CLPX_ECOLI
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 03-AUG-2022, entry version 153.
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; Proteobacteria; 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 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 AlphaFoldDB; P0A6H1; -.
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; P0A6H1; -.
DR PRIDE; P0A6H1; -.
DR EnsemblBacteria; AAC73541; AAC73541; b0438.
DR EnsemblBacteria; BAE76218; BAE76218; BAE76218.
DR GeneID; 67416487; -.
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; HYKRVQA; -.
DR PhylomeDB; P0A6H1; -.
DR BioCyc; EcoCyc:EG10159-MON; -.
DR BioCyc; MetaCyc:EG10159-MON; -.
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 Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 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 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; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 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
