TETX_CLOTE
ID TETX_CLOTE Reviewed; 1315 AA.
AC P04958;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tetanus toxin;
DE EC=3.4.24.68;
DE AltName: Full=Tentoxylysin;
DE Contains:
DE RecName: Full=Tetanus toxin light chain;
DE Short=Tetanus toxin chain L;
DE Contains:
DE RecName: Full=Tetanus toxin heavy chain;
DE Short=Tetanus toxin chain H;
DE Flags: Precursor;
GN Name=tetX; OrderedLocusNames=CTC_p60;
OS Clostridium tetani (strain Massachusetts / E88).
OG Plasmid pE88, and Plasmid 75 Kbp.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=75 Kbp;
RX PubMed=3536478; DOI=10.1002/j.1460-2075.1986.tb04527.x;
RA Eisel U., Jarausch W., Goretzki K., Henschen A., Engels J., Weller U.,
RA Hudel M., Habermann E., Niemann H.;
RT "Tetanus toxin: primary structure, expression in E. coli, and homology with
RT botulinum toxins.";
RL EMBO J. 5:2495-2502(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CN3911; PLASMID=75 Kbp;
RX PubMed=3774547; DOI=10.1093/nar/14.19.7809;
RA Fairweather N.F., Lyness V.A.;
RT "The complete nucleotide sequence of tetanus toxin.";
RL Nucleic Acids Res. 14:7809-7812(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88; PLASMID=pE88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 743-1315.
RC PLASMID=75 Kbp;
RX PubMed=3510187; DOI=10.1128/jb.165.1.21-27.1986;
RA Fairweather N.F., Lyness V.A., Pickard D.J., Allen G., Thomson R.O.;
RT "Cloning, nucleotide sequencing, and expression of tetanus toxin fragment C
RT in Escherichia coli.";
RL J. Bacteriol. 165:21-27(1986).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=2108021; DOI=10.1111/j.1432-1033.1990.tb15368.x;
RA Krieglstein K., Henschen A., Weller U., Habermann E.;
RT "Arrangement of disulfide bridges and positions of sulfhydryl groups in
RT tetanus toxin.";
RL Eur. J. Biochem. 188:39-45(1990).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1935979; DOI=10.1111/j.1432-1033.1991.tb16342.x;
RA Krieglstein K.G., Henschen A.H., Weller U., Habermann E.;
RT "Limited proteolysis of tetanus toxin. Relation to activity and
RT identification of cleavage sites.";
RL Eur. J. Biochem. 202:41-51(1991).
RN [7]
RP IDENTIFICATION AS A ZINC-PROTEASE.
RX PubMed=1396558; DOI=10.1002/j.1460-2075.1992.tb05441.x;
RA Schiavo G., Poulain B., Rossetto O., Benfenati F., Tauc L., Montecucco C.;
RT "Tetanus toxin is a zinc protein and its inhibition of neurotransmitter
RT release and protease activity depend on zinc.";
RL EMBO J. 11:3577-3583(1992).
RN [8]
RP IDENTIFICATION OF SUBSTRATE.
RX PubMed=1331807; DOI=10.1038/359832a0;
RA Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P.,
RA Dasgupta B.R., Montecucco C.;
RT "Tetanus and botulinum-B neurotoxins block neurotransmitter release by
RT proteolytic cleavage of synaptobrevin.";
RL Nature 359:832-835(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 875-1315.
RX PubMed=9334741; DOI=10.1038/nsb1097-788;
RA Umland T.C., Wingert L.M., Swaminathan S., Furey W.F. Jr., Schmidt J.J.,
RA Sax M.;
RT "Structure of the receptor binding fragment HC of tetanus neurotoxin.";
RL Nat. Struct. Biol. 4:788-792(1997).
CC -!- FUNCTION: Tetanus toxin acts by inhibiting neurotransmitter release. It
CC binds to peripheral neuronal synapses, is internalized and moves by
CC retrograde transport up the axon into the spinal cord where it can move
CC between postsynaptic and presynaptic neurons. It inhibits
CC neurotransmitter release by acting as a zinc endopeptidase that
CC catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of
CC synaptobrevin-2.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.;
CC EC=3.4.24.68;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: The precursor polypeptide is subsequently cleaved to yield
CC subchains L and H. These remain linked by a disulfide bridge and are
CC non-toxic after separation.
CC -!- INTERACTION:
CC P04958; P0DMV8: HSPA1A; Xeno; NbExp=3; IntAct=EBI-13951617, EBI-11052499;
CC -!- MISCELLANEOUS: The C-terminus of the heavy chain binds to ganglioside
CC receptors.
CC -!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Tetanus toxin Hc fragment;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_other_381";
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DR EMBL; X04436; CAA28033.1; -; Genomic_DNA.
DR EMBL; X06214; CAA29564.1; -; Genomic_DNA.
DR EMBL; AF528097; AAO37454.1; -; Genomic_DNA.
DR EMBL; M12739; AAA23282.1; -; Genomic_DNA.
DR PIR; A25689; BTCLTN.
DR RefSeq; WP_011100836.1; NC_004565.1.
DR PDB; 1A8D; X-ray; 1.57 A; A=865-1315.
DR PDB; 1AF9; X-ray; 2.70 A; A=865-1315.
DR PDB; 1D0H; X-ray; 2.10 A; A=872-1315.
DR PDB; 1DFQ; X-ray; 2.60 A; A=872-1315.
DR PDB; 1DIW; X-ray; 2.00 A; A=875-1315.
DR PDB; 1DLL; X-ray; 1.80 A; A=875-1315.
DR PDB; 1FV2; X-ray; 2.50 A; A=862-1315.
DR PDB; 1FV3; X-ray; 2.30 A; A/B=862-1315.
DR PDB; 1YVG; X-ray; 2.60 A; A=2-458.
DR PDB; 1YXW; X-ray; 2.20 A; A=875-1315.
DR PDB; 1YYN; X-ray; 2.30 A; A=875-1315.
DR PDB; 1Z7H; X-ray; 2.30 A; A=1-443.
DR PDB; 3HMY; X-ray; 2.00 A; A=866-1315.
DR PDB; 3HN1; X-ray; 2.10 A; A=866-1315.
DR PDB; 4J1L; X-ray; 2.60 A; A=2-427.
DR PDB; 5N0B; X-ray; 2.60 A; A=1-1315.
DR PDB; 5N0C; X-ray; 2.60 A; A/B=1-1315.
DR PDB; 7BXX; Other; 2.34 A; A/B=459-864.
DR PDB; 7BY4; X-ray; 1.50 A; A=865-1315.
DR PDB; 7BY5; X-ray; 2.27 A; A=2-1315.
DR PDBsum; 1A8D; -.
DR PDBsum; 1AF9; -.
DR PDBsum; 1D0H; -.
DR PDBsum; 1DFQ; -.
DR PDBsum; 1DIW; -.
DR PDBsum; 1DLL; -.
DR PDBsum; 1FV2; -.
DR PDBsum; 1FV3; -.
DR PDBsum; 1YVG; -.
DR PDBsum; 1YXW; -.
DR PDBsum; 1YYN; -.
DR PDBsum; 1Z7H; -.
DR PDBsum; 3HMY; -.
DR PDBsum; 3HN1; -.
DR PDBsum; 4J1L; -.
DR PDBsum; 5N0B; -.
DR PDBsum; 5N0C; -.
DR PDBsum; 7BXX; -.
DR PDBsum; 7BY4; -.
DR PDBsum; 7BY5; -.
DR AlphaFoldDB; P04958; -.
DR SASBDB; P04958; -.
DR SMR; P04958; -.
DR IntAct; P04958; 2.
DR BindingDB; P04958; -.
DR ChEMBL; CHEMBL2036; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02265; Ethyl-Trimethyl-Silane.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR DrugBank; DB04265; N-acetyl-beta-neuraminic acid.
DR DrugBank; DB11604; Tetanus immune globulin, human.
DR Allergome; 2757; Clo t Toxoid.
DR MEROPS; M27.001; -.
DR TCDB; 1.C.8.1.2; the botulinum and tetanus toxin (btt) family.
DR UniLectin; P04958; -.
DR ABCD; P04958; 12 sequenced antibodies.
DR EnsemblBacteria; AAO37454; AAO37454; CTC_p60.
DR KEGG; ctc:CTC_p60; -.
DR HOGENOM; CLU_262205_0_0_9; -.
DR OMA; VSFWIRI; -.
DR OrthoDB; 50987at2; -.
DR BRENDA; 3.4.24.68; 1526.
DR Reactome; R-HSA-5250982; Toxicity of tetanus toxin (tetX).
DR EvolutionaryTrace; P04958; -.
DR PRO; PR:P04958; -.
DR Proteomes; UP000001412; Plasmid pE88.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:CACAO.
DR GO; GO:0008320; F:protein transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IDA:CACAO.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1120.10; -; 1.
DR InterPro; IPR000395; Bot/tetX_LC.
DR InterPro; IPR036248; Clostridium_toxin_transloc.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR013104; Toxin_rcpt-bd_C.
DR InterPro; IPR012928; Toxin_rcpt-bd_N.
DR InterPro; IPR012500; Toxin_trans.
DR Pfam; PF01742; Peptidase_M27; 1.
DR Pfam; PF07951; Toxin_R_bind_C; 1.
DR Pfam; PF07953; Toxin_R_bind_N; 1.
DR Pfam; PF07952; Toxin_trans; 1.
DR PRINTS; PR00760; BONTOXILYSIN.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR SUPFAM; SSF58091; SSF58091; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Neurotoxin; Plasmid; Protease;
KW Reference proteome; Toxin; Virulence; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..457
FT /note="Tetanus toxin light chain"
FT /id="PRO_0000029229"
FT CHAIN 458..1315
FT /note="Tetanus toxin heavy chain"
FT /id="PRO_0000029230"
FT ACT_SITE 234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 439..467
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000269|PubMed:2108021"
FT DISULFID 1077..1093
FT /evidence="ECO:0000269|PubMed:2108021"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:5N0B"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 285..307
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1Z7H"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1Z7H"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4J1L"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:1YVG"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:7BY5"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1Z7H"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 509..517
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:5N0B"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 560..565
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:5N0B"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 597..603
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 612..627
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 646..650
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 661..668
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 697..729
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 731..761
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 768..806
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 808..834
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 836..839
FT /evidence="ECO:0007829|PDB:7BY5"
FT HELIX 841..854
FT /evidence="ECO:0007829|PDB:7BY5"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:5N0C"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:5N0C"
FT HELIX 877..883
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 885..892
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 895..898
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 900..902
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 913..917
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 920..928
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 933..936
FT /evidence="ECO:0007829|PDB:7BY4"
FT HELIX 939..941
FT /evidence="ECO:0007829|PDB:1A8D"
FT TURN 942..947
FT /evidence="ECO:0007829|PDB:1A8D"
FT STRAND 950..957
FT /evidence="ECO:0007829|PDB:7BY4"
FT HELIX 963..969
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 973..978
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 983..986
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 990..996
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 999..1005
FT /evidence="ECO:0007829|PDB:7BY4"
FT TURN 1007..1009
FT /evidence="ECO:0007829|PDB:1FV3"
FT STRAND 1011..1017
FT /evidence="ECO:0007829|PDB:7BY4"
FT TURN 1022..1024
FT /evidence="ECO:0007829|PDB:1DLL"
FT STRAND 1026..1030
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1032..1038
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1042..1048
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1051..1057
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1068..1076
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1083..1094
FT /evidence="ECO:0007829|PDB:7BY4"
FT HELIX 1098..1107
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1111..1113
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1119..1121
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1123..1125
FT /evidence="ECO:0007829|PDB:1DLL"
FT STRAND 1127..1132
FT /evidence="ECO:0007829|PDB:7BY4"
FT HELIX 1133..1135
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1138..1144
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1149..1153
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1156..1159
FT /evidence="ECO:0007829|PDB:7BY4"
FT TURN 1160..1163
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1174..1181
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1194..1202
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1205..1212
FT /evidence="ECO:0007829|PDB:7BY4"
FT TURN 1219..1221
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1222..1224
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1226..1228
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1232..1234
FT /evidence="ECO:0007829|PDB:5N0C"
FT STRAND 1239..1243
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1253..1258
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1260..1262
FT /evidence="ECO:0007829|PDB:1A8D"
FT STRAND 1264..1273
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1281..1287
FT /evidence="ECO:0007829|PDB:7BY4"
FT HELIX 1288..1292
FT /evidence="ECO:0007829|PDB:7BY4"
FT TURN 1293..1295
FT /evidence="ECO:0007829|PDB:1FV2"
FT STRAND 1296..1298
FT /evidence="ECO:0007829|PDB:7BY4"
FT STRAND 1303..1306
FT /evidence="ECO:0007829|PDB:7BY4"
SQ SEQUENCE 1315 AA; 150682 MW; 18838FB2654024CF CRC64;
MPITINNFRY SDPVNNDTII MMEPPYCKGL DIYYKAFKIT DRIWIVPERY EFGTKPEDFN
PPSSLIEGAS EYYDPNYLRT DSDKDRFLQT MVKLFNRIKN NVAGEALLDK IINAIPYLGN
SYSLLDKFDT NSNSVSFNLL EQDPSGATTK SAMLTNLIIF GPGPVLNKNE VRGIVLRVDN
KNYFPCRDGF GSIMQMAFCP EYVPTFDNVI ENITSLTIGK SKYFQDPALL LMHELIHVLH
GLYGMQVSSH EIIPSKQEIY MQHTYPISAE ELFTFGGQDA NLISIDIKND LYEKTLNDYK
AIANKLSQVT SCNDPNIDID SYKQIYQQKY QFDKDSNGQY IVNEDKFQIL YNSIMYGFTE
IELGKKFNIK TRLSYFSMNH DPVKIPNLLD DTIYNDTEGF NIESKDLKSE YKGQNMRVNT
NAFRNVDGSG LVSKLIGLCK KIIPPTNIRE NLYNRTASLT DLGGELCIKI KNEDLTFIAE
KNSFSEEPFQ DEIVSYNTKN KPLNFNYSLD KIIVDYNLQS KITLPNDRTT PVTKGIPYAP
EYKSNAASTI EIHNIDDNTI YQYLYAQKSP TTLQRITMTN SVDDALINST KIYSYFPSVI
SKVNQGAQGI LFLQWVRDII DDFTNESSQK TTIDKISDVS TIVPYIGPAL NIVKQGYEGN
FIGALETTGV VLLLEYIPEI TLPVIAALSI AESSTQKEKI IKTIDNFLEK RYEKWIEVYK
LVKAKWLGTV NTQFQKRSYQ MYRSLEYQVD AIKKIIDYEY KIYSGPDKEQ IADEINNLKN
KLEEKANKAM ININIFMRES SRSFLVNQMI NEAKKQLLEF DTQSKNILMQ YIKANSKFIG
ITELKKLESK INKVFSTPIP FSYSKNLDCW VDNEEDIDVI LKKSTILNLD INNDIISDIS
GFNSSVITYP DAQLVPGING KAIHLVNNES SEVIVHKAMD IEYNDMFNNF TVSFWLRVPK
VSASHLEQYG TNEYSIISSM KKHSLSIGSG WSVSLKGNNL IWTLKDSAGE VRQITFRDLP
DKFNAYLANK WVFITITNDR LSSANLYING VLMGSAEITG LGAIREDNNI TLKLDRCNNN
NQYVSIDKFR IFCKALNPKE IEKLYTSYLS ITFLRDFWGN PLRYDTEYYL IPVASSSKDV
QLKNITDYMY LTNAPSYTNG KLNIYYRRLY NGLKFIIKRY TPNNEIDSFV KSGDFIKLYV
SYNNNEHIVG YPKDGNAFNN LDRILRVGYN APGIPLYKKM EAVKLRDLKT YSVQLKLYDD
KNASLGLVGT HNGQIGNDPN RDILIASNWY FNHLKDKILG CDWYFVPTDE GWTND
