDBsum; 1XXI; -. DR PDBsum; 2AYA; -. DR PDBsum; 3GLF; -. DR PDBsum; 3GLG; -. DR PDBsum; 3GLH; -. DR PDBsum; 3GLI; -. DR PDBsum; 5FKU; -. DR PDBsum; 5FKV; -. DR AlphaFoldDB; P06710; -. DR BMRB; P06710; -. DR EMDB; EMD-3198; -. DR EMDB; EMD-3201; -. DR SMR; P06710; -. DR BioGRID; 4259846; 140. DR BioGRID; 849494; 14. DR ComplexPortal; CPX-1926; DNA polymerase III clamp loader complex. DR DIP; DIP-9464N; -. DR IntAct; P06710; 33. DR STRING; 511145.b0470; -. DR BindingDB; P06710; -. DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate. DR jPOST; P06710; -. DR PaxDb; 511145-b0470; -. DR EnsemblBacteria; AAC73572; AAC73572; b0470. DR EnsemblBacteria; AYC08179; AYC08179; b0470. DR GeneID; 945105; -. DR KEGG; ecj:JW0459; -. DR KEGG; eco:b0470; -. DR PATRIC; fig|1411691.4.peg.1806; -. DR EchoBASE; EB0241; -. DR eggNOG; COG2812; Bacteria. DR HOGENOM; CLU_006229_6_0_6; -. DR InParanoid; P06710; -. DR OMA; YALHQGN; -. DR OrthoDB; 9810148at2; -. DR PhylomeDB; P06710; -. DR BRENDA; 3.6.4.B8; 2026. DR EvolutionaryTrace; P06710; -. DR PRO; PR:P06710; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; NAS:ComplexPortal. DR GO; GO:0043846; C:DNA polymerase III, clamp loader complex; IDA:EcoliWiki. DR GO; GO:0030894; C:replisome; NAS:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:EcoliWiki. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:EcoliWiki. DR GO; GO:0006260; P:DNA replication; IMP:EcoliWiki. DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Direct protein sequencing; DNA replication; KW DNA-directed DNA polymerase; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Ribosomal frameshifting; Transferase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..643 FT /note="DNA polymerase III subunit tau" FT /id="PRO_0000007360" FT REGION 385..404 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 385..400 FT /note="Pro 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 FT /note="S -> E (in isoform gamma)" FT /evidence="ECO:0000305" FT /id="VSP_042848" FT VAR_SEQ 432..643 FT /note="Missing (in isoform gamma)" FT /evidence="ECO:0000305" FT /id="VSP_042849" FT MUTAGEN 118 FT /note="G->D: In dnaX2016(Ts); present in both isoforms, FT unable to grow at 42 degrees Celsius." FT /evidence="ECO:0000269|PubMed:8376347" FT MUTAGEN 601 FT /note="E->K: In dnaX36(Ts); present only in isoform tau, FT unable to grow at 42 degrees Celsius." FT /evidence="ECO:0000269|PubMed:8376347" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 22..34 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:3GLF" FT HELIX 51..63 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 77..83 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:1NJG" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 101..109 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:3GLG" FT STRAND 116..126 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 133..144 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 150..157 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 180..193 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 200..210 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 214..225 FT /evidence="ECO:0007829|PDB:1NJG" FT TURN 226..229 FT /evidence="ECO:0007829|PDB:1NJG" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 234..240 FT /evidence="ECO:0007829|PDB:1NJG" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 261..274 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 278..294 FT /evidence="ECO:0007829|PDB:3GLG" FT TURN 295..297 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:3GLG" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:3GLF" FT HELIX 307..318 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 322..338 FT /evidence="ECO:0007829|PDB:3GLG" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:3GLG" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 345..358 FT /evidence="ECO:0007829|PDB:3GLG" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:3GLG" FT HELIX 507..520 FT /evidence="ECO:0007829|PDB:2AYA" FT HELIX 522..530 FT /evidence="ECO:0007829|PDB:2AYA" FT HELIX 535..541 FT /evidence="ECO:0007829|PDB:2AYA" FT STRAND 543..547 FT /evidence="ECO:0007829|PDB:2AYA" FT STRAND 549..556 FT /evidence="ECO:0007829|PDB:2AYA" FT HELIX 558..560 FT /evidence="ECO:0007829|PDB:2AYA" FT TURN 561..563 FT /evidence="ECO:0007829|PDB:2AYA" FT HELIX 566..580 FT /evidence="ECO:0007829|PDB:2AYA" FT STRAND 585..590 FT /evidence="ECO:0007829|PDB:2AYA" FT HELIX 599..620 FT /evidence="ECO:0007829|PDB:2AYA" SQ SEQUENCE 643 AA; 71138 MW; D2028BD99E375150 CRC64; MSYQVLARKW RPQTFADVVG QEHVLTALAN GLSLGRIHHA YLFSGTRGVG KTSIARLLAK GLNCETGITA TPCGVCDNCR EIEQGRFVDL IEIDAASRTK VEDTRDLLDN VQYAPARGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEHV KFLLATTDPQ KLPVTILSRC LQFHLKALDV EQIRHQLEHI LNEEHIAHEP RALQLLARAA EGSLRDALSL TDQAIASGDG QVSTQAVSAM LGTLDDDQAL SLVEAMVEAN GERVMALINE AAARGIEWEA LLVEMLGLLH RIAMVQLSPA ALGNDMAAIE LRMRELARTI PPTDIQLYYQ TLLIGRKELP YAPDRRMGVE MTLLRALAFH PRMPLPEPEV PRQSFAPVAP TAVMTPTQVP PQPQSAPQQA PTVPLPETTS QVLAARQQLQ RVQGATKAKK SEPAAATRAR PVNNAALERL ASVTDRVQAR PVPSALEKAP AKKEAYRWKA TTPVMQQKEV VATPKALKKA LEHEKTPELA AKLAAEAIER DPWAAQVSQL SLPKLVEQVA LNAWKEESDN AVCLHLRSSQ RHLNNRGAQQ KLAEALSMLK GSTVELTIVE DDNPAVRTPL EWRQAIYEEK LAQARESIIA DNNIQTLRRF FDAELDEESI RPI //