DPO3X_ECOLI
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 03-AUG-2022, entry version 204.
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; Proteobacteria; 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};
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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 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; P06710; -.
DR PRIDE; P06710; -.
DR EnsemblBacteria; AAC73572; AAC73572; b0470.
DR EnsemblBacteria; AYC08179; AYC08179; b0470.
DR EnsemblBacteria; BAE76249; BAE76249; BAE76249.
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 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; IC:ComplexPortal.
DR GO; GO:0043846; C:DNA polymerase III, clamp loader complex; IDA:EcoliWiki.
DR GO; GO:0030894; C:replisome; IC: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:nucleoside-triphosphatase 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; 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 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
