HSLU_ECOLI
ID HSLU_ECOLI Reviewed; 443 AA.
AC P0A6H5; P32168; Q2M8M7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE AltName: Full=Heat shock protein HslU;
DE AltName: Full=Unfoldase HslU;
GN Name=hslU; Synonyms=htpI; OrderedLocusNames=b3931, JW3902;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8244018; DOI=10.1016/0378-1119(93)90167-2;
RA Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "Sequence analysis of four new heat-shock genes constituting the
RT hslTS/ibpAB and hslVU operons in Escherichia coli.";
RL Gene 134:1-6(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
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 [4]
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 [5]
RP MUTAGENESIS OF LYS-63.
RX PubMed=8977096; DOI=10.1016/s0014-5793(96)01223-9;
RA Shin D.H., Yoo S.J., Shim Y.K., Seol J.H., Kang M.S., Chung C.H.;
RT "Mutational analysis of the ATP-binding site in HslU, the ATPase component
RT of HslVU protease in Escherichia coli.";
RL FEBS Lett. 398:151-154(1996).
RN [6]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8662828; DOI=10.1074/jbc.271.24.14035;
RA Yoo S.J., Seol J.H., Shin D.H., Rohrwild M., Kang M.-S., Tanaka K.,
RA Goldberg A.L., Chung C.H.;
RT "Purification and characterization of the heat shock proteins HslV and HslU
RT that form a new ATP-dependent protease in Escherichia coli.";
RL J. Biol. Chem. 271:14035-14040(1996).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8650174; DOI=10.1073/pnas.93.12.5808;
RA Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., Seol J.H.,
RA Chung C.H., Goldberg A.L.;
RT "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli
RT related to the eukaryotic proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996).
RN [8]
RP EFFECTS OF ATP BINDING ON COMPLEX FORMATION.
RX PubMed=9299555; DOI=10.1006/bbrc.1997.7341;
RA Yoo S.J., Seol J.H., Seong I.S., Kang M.-S., Chung C.H.;
RT "ATP binding, but not its hydrolysis, is required for assembly and
RT proteolytic activity of the HslVU protease in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 238:581-585(1997).
RN [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=9288941; DOI=10.1111/j.1432-1033.1997.01143.x;
RA Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L.,
RA Chung C.H.;
RT "The heat-shock protein HslVU from Escherichia coli is a protein-activated
RT ATPase as well as an ATP-dependent proteinase.";
RL Eur. J. Biochem. 247:1143-1150(1997).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9393683; DOI=10.1128/jb.179.23.7219-7225.1997;
RA Kanemori M., Nishihara K., Yanagi H., Yura T.;
RT "Synergistic roles of HslVU and other ATP-dependent proteases in
RT controlling in vivo turnover of sigma32 and abnormal proteins in
RT Escherichia coli.";
RL J. Bacteriol. 179:7219-7225(1997).
RN [12]
RP MUTAGENESIS OF CYS-262 AND CYS-288.
RX PubMed=9722513; DOI=10.1074/jbc.273.36.22929;
RA Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H.,
RA Shimbara N., Tanaka K., Chung C.H.;
RT "Effects of the cys mutations on structure and function of the ATP-
RT dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in
RT HslU uncouples the ATP-dependent proteolysis by HslvU from ATP
RT hydrolysis.";
RL J. Biol. Chem. 273:22929-22935(1998).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10452560; DOI=10.1016/s0014-5793(99)00935-7;
RA Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.;
RT "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU
RT protease in Escherichia coli.";
RL FEBS Lett. 456:211-214(1999).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=10419524; DOI=10.1074/jbc.274.31.22002;
RA Kanemori M., Yanagi H., Yura T.;
RT "Marked instability of the sigma(32) heat shock transcription factor at
RT high temperature. Implications for heat shock regulation.";
RL J. Biol. Chem. 274:22002-22007(1999).
RN [15]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15696175; DOI=10.1038/nsmb898;
RA Burton R.E., Baker T.A., Sauer R.T.;
RT "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.";
RL Nat. Struct. Mol. Biol. 12:245-251(2005).
RN [16]
RP REACTION MECHANISM.
RX PubMed=19801685; DOI=10.1074/jbc.m109.045807;
RA Lee J.W., Park E., Jeong M.S., Jeon Y.J., Eom S.H., Seol J.H., Chung C.H.;
RT "HslVU ATP-dependent protease utilizes maximally six among twelve threonine
RT active sites during proteolysis.";
RL J. Biol. Chem. 284:33475-33484(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH ATP AND HSLV.
RX PubMed=10693812; DOI=10.1038/35001629;
RA Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D.,
RA Huber R.;
RT "The structures of HslU and the ATP-dependent protease HslU-HslV.";
RL Nature 403:800-805(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176 OF APOENZYME AND IN
RP COMPLEXES WITH HSLV AND ATP, AND MUTAGENESIS OF LYS-80; GLU-88; TYR-91;
RP VAL-92; GLY-93; GLU-95; GLU-266; GLU-286; ILE-312; GLU-321; ARG-325;
RP GLU-385 AND ARG-393.
RX PubMed=11114186; DOI=10.1073/pnas.250491797;
RA Song H.K., Hartmann C., Ramachandran R., Bochtler M., Behrendt R.,
RA Moroder L., Huber R.;
RT "Mutational studies on HslU and its docking mode with HslV.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14103-14108(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-443 IN COMPLEX WITH ADP.
RX PubMed=11709174; DOI=10.1016/s0969-2126(01)00670-0;
RA Wang J., Song J.J., Seong I.S., Franklin M.C., Kamtekar S., Eom S.H.,
RA Chung C.H.;
RT "Nucleotide-dependent conformational changes in a protease-associated
RT ATPase HslU.";
RL Structure 9:1107-1116(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (4.16 ANGSTROMS) IN COMPLEX WITH B.SUBTILIS HSLV AND
RP ADP.
RX PubMed=15983416; DOI=10.1107/s0907444905009546;
RA Wang J., Rho S.H., Park H.H., Eom S.H.;
RT "Correction of X-ray intensities from an HslV-HslU co-crystal containing
RT lattice-translocation defects.";
RL Acta Crystallogr. D 61:932-941(2005).
CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC subunit has chaperone activity. The binding of ATP and its subsequent
CC hydrolysis by HslU are essential for unfolding of protein substrates
CC subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC its protein substrates and unfolds these before they are guided to HslV
CC for hydrolysis. {ECO:0000269|PubMed:10419524,
CC ECO:0000269|PubMed:10452560, ECO:0000269|PubMed:15696175,
CC ECO:0000269|PubMed:8650174, ECO:0000269|PubMed:8662828,
CC ECO:0000269|PubMed:9288941, ECO:0000269|PubMed:9393683}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for ATP (in the absence of HslV)
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC KM=0.28 mM for ATP (in the presence of HslV)
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC Vmax=57 pmol/min/mg enzyme (in the absence of HslV)
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC Vmax=213 pmol/min/mg enzyme (in the presence of HslV)
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable
CC variant of Arc.;
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:15696175, ECO:0000269|PubMed:8662828};
CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC complex is dependent on binding of ATP. {ECO:0000269|PubMed:11709174,
CC ECO:0000269|PubMed:15983416}.
CC -!- INTERACTION:
CC P0A6H5; P0A6H5: hslU; NbExp=5; IntAct=EBI-369317, EBI-369317;
CC P0A6H5; P0A7B8: hslV; NbExp=16; IntAct=EBI-369317, EBI-552265;
CC P0A6H5; P0AFZ5: sulA; NbExp=5; IntAct=EBI-369317, EBI-2012039;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:8244018}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000305}.
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DR EMBL; L19201; AAB03063.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76913.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77379.1; -; Genomic_DNA.
DR PIR; JT0761; JT0761.
DR RefSeq; NP_418366.1; NC_000913.3.
DR RefSeq; WP_001293341.1; NZ_STEB01000017.1.
DR PDB; 1DO0; X-ray; 3.00 A; A/B/C/D/E/F=2-443.
DR PDB; 1DO2; X-ray; 4.00 A; A/B/C/D=2-443.
DR PDB; 1E94; X-ray; 2.80 A; E/F=2-443.
DR PDB; 1G4A; X-ray; 3.00 A; E/F=1-443.
DR PDB; 1G4B; X-ray; 7.00 A; E/F/K/L=1-443.
DR PDB; 1HQY; X-ray; 2.80 A; E/F=2-443.
DR PDB; 1HT1; X-ray; 2.80 A; E/F/G/I=2-443.
DR PDB; 1HT2; X-ray; 2.80 A; E/F/G/H=2-443.
DR PDB; 1YYF; X-ray; 4.16 A; A/B=1-443.
DR PDB; 5JI3; X-ray; 3.00 A; E/F=1-443.
DR PDB; 5TXV; X-ray; 7.09 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-443.
DR PDB; 6PXI; X-ray; 3.45 A; E/F=2-443.
DR PDB; 6PXK; X-ray; 3.65 A; A/B/C/D/E/F/G/H/I/J/K/L=2-443.
DR PDB; 6PXL; X-ray; 3.74 A; A/B/C/D/E/F/G/H/I/J/K/L=2-443.
DR PDBsum; 1DO0; -.
DR PDBsum; 1DO2; -.
DR PDBsum; 1E94; -.
DR PDBsum; 1G4A; -.
DR PDBsum; 1G4B; -.
DR PDBsum; 1HQY; -.
DR PDBsum; 1HT1; -.
DR PDBsum; 1HT2; -.
DR PDBsum; 1YYF; -.
DR PDBsum; 5JI3; -.
DR PDBsum; 5TXV; -.
DR PDBsum; 6PXI; -.
DR PDBsum; 6PXK; -.
DR PDBsum; 6PXL; -.
DR AlphaFoldDB; P0A6H5; -.
DR SMR; P0A6H5; -.
DR BioGRID; 4261787; 251.
DR ComplexPortal; CPX-2104; HslUV protease complex.
DR DIP; DIP-31855N; -.
DR IntAct; P0A6H5; 47.
DR STRING; 511145.b3931; -.
DR MEROPS; X20.005; -.
DR SWISS-2DPAGE; P0A6H5; -.
DR jPOST; P0A6H5; -.
DR PaxDb; P0A6H5; -.
DR PRIDE; P0A6H5; -.
DR EnsemblBacteria; AAC76913; AAC76913; b3931.
DR EnsemblBacteria; BAE77379; BAE77379; BAE77379.
DR GeneID; 58459844; -.
DR GeneID; 948430; -.
DR KEGG; ecj:JW3902; -.
DR KEGG; eco:b3931; -.
DR PATRIC; fig|1411691.4.peg.2774; -.
DR EchoBASE; EB1827; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_6; -.
DR InParanoid; P0A6H5; -.
DR OMA; KYGMIKT; -.
DR PhylomeDB; P0A6H5; -.
DR BioCyc; EcoCyc:EG11881-MON; -.
DR BioCyc; MetaCyc:EG11881-MON; -.
DR BRENDA; 3.4.25.2; 2026.
DR EvolutionaryTrace; P0A6H5; -.
DR PRO; PR:P0A6H5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009376; C:HslUV protease complex; IDA:CAFA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0034605; P:cellular response to heat; IC:ComplexPortal.
DR GO; GO:0030164; P:protein denaturation; IDA:ComplexPortal.
DR GO; GO:0043335; P:protein unfolding; IMP:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:CAFA.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR DisProt; DP00100; -.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00249; HslU; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00390; hslU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160500"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 63
FT /note="K->T: Can neither bind nor hydrolyze ATP. Do not
FT form multimers, but stays as monomer."
FT /evidence="ECO:0000269|PubMed:8977096"
FT MUTAGEN 80
FT /note="K->T: Some effect on protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 88
FT /note="E->Q: Severely reduced protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 91
FT /note="Y->G: Partial loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 92
FT /note="V->G: Partial loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 93
FT /note="G->A: Almost no protease or ATP hydrolysis
FT activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 95
FT /note="E->W: Partial loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 262
FT /note="C->V: No effect on ATP hydrolysis. Can support HslV-
FT mediated proteolysis at wild-type levels."
FT /evidence="ECO:0000269|PubMed:9722513"
FT MUTAGEN 266
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 286
FT /note="E->Q: Reduced protease activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 288
FT /note="C->V: No ATP hydrolysis activity. Binds ATP with
FT lower affinity than wild-type. Can support HslV-mediated
FT proteolysis to some extent."
FT /evidence="ECO:0000269|PubMed:9722513"
FT MUTAGEN 312
FT /note="I->W: No effect."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 321
FT /note="E->Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 325
FT /note="R->E: Complete loss of activity. Forms wild-type
FT complexes with HslV and is able to bind ATP."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 385
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 393
FT /note="R->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:11114186"
FT MUTAGEN 436
FT /note="E->K: Partial loss of protease activity; when
FT associated with K-437."
FT MUTAGEN 437
FT /note="D->K: Partial loss of protease activity; when
FT associated with K-436."
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1E94"
FT TURN 150..154
FT /evidence="ECO:0007829|PDB:1HQY"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1DO0"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6PXI"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:6PXI"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1DO0"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 269..286
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 370..386
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:1E94"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 422..434
FT /evidence="ECO:0007829|PDB:1E94"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:1E94"
SQ SEQUENCE 443 AA; 49594 MW; D2188639EA9AEF4C CRC64;
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR
YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA
PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK
QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA
TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI
DADYVSKHLD ALVADEDLSR FIL
