ID   CLPX_ECOLI              Reviewed;         424 AA.
AC   P0A6H1; P33138; Q2MBY8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
DE   AltName: Full=ATP-dependent unfoldase ClpX;
GN   Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; Synonyms=lopC;
GN   OrderedLocusNames=b0438, JW0428;
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;
RX   PubMed=8226770; DOI=10.1016/s0021-9258(18)41573-6;
RA   Gottesman S., Clark W.P., de Crecy-Lagard V., Maurizi M.R.;
RT   "ClpX, an alternative subunit for the ATP-dependent Clp protease of
RT   Escherichia coli. Sequence and in vivo activities.";
RL   J. Biol. Chem. 268:22618-22626(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, OPERON, AND ATP-BINDING.
RX   PubMed=8093059; DOI=10.1006/bbrc.1994.2253;
RA   Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.;
RT   "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can
RT   be expressed independently from clpP in Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 203:798-804(1994).
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 2-25, AND CHARACTERIZATION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8226769; DOI=10.1016/s0021-9258(18)41572-4;
RA   Wojtkowiak D., Georgopoulos C., Zylicz M.;
RT   "Isolation and characterization of ClpX, a new ATP-dependent specificity
RT   component of the Clp protease of Escherichia coli.";
RL   J. Biol. Chem. 268:22609-22617(1993).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=7743994; DOI=10.1002/j.1460-2075.1995.tb07179.x;
RA   Wawrzynow A., Wojtkowiak D., Marszalek J., Banecki B., Jonsen M.,
RA   Graves B., Georgopoulos C., Zylicz M.;
RT   "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent
RT   substrate specificity component of the ClpP-ClpX protease, is a novel
RT   molecular chaperone.";
RL   EMBO J. 14:1867-1877(1995).
RN   [8]
RP   FUNCTION.
RX   PubMed=12941278; DOI=10.1016/s0092-8674(03)00612-3;
RA   Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.;
RT   "Linkage between ATP consumption and mechanical unfolding during the
RT   protein processing reactions of an AAA+ degradation machine.";
RL   Cell 114:511-520(2003).
RN   [9]
RP   FUNCTION, SUBSTRATE, AND DISRUPTION PHENOTYPE.
RX   PubMed=15371343; DOI=10.1101/gad.1240104;
RA   Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT   "Modulating substrate choice: the SspB adaptor delivers a regulator of the
RT   extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT   degradation.";
RL   Genes Dev. 18:2292-2301(2004).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17210793; DOI=10.1101/gad.1496707;
RA   Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
RT   "Design principles of the proteolytic cascade governing the sigmaE-mediated
RT   envelope stress response in Escherichia coli: keys to graded, buffered, and
RT   rapid signal transduction.";
RL   Genes Dev. 21:124-136(2007).
RN   [11]
RP   INTERACTION WITH MU DDE-RECOMBINASE A.
RX   PubMed=18406325; DOI=10.1016/j.molcel.2008.02.013;
RA   Abdelhakim A.H., Oakes E.C., Sauer R.T., Baker T.A.;
RT   "Unique contacts direct high-priority recognition of the tetrameric Mu
RT   transposase-DNA complex by the AAA+ unfoldase ClpX.";
RL   Mol. Cell 30:39-50(2008).
RN   [12]
RP   STRUCTURE BY NMR OF 2-61 IN COMPLEX WITH ZINC.
RX   PubMed=14525985; DOI=10.1074/jbc.m307826200;
RA   Donaldson L.W., Wojtyra U., Houry W.A.;
RT   "Solution structure of the dimeric zinc binding domain of the chaperone
RT   ClpX.";
RL   J. Biol. Chem. 278:48991-48996(2003).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-52 IN COMPLEX WITH ZINC AND IN
RP   COMPLEX WITH SSPB, AND SUBUNIT.
RX   PubMed=17258768; DOI=10.1016/j.jmb.2007.01.003;
RA   Park E.Y., Lee B.G., Hong S.B., Kim H.W., Jeon H., Song H.K.;
RT   "Structural basis of SspB-tail recognition by the zinc binding domain of
RT   ClpX.";
RL   J. Mol. Biol. 367:514-526(2007).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP, AND
RP   SUBUNIT.
RX   PubMed=19914167; DOI=10.1016/j.cell.2009.09.034;
RA   Glynn S.E., Martin A., Nager A.R., Baker T.A., Sauer R.T.;
RT   "Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions
RT   in a AAA+ protein-unfolding machine.";
RL   Cell 139:744-756(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP, AND
RP   MUTAGENESIS OF GLU-185 AND ARG-370.
RX   PubMed=23622246; DOI=10.1016/j.cell.2013.03.029;
RA   Stinson B.M., Nager A.R., Glynn S.E., Schmitz K.R., Baker T.A., Sauer R.T.;
RT   "Nucleotide binding and conformational switching in the hexameric ring of a
RT   AAA+ machine.";
RL   Cell 153:628-639(2013).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease. Uses
CC       cycles of ATP binding and hydrolysis to unfold proteins and translocate
CC       them to the ClpP protease. It directs the protease to specific
CC       substrates both with and without the help of adapter proteins such as
CC       SspB. Participates in the final steps of RseA-sigma-E degradation,
CC       liberating sigma-E to induce the extracytoplasmic-stress response. It
CC       may bind to the lambda O substrate protein and present it to the ClpP
CC       protease in a form that can be recognized and readily hydrolyzed by
CC       ClpP. Can perform chaperone functions in the absence of ClpP.
CC       {ECO:0000269|PubMed:12941278, ECO:0000269|PubMed:15371343}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 Zn(2+) ion per subunit.;
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC       that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC       into a disk-like structure with a central cavity, resembling the
CC       structure of eukaryotic proteasomes. Interacts with Mu phage DDE-
CC       recombinase A; this interaction remodels the viral transpososome for
CC       replication. {ECO:0000255|HAMAP-Rule:MF_00175,
CC       ECO:0000269|PubMed:14525985, ECO:0000269|PubMed:17258768,
CC       ECO:0000269|PubMed:18406325, ECO:0000269|PubMed:19914167,
CC       ECO:0000269|PubMed:23622246}.
CC   -!- INTERACTION:
CC       P0A6H1; P0A6G7: clpP; NbExp=5; IntAct=EBI-547386, EBI-370625;
CC       P0A6H1; P0A6H1: clpX; NbExp=9; IntAct=EBI-547386, EBI-547386;
CC       P0A6H1; P0A9A6: ftsZ; NbExp=2; IntAct=EBI-547386, EBI-370963;
CC   -!- INDUCTION: By heat shock. Part of the clpP-clpX operon, clpX can be
CC       expressed individually from its own promoter.
CC       {ECO:0000269|PubMed:8093059}.
CC   -!- DISRUPTION PHENOTYPE: Delayed and decreased induction of the
CC       extracytoplasmic-stress response. {ECO:0000269|PubMed:15371343,
CC       ECO:0000269|PubMed:17210793}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00175}.
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DR   EMBL; L18867; AAA16116.1; -; Unassigned_DNA.
DR   EMBL; Z23278; CAA80816.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40194.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73541.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76218.1; -; Genomic_DNA.
DR   PIR; A48709; A48709.
DR   RefSeq; NP_414972.1; NC_000913.3.
DR   RefSeq; WP_000130305.1; NZ_STEB01000007.1.
DR   PDB; 1OVX; NMR; -; A/B=2-61.
DR   PDB; 2DS5; X-ray; 1.50 A; A/B=2-52.
DR   PDB; 2DS6; X-ray; 2.00 A; A/B=2-52.
DR   PDB; 2DS7; X-ray; 2.50 A; A=2-52.
DR   PDB; 2DS8; X-ray; 1.60 A; A/B=2-52.
DR   PDB; 3HTE; X-ray; 4.03 A; A/B/C/D/E/F=62-424.
DR   PDB; 3HWS; X-ray; 3.25 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I34; X-ray; 4.12 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I4L; X-ray; 3.70 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I5O; X-ray; 4.48 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I63; X-ray; 5.71 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I81; X-ray; 3.82 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I9K; X-ray; 5.00 A; A/B=62-424.
DR   PDB; 6PO1; EM; 4.20 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PO3; EM; 4.28 A; A/B/C/D/E/F=62-424.
DR   PDB; 6POD; EM; 4.05 A; A/B/C/D/E/F=62-424.
DR   PDB; 6POS; EM; 4.12 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PP5; EM; 3.98 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PP6; EM; 4.28 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PP7; EM; 4.05 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PP8; EM; 4.12 A; A/B/C/D/E/F=62-424.
DR   PDB; 6PPE; EM; 3.19 A; 1/2/3/O/P/Q/R/S/T/U/V/X/Y/Z=62-424.
DR   PDB; 6WR2; EM; 2.88 A; A/B/C/D/E/F=62-424.
DR   PDB; 6WRF; EM; 3.14 A; A/B/C/D/E/F=62-424.
DR   PDB; 6WSG; EM; 3.16 A; A/B/C/D/E/F=62-424.
DR   PDB; 8E7V; EM; 3.10 A; A/B/C/D/E/F=62-424.
DR   PDB; 8E8Q; EM; 3.12 A; A/B/C/D/E/F=62-424.
DR   PDB; 8ET3; EM; 3.70 A; A/B/C/D/E/F=1-424.
DR   PDBsum; 1OVX; -.
DR   PDBsum; 2DS5; -.
DR   PDBsum; 2DS6; -.
DR   PDBsum; 2DS7; -.
DR   PDBsum; 2DS8; -.
DR   PDBsum; 3HTE; -.
DR   PDBsum; 3HWS; -.
DR   PDBsum; 4I34; -.
DR   PDBsum; 4I4L; -.
DR   PDBsum; 4I5O; -.
DR   PDBsum; 4I63; -.
DR   PDBsum; 4I81; -.
DR   PDBsum; 4I9K; -.
DR   PDBsum; 6PO1; -.
DR   PDBsum; 6PO3; -.
DR   PDBsum; 6POD; -.
DR   PDBsum; 6POS; -.
DR   PDBsum; 6PP5; -.
DR   PDBsum; 6PP6; -.
DR   PDBsum; 6PP7; -.
DR   PDBsum; 6PP8; -.
DR   PDBsum; 6PPE; -.
DR   PDBsum; 6WR2; -.
DR   PDBsum; 6WRF; -.
DR   PDBsum; 6WSG; -.
DR   PDBsum; 8E7V; -.
DR   PDBsum; 8E8Q; -.
DR   PDBsum; 8ET3; -.
DR   AlphaFoldDB; P0A6H1; -.
DR   EMDB; EMD-20406; -.
DR   EMDB; EMD-20408; -.
DR   EMDB; EMD-20412; -.
DR   EMDB; EMD-20418; -.
DR   EMDB; EMD-20419; -.
DR   EMDB; EMD-20420; -.
DR   EMDB; EMD-20421; -.
DR   EMDB; EMD-20422; -.
DR   EMDB; EMD-20434; -.
DR   EMDB; EMD-21875; -.
DR   EMDB; EMD-21882; -.
DR   EMDB; EMD-21892; -.
DR   EMDB; EMD-27941; -.
DR   EMDB; EMD-27946; -.
DR   SMR; P0A6H1; -.
DR   BioGRID; 4260735; 560.
DR   BioGRID; 849472; 1.
DR   ComplexPortal; CPX-3176; Endopeptidase ClpXP complex.
DR   DIP; DIP-35907N; -.
DR   IntAct; P0A6H1; 35.
DR   STRING; 511145.b0438; -.
DR   MEROPS; X20.004; -.
DR   jPOST; P0A6H1; -.
DR   PaxDb; 511145-b0438; -.
DR   EnsemblBacteria; AAC73541; AAC73541; b0438.
DR   GeneID; 83577598; -.
DR   GeneID; 945083; -.
DR   KEGG; ecj:JW0428; -.
DR   KEGG; eco:b0438; -.
DR   PATRIC; fig|1411691.4.peg.1838; -.
DR   EchoBASE; EB0157; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_6; -.
DR   InParanoid; P0A6H1; -.
DR   OMA; LDTMFDL; -.
DR   OrthoDB; 9804062at2; -.
DR   PhylomeDB; P0A6H1; -.
DR   BioCyc; EcoCyc:EG10159-MONOMER; -.
DR   BioCyc; MetaCyc:EG10159-MONOMER; -.
DR   BRENDA; 3.4.21.92; 2026.
DR   EvolutionaryTrace; P0A6H1; -.
DR   PRO; PR:P0A6H1; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IPI:ComplexPortal.
DR   GO; GO:0009376; C:HslUV protease complex; IDA:CAFA.
DR   GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:CACAO.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:CAFA.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0002020; F:protease binding; IPI:CAFA.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IGI:CACAO.
DR   GO; GO:0030164; P:protein denaturation; IDA:CAFA.
DR   GO; GO:0043335; P:protein unfolding; IDA:CACAO.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR046425; ClpX_bact.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Direct protein sequencing;
KW   Host-virus interaction; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Stress response; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8226769"
FT   CHAIN           2..424
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_0000160352"
FT   DOMAIN          2..56
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250,
FT                   ECO:0000269|PubMed:14525985"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250,
FT                   ECO:0000269|PubMed:14525985"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250,
FT                   ECO:0000269|PubMed:14525985"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250,
FT                   ECO:0000269|PubMed:14525985"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175,
FT                   ECO:0000269|PubMed:19914167, ECO:0000269|PubMed:23622246"
FT   MUTAGEN         185
FT                   /note="E->Q: No ATP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:23622246"
FT   MUTAGEN         370
FT                   /note="R->K: No ATP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:23622246"
FT   CONFLICT        268..274
FT                   /note="IGFGATV -> HWCWRSG (in Ref. 2; CAA80816)"
FT                   /evidence="ECO:0000305"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:2DS5"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:2DS5"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:2DS5"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:2DS5"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:2DS5"
FT   HELIX           67..77
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           82..100
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:6WSG"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           125..135
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6WSG"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           160..168
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:3HWS"
FT   HELIX           173..177
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           205..216
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           254..262
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:6WR2"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           283..287
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           292..298
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           302..306
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          310..313
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           319..327
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            343..345
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          347..350
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           352..365
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           368..370
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           371..379
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           381..386
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   TURN            387..389
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          392..398
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   HELIX           400..404
FT                   /evidence="ECO:0007829|PDB:6WRF"
FT   STRAND          405..407
FT                   /evidence="ECO:0007829|PDB:6WSG"
FT   STRAND          410..413
FT                   /evidence="ECO:0007829|PDB:6WRF"
SQ   SEQUENCE   424 AA;  46356 MW;  9DEF1B0786E42B6F CRC64;
     MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE
     RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP
     TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI
     VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT
     SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL
     IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK
     KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ
     ASGE
//