TOXA_PSEAE
ID TOXA_PSEAE Reviewed; 638 AA.
AC P11439; Q9I4I7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Exotoxin A {ECO:0000303|PubMed:6201861};
DE Short=ETA {ECO:0000303|PubMed:6201861};
DE EC=2.4.2.36 {ECO:0000269|PubMed:2170123};
DE AltName: Full=NAD(+)--diphthamide ADP-ribosyltransferase;
DE AltName: Full=Pseudomonas exotoxin {ECO:0000303|PubMed:2118903};
DE Short=PE {ECO:0000303|PubMed:2118903};
DE Flags: Precursor;
GN Name=eta {ECO:0000303|PubMed:6201861}; OrderedLocusNames=PA1148;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-53.
RX PubMed=6201861; DOI=10.1073/pnas.81.9.2645;
RA Gray G.L., Smith D.H., Baldridge J.S., Harkins R.N., Vasil M.L., Chen E.Y.,
RA Heyneker H.L.;
RT "Cloning, nucleotide sequence, and expression in Escherichia coli of the
RT exotoxin A structural gene of Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2645-2649(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP ACTIVE SITE.
RX PubMed=2885323; DOI=10.1016/s0021-9258(18)47472-8;
RA Carroll S.F., Collier R.J.;
RT "Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is
RT photolabeled by NAD and shows functional homology with glutamic acid 148 of
RT diphtheria toxin.";
RL J. Biol. Chem. 262:8707-8711(1987).
RN [4]
RP DOMAINS, AND MUTAGENESIS OF LYS-82; 266-PRO--PHE-275 AND 271-HIS--HIS-274.
RX PubMed=2118903; DOI=10.1016/s0021-9258(17)46223-5;
RA Chaudhary V.K., Jinno Y., Galo M.G., Fitzgerald D., Pastan I.;
RT "Mutagenesis of Pseudomonas exotoxin in identification of sequences
RT responsible for the animal toxicity.";
RL J. Biol. Chem. 265:16306-16310(1990).
RN [5]
RP PROTEIN SEQUENCE OF 396-408 AND 415-424, FUNCTION, CATALYTIC ACTIVITY, AND
RP DOMAINS.
RX PubMed=2170123; DOI=10.1111/j.1432-1033.1990.tb19238.x;
RA Bourdenet S., Vacheron M.-J., Guinand M., Michel G., Arminjon F.;
RT "Biochemical and immunochemical studies of proteolytic fragments of
RT exotoxin A from Pseudomonas aeruginosa.";
RL Eur. J. Biochem. 192:379-385(1990).
RN [6]
RP RECEPTOR-BINDING, AND MUTAGENESIS OF LYS-82.
RX PubMed=1618748; DOI=10.1016/s0021-9258(18)42291-0;
RA Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K.,
RA Saelinger C.B.;
RT "The alpha 2-macroglobulin receptor/low density lipoprotein receptor-
RT related protein binds and internalizes Pseudomonas exotoxin A.";
RL J. Biol. Chem. 267:12420-12423(1992).
RN [7]
RP DISULFIDE BOND.
RX PubMed=10600112; DOI=10.1021/bi991308+;
RA McKee M.L., FitzGerald D.J.;
RT "Reduction of furin-nicked Pseudomonas exotoxin A: an unfolding story.";
RL Biochemistry 38:16507-16513(1999).
RN [8]
RP FUNCTION AS A TOXIN, FUNCTION AS A GLYCOHYDROLASE, FUNCTION AS AN
RP ADP-RIBOSYLTRANSFERASE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-578.
RX PubMed=18276581; DOI=10.1074/jbc.m710008200;
RA Jorgensen R., Purdy A.E., Fieldhouse R.J., Kimber M.S., Bartlett D.H.,
RA Merrill A.R.;
RT "Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae.";
RL J. Biol. Chem. 283:10671-10678(2008).
RN [9]
RP ACTIVITY REGULATION, AND TOXIC DOSE.
RX PubMed=21135177; DOI=10.1128/aac.01164-10;
RA Turgeon Z., Jorgensen R., Visschedyk D., Edwards P.R., Legree S.,
RA McGregor C., Fieldhouse R.J., Mangroo D., Schapira M., Merrill A.R.;
RT "Newly discovered and characterized antivirulence compounds inhibit
RT bacterial mono-ADP-ribosyltransferase toxins.";
RL Antimicrob. Agents Chemother. 55:983-991(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 424-638.
RX PubMed=7568123; DOI=10.1073/pnas.92.20.9308;
RA Li M., Dyda F., Benhar I., Pastan I., Davies D.R.;
RT "The crystal structure of Pseudomonas aeruginosa exotoxin domain III with
RT nicotinamide and AMP: conformational differences with the intact
RT exotoxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9308-9312(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 424-638.
RX PubMed=8692916; DOI=10.1073/pnas.93.14.6902;
RA Li M., Dyda F., Benhar I., Pastan I., Davies D.R.;
RT "Crystal structure of the catalytic domain of Pseudomonas exotoxin A
RT complexed with a nicotinamide adenine dinucleotide analog: implications for
RT the activation process and for ADP ribosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6902-6906(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 425-630 IN COMPLEX WITH YEAST
RP EEF2 AND NAD, AND MUTAGENESIS OF ARG-481; GLU-571; ARG-576 AND GLU-578.
RX PubMed=18583986; DOI=10.1038/embor.2008.90;
RA Jorgensen R., Wang Y., Visschedyk D., Merrill A.R.;
RT "The nature and character of the transition state for the ADP-
RT ribosyltransferase reaction.";
RL EMBO Rep. 9:802-809(2008).
CC -!- FUNCTION: An NAD-dependent ADP-ribosyltransferase (ADPRT). Catalyzes
CC the transfer of the ADP ribosyl moiety of oxidized NAD (NAD(+)) onto
CC eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis
CC (PubMed:2170123, PubMed:18276581). Has an LD(50) of 65 ng/ml against
CC the human lung epithelial cell line C38 (PubMed:21135177).
CC {ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:21135177,
CC ECO:0000269|PubMed:2170123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphthamide-[translation elongation factor 2] + NAD(+) = H(+)
CC + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] +
CC nicotinamide; Xref=Rhea:RHEA:11820, Rhea:RHEA-COMP:10174, Rhea:RHEA-
CC COMP:10175, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:82697; EC=2.4.2.36;
CC Evidence={ECO:0000269|PubMed:18276581, ECO:0000269|PubMed:2170123};
CC -!- ACTIVITY REGULATION: Inhibited by 1,8-naphthalimide (NAP) as well as a
CC number of poly(ADP-ribose) polymerase inhibitors and other compounds.
CC {ECO:0000269|PubMed:21135177}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=121 uM for NAD;
CC Note=For ADP-ribosyltransferase activity of the catalytic fragment
CC 399-605.;
CC -!- DOMAIN: Domain I (which is divided into 2 non-contiguous regions Ia and
CC Ib) is required for binding to cells, but not for ADPRT activity
CC (Probable) (PubMed:2170123). A subtilisin-digested fragment starting
CC about residue 417 and extending to the C-terminus has full ADPRT
CC activity (PubMed:2170123). {ECO:0000269|PubMed:2170123,
CC ECO:0000305|PubMed:2118903}.
CC -!- PTM: The 8 cysteines participate in intrachain disulfide bonds.
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DR EMBL; K01397; AAB59097.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04537.1; -; Genomic_DNA.
DR PIR; A30347; A30347.
DR PIR; C83503; C83503.
DR RefSeq; NP_249839.1; NC_002516.2.
DR RefSeq; WP_003112478.1; NZ_QZGE01000006.1.
DR PDB; 1AER; X-ray; 2.30 A; A/B=425-634.
DR PDB; 1DMA; X-ray; 2.50 A; A/B=425-638.
DR PDB; 1IKP; X-ray; 1.45 A; A=26-638.
DR PDB; 1IKQ; X-ray; 1.62 A; A=26-638.
DR PDB; 1XK9; X-ray; 2.10 A; A/B=424-638.
DR PDB; 1ZM2; X-ray; 3.07 A; B/D/F=424-630.
DR PDB; 1ZM3; X-ray; 3.07 A; B/D/F=424-630.
DR PDB; 1ZM4; X-ray; 2.90 A; B/D/F=424-630.
DR PDB; 1ZM9; X-ray; 2.80 A; B/D/F=424-630.
DR PDB; 2ZIT; X-ray; 3.00 A; B/D/F=425-630.
DR PDB; 3B78; X-ray; 2.50 A; B/D/F=425-630.
DR PDB; 3B82; X-ray; 2.35 A; B/D/F=425-630.
DR PDB; 3B8H; X-ray; 2.50 A; B/D/F=425-630.
DR PDBsum; 1AER; -.
DR PDBsum; 1DMA; -.
DR PDBsum; 1IKP; -.
DR PDBsum; 1IKQ; -.
DR PDBsum; 1XK9; -.
DR PDBsum; 1ZM2; -.
DR PDBsum; 1ZM3; -.
DR PDBsum; 1ZM4; -.
DR PDBsum; 1ZM9; -.
DR PDBsum; 2ZIT; -.
DR PDBsum; 3B78; -.
DR PDBsum; 3B82; -.
DR PDBsum; 3B8H; -.
DR AlphaFoldDB; P11439; -.
DR SMR; P11439; -.
DR STRING; 287.DR97_786; -.
DR DrugBank; DB02701; Nicotinamide.
DR DrugBank; DB08348; N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE.
DR TCDB; 1.C.73.1.1; the pseudomonas exotoxin a (p-exoa) family.
DR PaxDb; P11439; -.
DR ABCD; P11439; 2 sequenced antibodies.
DR EnsemblBacteria; AAG04537; AAG04537; PA1148.
DR GeneID; 877850; -.
DR KEGG; pae:PA1148; -.
DR PATRIC; fig|208964.12.peg.1194; -.
DR PseudoCAP; PA1148; -.
DR HOGENOM; CLU_426954_0_0_6; -.
DR OMA; HESNEMQ; -.
DR BioCyc; MetaCyc:MON-15587; -.
DR BioCyc; PAER208964:G1FZ6-1174-MON; -.
DR BRENDA; 2.4.2.36; 5087.
DR SABIO-RK; P11439; -.
DR EvolutionaryTrace; P11439; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0047286; F:NAD+-diphthamide ADP-ribosyltransferase activity; IDA:CACAO.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd01436; Dipth_tox_like; 1.
DR Gene3D; 3.90.1350.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR015185; Exotox-A_bind.
DR InterPro; IPR015099; Exotox-A_cataly_dom.
DR InterPro; IPR015186; Exotox-A_middle_dom.
DR InterPro; IPR036478; Exotox-A_middle_dom_sf.
DR Pfam; PF09101; Exotox-A_bind; 1.
DR Pfam; PF09009; Exotox-A_cataly; 1.
DR Pfam; PF09102; Exotox-A_target; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56864; SSF56864; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Glycosyltransferase; NAD; Nucleotidyltransferase; Reference proteome;
KW Signal; Toxin; Transferase; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:6201861"
FT CHAIN 26..638
FT /note="Exotoxin A"
FT /id="PRO_0000019365"
FT REGION 26..277
FT /note="Domain Ia (required for target cell recognition)"
FT /evidence="ECO:0000305|PubMed:2118903"
FT REGION 278..389
FT /note="II (required for translocation in target cell
FT cytoplasm)"
FT REGION 390..429
FT /note="Domain Ib"
FT REGION 430..638
FT /note="III (required for ADP-ribosyl activity)"
FT REGION 596..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 578
FT /evidence="ECO:0000269|PubMed:2885323"
FT BINDING 465..467
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18583986"
FT BINDING 474
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18583986"
FT BINDING 479..485
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18583986"
FT BINDING 578
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18583986"
FT DISULFID 290..312
FT /evidence="ECO:0000269|PubMed:10600112"
FT MUTAGEN 82
FT /note="K->E: Loss of toxicity, no binding to LRP1 receptor.
FT 100-fold less cytotoxic, 5-fold less toxic in mice."
FT /evidence="ECO:0000269|PubMed:1618748,
FT ECO:0000269|PubMed:2118903"
FT MUTAGEN 266..275
FT /note="Missing: Loss of cytotoxicity; when associated with
FT E-82."
FT /evidence="ECO:0000269|PubMed:2118903"
FT MUTAGEN 271..274
FT /note="HRLH->EELE: Slight decrease in cytotoxicity. Loss of
FT cytotoxicity, 150-fold less toxic in mice; when associated
FT with E-82."
FT /evidence="ECO:0000269|PubMed:2118903"
FT MUTAGEN 271..274
FT /note="HRLH->GGLG: Loss of cytotoxicity; when associated
FT with E-82."
FT /evidence="ECO:0000269|PubMed:2118903"
FT MUTAGEN 271..274
FT /note="HRLH->KKLK: 100-fold reduction of cytotoxicity; when
FT associated with E-82."
FT /evidence="ECO:0000269|PubMed:2118903"
FT MUTAGEN 481
FT /note="R->H: 52-fold decrease in ADPRT activity, 55-fold
FT reduction in GH activity, 31-fold increase in dissociation
FT constant for NAD(+)."
FT /evidence="ECO:0000269|PubMed:18583986"
FT MUTAGEN 571
FT /note="E->A: 833-fold decrease in ADPRT activity, 4-fold
FT reduction in GH activity, 2-fold increase in dissociation
FT constant for NAD(+)."
FT /evidence="ECO:0000269|PubMed:18583986"
FT MUTAGEN 576
FT /note="R->A: 2-fold decrease in ADPRT activity, 14-fold
FT reduction in GH activity, 3-fold increase in dissociation
FT constant for NAD(+)."
FT /evidence="ECO:0000269|PubMed:18583986"
FT MUTAGEN 578
FT /note="E->A: 666-fold decrease in ADPRT activity, 14-fold
FT reduction in GH activity, 2-fold increase in dissociation
FT constant for NAD(+), loss of toxicity against mouse cells."
FT /evidence="ECO:0000269|PubMed:18276581,
FT ECO:0000269|PubMed:18583986"
FT CONFLICT 4
FT /note="T -> I (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="F -> S (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="A -> T (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="S -> N (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="I -> V (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="G -> S (in Ref. 1; AAB59097)"
FT /evidence="ECO:0000305"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:1IKP"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1IKP"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 189..201
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:1IKP"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 358..376
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:1DMA"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1DMA"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 469..477
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 522..529
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:3B8H"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:1DMA"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 583..587
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:1IKP"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:1IKP"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:1IKP"
SQ SEQUENCE 638 AA; 69284 MW; 7B9AAD56A27C700A CRC64;
MHLTPHWIPL VASLGLLAGG SFASAAEEAF DLWNECAKAC VLDLKDGVRS SRMSVDPAIA
DTNGQGVLHY SMVLEGGNDA LKLAIDNALS ITSDGLTIRL EGGVEPNKPV RYSYTRQARG
SWSLNWLVPI GHEKPSNIKV FIHELNAGNQ LSHMSPIYTI EMGDELLAKL ARDATFFVRA
HESNEMQPTL AISHAGVSVV MAQAQPRREK RWSEWASGKV LCLLDPLDGV YNYLAQQRCN
LDDTWEGKIY RVLAGNPAKH DLDIKPTVIS HRLHFPEGGS LAALTAHQAC HLPLETFTRH
RQPRGWEQLE QCGYPVQRLV ALYLAARLSW NQVDQVIRNA LASPGSGGDL GEAIREQPEQ
ARLALTLAAA ESERFVRQGT GNDEAGAASA DVVSLTCPVA AGECAGPADS GDALLERNYP
TGAEFLGDGG DISFSTRGTQ NWTVERLLQA HRQLEERGYV FVGYHGTFLE AAQSIVFGGV
RARSQDLDAI WRGFYIAGDP ALAYGYAQDQ EPDARGRIRN GALLRVYVPR SSLPGFYRTG
LTLAAPEAAG EVERLIGHPL PLRLDAITGP EEEGGRLETI LGWPLAERTV VIPSAIPTDP
RNVGGDLDPS SIPDKEQAIS ALPDYASQPG KPPREDLK
