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Chaperone protein ClpB (Heat shock protein F84.1)

 CLPB_ECOLI              Reviewed;         857 AA.
P63284; P03815;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
07-NOV-2018, entry version 131.
RecName: Full=Chaperone protein ClpB;
AltName: Full=Heat shock protein F84.1;
Name=clpB; Synonyms=htpM; OrderedLocusNames=b2592, JW2573;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
"Conservation of the regulatory subunit for the Clp ATP-dependent
protease in prokaryotes and eukaryotes.";
Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593.
STRAIN=K12;
PubMed=1906060; DOI=10.1128/jb.173.14.4247-4253.1991;
Kitagawa M., Wada C., Yoshioka S., Yura T.;
"Expression of ClpB, an analog of the ATP-dependent protease
regulatory subunit in Escherichia coli, is controlled by a heat shock
sigma factor (sigma 32).";
J. Bacteriol. 173:4247-4253(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 753-857.
PubMed=6285294; DOI=10.1093/nar/10.10.3303;
Shen W.-F., Squires C., Squires C.L.;
"Nucleotide sequence of the rrnG ribosomal RNA promoter region of
Escherichia coli.";
Nucleic Acids Res. 10:3303-3313(1982).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Ogura T., Tomoyasu T.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 1-14; 150-157; 355-364 AND 452-460.
PubMed=1953774; DOI=10.1016/S0006-291X(05)81326-9;
Pontis E., Sun X.Y., Joernvall H., Krook M., Reichard P.;
"ClpB proteins copurify with the anaerobic Escherichia coli
reductase.";
Biochem. Biophys. Res. Commun. 180:1222-1226(1991).
[9]
IDENTIFICATION AS A HEAT SHOCK PROTEIN.
PubMed=2066329; DOI=10.1128/jb.173.14.4254-4262.1991;
Squires C.L., Pedersen S., Ross B.M., Squires C.;
"ClpB is the Escherichia coli heat shock protein F84.1.";
J. Bacteriol. 173:4254-4262(1991).
[10]
ALTERNATIVE INITIATION, ATPASE ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=8376377;
Park S.K., Kim K.I., Woo K.M., Seol J.H., Tanaka K., Ichihara A.,
Ha D.B., Chung C.H.;
"Site-directed mutagenesis of the dual translational initiation sites
of the clpB gene of Escherichia coli and characterization of its gene
products.";
J. Biol. Chem. 268:20170-20174(1993).
[11]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[12]
SUBUNIT, AND MUTAGENESIS OF LYS-212 AND LYS-611.
PubMed=11061966; DOI=10.1006/jmbi.2000.4165;
Kim K.I., Cheong G.-W., Park S.-C., Ha J.-S., Woo K.M., Choi S.J.,
Chung C.H.;
"Heptameric ring structure of the heat-shock protein ClpB, a protein-
activated ATPase in Escherichia coli.";
J. Mol. Biol. 303:655-666(2000).
[13]
FUNCTION OF DOMAINS.
PubMed=10982797; DOI=10.1074/jbc.M005211200;
Barnett M.E., Zolkiewska A., Zolkiewski M.;
"Structure and activity of ClpB from Escherichia coli. Role of the
amino- and -carboxyl-terminal domains.";
J. Biol. Chem. 275:37565-37571(2000).
[14]
FUNCTION OF DOMAINS, AND MUTAGENESIS OF LYS-212; GLU-279; ARG-332;
TRP-543; LYS-611; GLU-678; ARG-756 AND 813-GLY--ARG-815.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12624113; DOI=10.1074/jbc.M209686200;
Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B.;
"Roles of individual domains and conserved motifs of the AAA+
chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone
activity.";
J. Biol. Chem. 278:17615-17624(2003).
[15]
BINDING TO PROTEIN AGGREGATES, AND INTERACTION WITH DNAK.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12805357; DOI=10.1074/jbc.M303653200;
Weibezahn J., Schlieker C., Bukau B., Mogk A.;
"Characterization of a trap mutant of the AAA+ chaperone ClpB.";
J. Biol. Chem. 278:32608-32617(2003).
[16]
FUNCTION OF MIDDLE DOMAIN.
PubMed=14640692; DOI=10.1021/bi035573d;
Kedzierska S., Akoev V., Barnett M.E., Zolkiewski M.;
"Structure and function of the middle domain of ClpB from Escherichia
coli.";
Biochemistry 42:14242-14248(2003).
[17]
OLIGOMERIZATION, AND NUCLEOTIDE-BINDING.
STRAIN=K12 / MC1000 / ATCC 39531;
PubMed=14978298; DOI=10.1110/ps.03422604;
Akoev V., Gogol E.P., Barnett M.E., Zolkiewski M.;
"Nucleotide-induced switch in oligomerization of the AAA+ ATPase
ClpB.";
Protein Sci. 13:567-574(2004).
[18]
SUBSTRATE-BINDING, AND MUTAGENESIS OF TYR-251; GLU-254 AND GLU-257.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=15208691; DOI=10.1038/nsmb787;
Schlieker C., Weibezahn J., Patzelt H., Tessarz P., Strub C., Zeth K.,
Erbse A., Schneider-Mergener J., Chin J.W., Schultz P.G., Bukau B.,
Mogk A.;
"Substrate recognition by the AAA+ chaperone ClpB.";
Nat. Struct. Mol. Biol. 11:607-615(2004).
[19]
MUTAGENESIS OF THR-7; SER-84; ASP-103 AND GLU-109.
PubMed=12139937; DOI=10.1016/S0022-2836(02)00591-0;
Liu Z., Tek V., Akoev V., Zolkiewski M.;
"Conserved amino acid residues within the amino-terminal domain of
ClpB are essential for the chaperone activity.";
J. Mol. Biol. 321:111-120(2002).
[20]
MUTAGENESIS OF LYS-212; LYS-611; ASP-797; ARG-815; ARG-819 AND
GLU-826.
PubMed=12220194; DOI=10.1021/bi026161s;
Barnett M.E., Zolkiewski M.;
"Site-directed mutagenesis of conserved charged amino acid residues in
ClpB from Escherichia coli.";
Biochemistry 41:11277-11283(2002).
[21]
CRYSTALLIZATION OF N-TERMINAL DOMAIN.
PubMed=11717522; DOI=10.1107/S0907444901017322;
Li J., Sha B.;
"Cloning, expression, purification and preliminary X-ray
crystallographic studies of Escherichia coli Hsp100 ClpB N-terminal
domain.";
Acta Crystallogr. D 57:1933-1935(2001).
[22]
CRYSTALLIZATION OF NBD2.
PubMed=12037306; DOI=10.1107/S0907444902006327;
Li J., Sha B.;
"Cloning, expression, purification and preliminary X-ray
crystallographic studies of Escherichia coli Hsp100 nucleotide-binding
domain 2 (NBD2).";
Acta Crystallogr. D 58:1030-1031(2002).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-176 AND LYS-640, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[24]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-351.
PubMed=12054807; DOI=10.1016/S0022-2836(02)00188-2;
Li J., Sha B.;
"Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1
(NBD1) and mechanistic studies on ClpB ATPase activity.";
J. Mol. Biol. 318:1127-1137(2002).
[25]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-142, AND MUTAGENESIS OF
LEU-93; LEU-97 AND LEU-110.
PubMed=12623019; DOI=10.1016/S0969-2126(03)00030-3;
Li J., Sha B.;
"Crystal structure of the E. coli Hsp100 ClpB N-terminal domain.";
Structure 11:323-328(2003).
-!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
involved in the recovery of the cell from heat-induced damage, in
cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
processing of protein aggregates. Protein binding stimulates the
ATPase activity; ATP hydrolysis unfolds the denatured protein
aggregates, which probably helps expose new hydrophobic binding
sites on the surface of ClpB-bound aggregates, contributing to the
solubilization and refolding of denatured protein aggregates by
DnaK. {ECO:0000269|PubMed:10982797, ECO:0000269|PubMed:12624113,
ECO:0000269|PubMed:14640692}.
-!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
{ECO:0000269|PubMed:11061966}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-546182, EBI-546182;
P0A6Y8:dnaK; NbExp=8; IntAct=EBI-546182, EBI-542092;
P33014:yeeD; NbExp=3; IntAct=EBI-546182, EBI-9130839;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8376377}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=ClpB;
IsoId=P63284-1; Sequence=Displayed;
Name=ClpB-3;
IsoId=P63284-2; Sequence=VSP_018703, VSP_018987;
Note=ClpB-3 ATPase activity is not activated by proteins, as it
is in ClpB.;
-!- INDUCTION: By heat shock and other environmental stresses.
-!- DOMAIN: The N-terminal domain probably functions as a substrate-
discriminating domain, recruiting aggregated proteins to the ClpB
hexamer and/or stabilizing bound proteins. The NBD2 domain is
responsible for oligomerization, whereas the NBD1 domain
stabilizes the hexamer probably in an ATP-dependent manner. The
movement of the coiled-coil domain is essential for ClpB ability
to rescue proteins from an aggregated state, probably by pulling
apart large aggregated proteins, which are bound between the
coiled-coils motifs of adjacent ClpB subunits in the functional
hexamer.
-!- MISCELLANEOUS: One peptide binds per ClpB hexamer; the binding
site is formed only upon ATP-driven oligomerization.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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EMBL; M29364; AAA24422.1; -; Genomic_DNA.
EMBL; U00096; AAC75641.1; -; Genomic_DNA.
EMBL; AP009048; BAA16476.1; -; Genomic_DNA.
EMBL; X57620; CAA40846.1; -; Genomic_DNA.
EMBL; V00350; CAA23639.1; -; Genomic_DNA.
EMBL; U50134; AAA92959.1; -; Genomic_DNA.
PIR; C65037; D35905.
RefSeq; NP_417083.1; NC_000913.3.
RefSeq; WP_001235102.1; NZ_LN832404.1.
PDB; 1JBK; X-ray; 1.80 A; A=159-351.
PDB; 1KHY; X-ray; 1.95 A; A/B/C/D=1-148.
PDB; 4CIU; X-ray; 3.50 A; A=143-857.
PDB; 4D2Q; EM; 18.00 A; A/B/C/D/E/F=1-857.
PDB; 4D2U; EM; 17.00 A; A/B/C/D/E/F=1-857.
PDB; 4D2X; EM; 20.00 A; A/B/C/D/E/F=1-857.
PDB; 5OFO; EM; 4.60 A; A/B/C/D/E/F=1-721, A/B/C/D/E/F=750-857.
PDB; 5OG1; EM; 4.50 A; A/B/C/D/E/F=1-721, A/B/C/D/E/F=750-857.
PDBsum; 1JBK; -.
PDBsum; 1KHY; -.
PDBsum; 4CIU; -.
PDBsum; 4D2Q; -.
PDBsum; 4D2U; -.
PDBsum; 4D2X; -.
PDBsum; 5OFO; -.
PDBsum; 5OG1; -.
ProteinModelPortal; P63284; -.
SMR; P63284; -.
BioGrid; 4260618; 221.
BioGrid; 851414; 30.
DIP; DIP-35844N; -.
IntAct; P63284; 81.
MINT; P63284; -.
STRING; 316385.ECDH10B_2760; -.
CarbonylDB; P63284; -.
iPTMnet; P63284; -.
SWISS-2DPAGE; P63284; -.
EPD; P63284; -.
PaxDb; P63284; -.
PRIDE; P63284; -.
EnsemblBacteria; AAC75641; AAC75641; b2592.
EnsemblBacteria; BAA16476; BAA16476; BAA16476.
GeneID; 947077; -.
KEGG; ecj:JW2573; -.
KEGG; eco:b2592; -.
PATRIC; fig|1411691.4.peg.4145; -.
EchoBASE; EB0155; -.
EcoGene; EG10157; clpB.
eggNOG; ENOG4105C2Z; Bacteria.
eggNOG; COG0542; LUCA.
HOGENOM; HOG000218211; -.
InParanoid; P63284; -.
KO; K03695; -.
PhylomeDB; P63284; -.
BioCyc; EcoCyc:EG10157-MONOMER; -.
SABIO-RK; P63284; -.
EvolutionaryTrace; P63284; -.
PRO; PR:P63284; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042623; F:ATPase activity, coupled; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
GO; GO:0042026; P:protein refolding; IEA:InterPro.
GO; GO:0009408; P:response to heat; IMP:EcoCyc.
GO; GO:0006986; P:response to unfolded protein; IDA:EcoCyc.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR017730; Chaperonin_ClpB.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004176; Clp_N.
InterPro; IPR036628; Clp_N_dom_sf.
InterPro; IPR001270; ClpA/B.
InterPro; IPR018368; ClpA/B_CS1.
InterPro; IPR028299; ClpA/B_CS2.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF02861; Clp_N; 2.
Pfam; PF10431; ClpB_D2-small; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81923; SSF81923; 1.
TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation; ATP-binding;
Chaperone; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleotide-binding; Reference proteome;
Repeat; Stress response.
CHAIN 1 857 Chaperone protein ClpB.
/FTId=PRO_0000005491.
NP_BIND 206 213 ATP 1.
NP_BIND 605 612 ATP 2.
REGION 1 143 N-terminal.
REGION 159 340 NBD1.
REGION 341 545 Linker.
REGION 555 765 NBD2.
REGION 766 857 C-terminal.
COILED 391 525 {ECO:0000250}.
MOD_RES 96 96 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 176 176 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 640 640 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
VAR_SEQ 1 148 Missing (in isoform ClpB-3).
{ECO:0000305}.
/FTId=VSP_018703.
VAR_SEQ 149 149 V -> M (in isoform ClpB-3).
{ECO:0000305}.
/FTId=VSP_018987.
MUTAGEN 7 7 T->A: Loss of chaperone activity.
{ECO:0000269|PubMed:12139937}.
MUTAGEN 84 84 S->A: No effect.
{ECO:0000269|PubMed:12139937}.
MUTAGEN 93 93 L->Q: Loss of chaperone activity. Retains
ATPase activity.
{ECO:0000269|PubMed:12623019}.
MUTAGEN 97 97 L->Q: 75% decrease in chaperone activity;
retains ATPase activity.
{ECO:0000269|PubMed:12623019}.
MUTAGEN 103 103 D->A: Loss of chaperone activity.
{ECO:0000269|PubMed:12139937}.
MUTAGEN 109 109 E->A: Loss of chaperone activity.
{ECO:0000269|PubMed:12139937}.
MUTAGEN 110 110 L->Q: 30% decrease in chaperone activity;
retains ATPase activity.
{ECO:0000269|PubMed:12623019}.
MUTAGEN 212 212 K->T: Loss of ability to form oligomers
even in the presence of ATP. Loss of
chaperone activity.
{ECO:0000269|PubMed:11061966,
ECO:0000269|PubMed:12220194,
ECO:0000269|PubMed:12624113}.
MUTAGEN 251 251 Y->A: Decrease in ability to disaggregate
proteins due to decreased substrate-
binding activity. Retains hexameric
quaternary structure and ATPase activity.
{ECO:0000269|PubMed:15208691}.
MUTAGEN 254 254 E->A: Decrease in ability to disaggregate
proteins due to decreased substrate-
binding activity. Retains hexameric
quaternary structure and ATPase activity;
when associated with A-257.
{ECO:0000269|PubMed:15208691}.
MUTAGEN 257 257 E->A: Decrease in ability to disaggregate
proteins due to decreased substrate-
binding activity. Retains hexameric
quaternary structure and ATPase activity;
when associated with A-254.
{ECO:0000269|PubMed:15208691}.
MUTAGEN 279 279 E->A: No effect on oligomerization.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 332 332 R->A: Loss of ability to form oligomers.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 543 543 W->F: No effect on chaperone activity or
ability to form oligomers.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 611 611 K->T: No effect on ability to form
oligomers. Loss of chaperone activity.
{ECO:0000269|PubMed:11061966,
ECO:0000269|PubMed:12220194,
ECO:0000269|PubMed:12624113}.
MUTAGEN 678 678 E->A: No effect on oligomerization.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 756 756 R->A: No effect on oligomerization. Loss
of ATPase activity.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 797 797 D->A: No effect.
{ECO:0000269|PubMed:12220194}.
MUTAGEN 813 815 GAR->AAA: No effect on oligomerization.
{ECO:0000269|PubMed:12624113}.
MUTAGEN 815 815 R->A: Loss of ability to form oligomers;
loss of chaperone activity.
{ECO:0000269|PubMed:12220194}.
MUTAGEN 819 819 R->A: Loss of ability to form oligomers;
loss of chaperone activity.
{ECO:0000269|PubMed:12220194}.
MUTAGEN 826 826 E->A: No effect.
{ECO:0000269|PubMed:12220194}.
CONFLICT 96 97 KL -> NV (in Ref. 1; AAA24422).
{ECO:0000305}.
CONFLICT 122 122 L -> V (in Ref. 1; AAA24422).
{ECO:0000305}.
HELIX 8 23 {ECO:0000244|PDB:1KHY}.
STRAND 27 29 {ECO:0000244|PDB:1KHY}.
HELIX 31 39 {ECO:0000244|PDB:1KHY}.
HELIX 46 53 {ECO:0000244|PDB:1KHY}.
HELIX 57 68 {ECO:0000244|PDB:1KHY}.
HELIX 85 101 {ECO:0000244|PDB:1KHY}.
STRAND 104 106 {ECO:0000244|PDB:1KHY}.
HELIX 108 116 {ECO:0000244|PDB:1KHY}.
HELIX 120 128 {ECO:0000244|PDB:1KHY}.
HELIX 133 141 {ECO:0000244|PDB:1KHY}.
HELIX 159 164 {ECO:0000244|PDB:1JBK}.
STRAND 165 167 {ECO:0000244|PDB:1JBK}.
HELIX 168 173 {ECO:0000244|PDB:1JBK}.
HELIX 184 194 {ECO:0000244|PDB:1JBK}.
STRAND 196 199 {ECO:0000244|PDB:1JBK}.
STRAND 201 205 {ECO:0000244|PDB:1JBK}.
HELIX 212 225 {ECO:0000244|PDB:1JBK}.
HELIX 230 232 {ECO:0000244|PDB:1JBK}.
STRAND 236 240 {ECO:0000244|PDB:1JBK}.
HELIX 242 246 {ECO:0000244|PDB:1JBK}.
TURN 247 249 {ECO:0000244|PDB:1JBK}.
HELIX 252 268 {ECO:0000244|PDB:1JBK}.
TURN 270 272 {ECO:0000244|PDB:1JBK}.
STRAND 273 278 {ECO:0000244|PDB:1JBK}.
HELIX 280 283 {ECO:0000244|PDB:1JBK}.
HELIX 296 304 {ECO:0000244|PDB:1JBK}.
STRAND 310 314 {ECO:0000244|PDB:1JBK}.
HELIX 316 322 {ECO:0000244|PDB:1JBK}.
TURN 323 325 {ECO:0000244|PDB:1JBK}.
HELIX 327 330 {ECO:0000244|PDB:1JBK}.
STRAND 333 337 {ECO:0000244|PDB:1JBK}.
HELIX 343 347 {ECO:0000244|PDB:1JBK}.
STRAND 363 365 {ECO:0000244|PDB:4CIU}.
HELIX 367 380 {ECO:0000244|PDB:4CIU}.
HELIX 388 406 {ECO:0000244|PDB:4CIU}.
HELIX 410 429 {ECO:0000244|PDB:4CIU}.
HELIX 444 492 {ECO:0000244|PDB:4CIU}.
HELIX 496 503 {ECO:0000244|PDB:4CIU}.
HELIX 505 523 {ECO:0000244|PDB:4CIU}.
HELIX 533 544 {ECO:0000244|PDB:4CIU}.
HELIX 549 552 {ECO:0000244|PDB:4CIU}.
HELIX 555 560 {ECO:0000244|PDB:4CIU}.
HELIX 562 569 {ECO:0000244|PDB:4CIU}.
HELIX 574 589 {ECO:0000244|PDB:4CIU}.
STRAND 598 605 {ECO:0000244|PDB:4CIU}.
STRAND 607 610 {ECO:0000244|PDB:4CIU}.
HELIX 611 623 {ECO:0000244|PDB:4CIU}.
STRAND 624 633 {ECO:0000244|PDB:4CIU}.
HELIX 634 636 {ECO:0000244|PDB:4CIU}.
HELIX 640 645 {ECO:0000244|PDB:4CIU}.
HELIX 661 668 {ECO:0000244|PDB:4CIU}.
STRAND 673 678 {ECO:0000244|PDB:4CIU}.
HELIX 679 681 {ECO:0000244|PDB:4CIU}.
HELIX 684 696 {ECO:0000244|PDB:4CIU}.
STRAND 697 700 {ECO:0000244|PDB:4CIU}.
STRAND 706 708 {ECO:0000244|PDB:4CIU}.
STRAND 713 719 {ECO:0000244|PDB:4CIU}.
HELIX 722 726 {ECO:0000244|PDB:4CIU}.
TURN 734 736 {ECO:0000244|PDB:4CIU}.
HELIX 737 748 {ECO:0000244|PDB:4CIU}.
HELIX 751 756 {ECO:0000244|PDB:4CIU}.
STRAND 757 762 {ECO:0000244|PDB:4CIU}.
HELIX 768 788 {ECO:0000244|PDB:4CIU}.
STRAND 792 795 {ECO:0000244|PDB:4CIU}.
HELIX 797 807 {ECO:0000244|PDB:4CIU}.
TURN 810 812 {ECO:0000244|PDB:4CIU}.
TURN 814 816 {ECO:0000244|PDB:4CIU}.
HELIX 817 824 {ECO:0000244|PDB:4CIU}.
HELIX 826 835 {ECO:0000244|PDB:4CIU}.
STRAND 836 838 {ECO:0000244|PDB:4CIU}.
STRAND 842 849 {ECO:0000244|PDB:4CIU}.
STRAND 852 857 {ECO:0000244|PDB:4CIU}.
SEQUENCE 857 AA; 95585 MW; FD38CD96B2F7C32A CRC64;
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL
RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG
TLADILKAAG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL
DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII
QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE
QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL
ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK
RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP
GKVIRLEVNE DRIVAVQ


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