CLPB_THET8
ID CLPB_THET8 Reviewed; 854 AA.
AC Q9RA63; P74942; Q5SI87;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=TTHA1487;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10377389; DOI=10.1073/pnas.96.13.7184;
RA Motohashi K., Watanabe Y.H., Yohda M., Yoshida M.;
RT "Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB
RT chaperones.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7184-7189(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-508.
RX PubMed=10092456; DOI=10.1006/jmbi.1999.2636;
RA Klostermeier D., Seidel R., Reinstein J.;
RT "The functional cycle and regulation of the Thermus thermophilus DnaK
RT chaperone system.";
RL J. Mol. Biol. 287:511-525(1999).
RN [4]
RP INTERACTION WITH THE DNAK-DNAJ-GRPE CHAPERONE SYSTEM.
RX PubMed=10777521; DOI=10.1074/jbc.275.17.12388;
RA Watanabe Y.H., Motohashi K., Taguchi H., Yoshida M.;
RT "Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are
RT released as a chaperonin-recognizable non-native form.";
RL J. Biol. Chem. 275:12388-12392(2000).
RN [5]
RP PRELIMINARY CHARACTERIZATION OF SUBUNIT.
RX PubMed=11243796; DOI=10.1006/jmbi.2001.4455;
RA Schlee S., Groemping Y., Herde P., Seidel R., Reinstein J.;
RT "The chaperone function of ClpB from Thermus thermophilus depends on
RT allosteric interactions of its two ATP-binding sites.";
RL J. Mol. Biol. 306:889-899(2001).
RN [6]
RP SUBUNIT, AND MUTAGENESIS OF 204-LYS-THR-205; ASP-270; GLU-271;
RP 601-LYS-THR-602; ASP-667 AND GLU-668.
RX PubMed=11741950; DOI=10.1074/jbc.m109349200;
RA Watanabe Y.H., Motohashi K., Yoshida M.;
RT "Roles of the two ATP binding sites of ClpB from Thermus thermophilus.";
RL J. Biol. Chem. 277:5804-5809(2002).
RN [7]
RP INTERACTION WITH DNAK.
RX PubMed=14741222; DOI=10.1016/j.jmb.2003.12.013;
RA Schlee S., Beinker P., Akhrymuk A., Reinstein J.;
RT "A chaperone network for the resolubilization of protein aggregates: direct
RT interaction of ClpB and DnaK.";
RL J. Mol. Biol. 336:275-285(2004).
RN [8]
RP CRYSTALLIZATION.
RX PubMed=14646112; DOI=10.1107/s0907444903023266;
RA Lee S., Hisayoshi M., Yoshida M., Tsai F.T.F.;
RT "Crystallization and preliminary X-ray crystallographic analysis of the
RT Hsp100 protein clpB from Thermus thermophilus.";
RL Acta Crystallogr. D 59:2334-2336(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH AMPPNP, AND
RP MUTAGENESIS OF GLY-167; VAL-350; GLY-353; ARG-355; LEU-396; LEU-460;
RP ARG-464; GLN-467; ARG-475 AND GLU-520.
RX PubMed=14567920; DOI=10.1016/s0092-8674(03)00807-9;
RA Lee S., Sowa M.E., Watanabe Y.H., Sigler P.B., Chiu W., Yoshida M.,
RA Tsai F.T.F.;
RT "The structure of ClpB: a molecular chaperone that rescues proteins from an
RT aggregated state.";
RL Cell 115:229-240(2003).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000269|PubMed:10377389}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000269|PubMed:11741950, ECO:0000269|PubMed:14567920}.
CC -!- INTERACTION:
CC Q9RA63; Q9RA63: clpB; NbExp=9; IntAct=EBI-7698530, EBI-7698530;
CC Q9RA63; P02668: CSN3; Xeno; NbExp=3; IntAct=EBI-7698530, EBI-7234047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AB012390; BAA81745.1; -; Genomic_DNA.
DR EMBL; AB032368; BAA96085.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71310.1; -; Genomic_DNA.
DR EMBL; Y07826; CAA69163.2; -; Genomic_DNA.
DR RefSeq; WP_011228712.1; NC_006461.1.
DR RefSeq; YP_144753.1; NC_006461.1.
DR PDB; 1QVR; X-ray; 3.00 A; A/B/C=1-854.
DR PDB; 4FCT; X-ray; 4.00 A; A=545-852.
DR PDB; 4FCV; X-ray; 3.40 A; A/B/C=544-852.
DR PDB; 4FCW; X-ray; 2.35 A; A/C/F=544-852.
DR PDB; 4FD2; X-ray; 3.00 A; A/B/D=545-852.
DR PDB; 4HSE; X-ray; 2.20 A; A=142-534.
DR PDB; 4LJ4; X-ray; 2.80 A; A=520-854.
DR PDB; 4LJ5; X-ray; 2.40 A; A=520-854.
DR PDB; 4LJ6; X-ray; 1.90 A; A=520-854.
DR PDB; 4LJ7; X-ray; 2.80 A; A/B/C=520-854.
DR PDB; 4LJ8; X-ray; 2.10 A; A=520-854.
DR PDB; 4LJ9; X-ray; 1.70 A; A=520-854.
DR PDB; 4LJA; X-ray; 2.00 A; A=520-854.
DR PDBsum; 1QVR; -.
DR PDBsum; 4FCT; -.
DR PDBsum; 4FCV; -.
DR PDBsum; 4FCW; -.
DR PDBsum; 4FD2; -.
DR PDBsum; 4HSE; -.
DR PDBsum; 4LJ4; -.
DR PDBsum; 4LJ5; -.
DR PDBsum; 4LJ6; -.
DR PDBsum; 4LJ7; -.
DR PDBsum; 4LJ8; -.
DR PDBsum; 4LJ9; -.
DR PDBsum; 4LJA; -.
DR AlphaFoldDB; Q9RA63; -.
DR SMR; Q9RA63; -.
DR DIP; DIP-41758N; -.
DR IntAct; Q9RA63; 1.
DR MINT; Q9RA63; -.
DR STRING; 300852.55772869; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR PRIDE; Q9RA63; -.
DR EnsemblBacteria; BAD71310; BAD71310; BAD71310.
DR GeneID; 3167975; -.
DR KEGG; ttj:TTHA1487; -.
DR PATRIC; fig|300852.9.peg.1462; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; Q9RA63; -.
DR BRENDA; 3.6.4.10; 2305.
DR EvolutionaryTrace; Q9RA63; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Reference proteome; Repeat; Stress response.
FT CHAIN 1..854
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191195"
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 83..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 151..331
FT /note="NBD1"
FT REGION 332..535
FT /note="Linker"
FT REGION 545..756
FT /note="NBD2"
FT REGION 757..854
FT /note="C-terminal"
FT COILED 382..516
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT BINDING 595..602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT MUTAGEN 167
FT /note="G->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-475."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 204..205
FT /note="KT->AA: Loss of ability to bind ATP. Residual ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT MUTAGEN 270
FT /note="D->N: No effect on ability to bind ATP. Decrease in
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT MUTAGEN 271
FT /note="E->Q: No effect on ability to bind ATP. Increase in
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT MUTAGEN 350
FT /note="V->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-467."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 353
FT /note="G->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-464."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 355
FT /note="R->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-520."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 396
FT /note="L->A: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 460
FT /note="L->A: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 464
FT /note="R->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-353."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 467
FT /note="Q->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-350."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 475
FT /note="R->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-167."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 520
FT /note="E->C: Great decrease in chaperone activity. Retains
FT ATPase activity and oligomerization; when associated with
FT C-355."
FT /evidence="ECO:0000269|PubMed:14567920"
FT MUTAGEN 601..602
FT /note="KT->AA: Loss of ability to bind ATP. Residual ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT MUTAGEN 667
FT /note="D->N: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT MUTAGEN 668
FT /note="E->Q: Decrease in ATPase activity."
FT /evidence="ECO:0000269|PubMed:11741950"
FT CONFLICT 96
FT /note="A -> G (in Ref. 1; BAA81745/BAA96085)"
FT /evidence="ECO:0000305"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:1QVR"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:1QVR"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:1QVR"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:4HSE"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 334..352
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 358..371
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 379..397
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 401..419
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 429..483
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 486..493
FT /evidence="ECO:0007829|PDB:4HSE"
FT HELIX 496..512
FT /evidence="ECO:0007829|PDB:4HSE"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:1QVR"
FT HELIX 523..534
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 543..549
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 564..578
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4LJ5"
FT STRAND 588..595
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:4FCW"
FT HELIX 601..613
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 632..637
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:4FCV"
FT TURN 644..648
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 651..658
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 674..686
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:4LJ4"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 703..707
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 712..721
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 725..739
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 742..745
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 748..753
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 759..769
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 771..779
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 788..798
FT /evidence="ECO:0007829|PDB:4LJ9"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:4LJ9"
FT TURN 805..807
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 808..815
FT /evidence="ECO:0007829|PDB:4LJ9"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:4LJ7"
FT STRAND 834..839
FT /evidence="ECO:0007829|PDB:4LJ9"
FT STRAND 841..847
FT /evidence="ECO:0007829|PDB:4LJ9"
SQ SEQUENCE 854 AA; 96254 MW; FB9A39BB040363E0 CRC64;
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL EKAGADPKAL
KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE LKDRYVAVDT LVLALAEATP
GLPGLEALKG ALKELRGGRT VQTEHAESTY NALEQYGIDL TRLAAEGKLD PVIGRDEEIR
RVIQILLRRT KNNPVLIGEP GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG
AKYRGEFEER LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV HHGVRISDSA
IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP EEIDALERKK LQLEIEREAL
KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR AEWEREREIL RKLREAQHRL DEVRREIELA
ERQYDLNRAA ELRYGELPKL EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK
LLEGEREKLL RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG QLTEAVRRRP
YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR NTVIILTSNL GSPLILEGLQ
KGWPYERIRD EVFKVLQQHF RPEFLNRLDE IVVFRPLTKE QIRQIVEIQL SYLRARLAEK
RISLELTEAA KDFLAERGYD PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG
PAGLVFAVPA RVEA
