YESX_BACSU
ID YESX_BACSU Reviewed; 612 AA.
AC O31527;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Rhamnogalacturonan exolyase YesX;
DE EC=4.2.2.24 {ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
GN Name=yesX; OrderedLocusNames=BSU07060;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
RN [3] {ECO:0007744|PDB:2ZUY}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND DELETION
RP MUTAGENESIS OF 439-PRO--TYR-447.
RC STRAIN=168 {ECO:0000303|PubMed:19193638};
RX PubMed=19193638; DOI=10.1074/jbc.m807799200;
RA Ochiai A., Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Structural determinants responsible for substrate recognition and mode of
RT action in family 11 polysaccharide lyases.";
RL J. Biol. Chem. 284:10181-10189(2009).
CC -!- FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan
CC from plant cell walls and releases disaccharide products
CC (PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan,
CC polygalacturonic acid and pectic acid. Has very low activity on pectin
CC (PubMed:17449691). {ECO:0000269|PubMed:17449691,
CC ECO:0000269|PubMed:19193638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I oligosaccharides containing alpha-L-
CC rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-
CC galactopyranosyluronic acid at the non-reducing end. The products are
CC the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-
CC alpha-L-rhamnopyranose and the shortened rhamnogalacturonan
CC oligosaccharide containing one 4-deoxy-4,5-unsaturated D-
CC galactopyranosyluronic acid at the non-reducing end.; EC=4.2.2.24;
CC Evidence={ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17449691};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17449691};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17449691};
CC Note=Divalent metal cations. Has highest activity with Mn(2+), followed
CC by Zn(2+) and Co(2+). {ECO:0000269|PubMed:17449691};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
CC Note=Binds 10 calcium ions. The calcium may have a structural role.
CC {ECO:0000269|PubMed:17449691};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.78 mg/ml for rhamnogalacturonan (RG) type I region of plant cell
CC wall pectin {ECO:0000269|PubMed:19193638};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17449691};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:17449691};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17449691}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 11 family.
CC {ECO:0000305}.
CC -!- CAUTION: This enzyme is expected to be secreted, but there is no
CC predicted signal sequence. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL009126; CAB12525.1; -; Genomic_DNA.
DR PIR; G69797; G69797.
DR RefSeq; NP_388587.1; NC_000964.3.
DR RefSeq; WP_010886437.1; NZ_CP053102.1.
DR PDB; 2ZUY; X-ray; 1.65 A; A=1-612.
DR PDBsum; 2ZUY; -.
DR AlphaFoldDB; O31527; -.
DR SMR; O31527; -.
DR STRING; 224308.BSU07060; -.
DR CAZy; PL11; Polysaccharide Lyase Family 11.
DR PaxDb; O31527; -.
DR PRIDE; O31527; -.
DR EnsemblBacteria; CAB12525; CAB12525; BSU_07060.
DR GeneID; 936081; -.
DR KEGG; bsu:BSU07060; -.
DR PATRIC; fig|224308.43.peg.744; -.
DR eggNOG; COG3401; Bacteria.
DR InParanoid; O31527; -.
DR OMA; DGLMWGD; -.
DR PhylomeDB; O31527; -.
DR BioCyc; BSUB:BSU07060-MON; -.
DR BioCyc; MetaCyc:BSU07060-MON; -.
DR BRENDA; 4.2.2.24; 658.
DR SABIO-RK; O31527; -.
DR EvolutionaryTrace; O31527; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd10318; RGL11; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR041624; RGI_lyase.
DR InterPro; IPR034641; RGL11.
DR PANTHER; PTHR43118; PTHR43118; 1.
DR Pfam; PF18370; RGI_lyase; 1.
DR SUPFAM; SSF69318; SSF69318; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Lyase; Metal-binding; Reference proteome;
KW Repeat; Secreted.
FT CHAIN 1..612
FT /note="Rhamnogalacturonan exolyase YesX"
FT /id="PRO_0000360213"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 516..518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 533
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 533
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31526"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUY"
FT MUTAGEN 439..447
FT /note="Missing: Changes the activity from exo- to endo-
FT cleavage."
FT /evidence="ECO:0000269|PubMed:19193638"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2ZUY"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2ZUY"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2ZUY"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:2ZUY"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:2ZUY"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:2ZUY"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:2ZUY"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:2ZUY"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:2ZUY"
FT HELIX 568..574
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:2ZUY"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:2ZUY"
SQ SEQUENCE 612 AA; 67690 MW; E7A320888A608D4B CRC64;
MKPKKRQMEY LTRGLIAVQT EQGVFVSWRF LGTDHETTAF HLYRDGKRIT RDPIAESTNF
LDQNGTADSV YQVAAVNKGR EEKLSKKARV WQENVLEVPL AKPEGGVTPD GKPYTYSAND
ASVGDIDGDG EYEMILKWDP SNSKDNAHDG YTGEVLIDAY KLDGTFLWRI NLGRNIRAGA
HYTQFMVYDL DGDGKAEIAM KTADGTTDGK GHIIGDEQAD FRNEQGRILS GPEYLTVFKG
ETGEALTTVE YEPPRGKLED WGDGYGNRMD RFLAGTAYLD GERPSLVMAR GYYTRTVLVA
YDFRNGRLKK RWVFDSNQPG HEAYAGQGNH SLSVADVDGD GKDEIIYGAM AVDHDGTGLY
STGLGHGDAM HVGDLDPSRK GLEVFQVHED ATKPYGLSLR DAGTGEILWG VHAGTDVGRG
MAAHIDPSYK GSLVWGIDPP GNDGMSYGLF TSKGEKISDK APSSANFAIW WDGDLVRELL
DHDWDGTIGR PKIEKWDAEN GCLKTIFQPA GVLSNNGTKG NPVLQANLFG DWREEVIWRT
EDSSALRIYT TTHLTRHCFY TLMHDPVYRL GIAWQNTAYN QPPHTSFYLG TGMKKPPKPA
LYIAGSKAEA PL
