PULA_STRPN
ID PULA_STRPN Reviewed; 1280 AA.
AC A0A0H2UNG0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Pullulanase A {ECO:0000303|PubMed:20497336};
DE EC=3.2.1.41 {ECO:0000269|PubMed:20497336, ECO:0000269|PubMed:21565699};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000305};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000305};
DE Flags: Precursor;
GN Name=spuA {ECO:0000305|PubMed:17187076, ECO:0000305|PubMed:20497336,
GN ECO:0000305|PubMed:21565699};
GN OrderedLocusNames=SP_0268 {ECO:0000312|EMBL:AAK74446.1};
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187 {ECO:0000312|EMBL:AAK74446.1};
RN [1] {ECO:0000312|EMBL:AAK74446.1, ECO:0000312|Proteomes:UP000000585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4 {ECO:0000312|Proteomes:UP000000585};
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20497336; DOI=10.1111/j.1365-2958.2010.07199.x;
RA Abbott D.W., Higgins M.A., Hyrnuik S., Pluvinage B.,
RA Lammerts van Bueren A., Boraston A.B.;
RT "The molecular basis of glycogen breakdown and transport in Streptococcus
RT pneumoniae.";
RL Mol. Microbiol. 77:183-199(2010).
RN [3] {ECO:0007744|PDB:2J44}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 135-353 IN COMPLEX WITH
RP MALTOTETRAOSE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RX PubMed=17187076; DOI=10.1038/nsmb1187;
RA van Bueren A.L., Higgins M., Wang D., Burke R.D., Boraston A.B.;
RT "Identification and structural basis of binding to host lung glycogen by
RT streptococcal virulence factors.";
RL Nat. Struct. Mol. Biol. 14:76-84(2007).
RN [4] {ECO:0007744|PDB:2YA0, ECO:0007744|PDB:2YA1, ECO:0007744|PDB:2YA2}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 437-1150 AND IN COMPLEXES WITH
RP CALCIUM; MALTOTETRAOSE AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP DOMAIN, ACTIVE SITES, AND MUTAGENESIS OF 1-MET--TYR-445; ASP-778 AND
RP GLU-807.
RX PubMed=21565699; DOI=10.1016/j.str.2011.03.001;
RA Lammerts van Bueren A., Ficko-Blean E., Pluvinage B., Hehemann J.H.,
RA Higgins M.A., Deng L., Ogunniyi A.D., Stroeher U.H., El Warry N.,
RA Burke R.D., Czjzek M., Paton J.C., Vocadlo D.J., Boraston A.B.;
RT "The conformation and function of a multimodular glycogen-degrading
RT pneumococcal virulence factor.";
RL Structure 19:640-651(2011).
CC -!- FUNCTION: Virulence factor (By similarity). Involved in the degradation
CC of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes
CC the alpha-1,6-branchpoints of glycogen (PubMed:20497336,
CC PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran
CC (PubMed:20497336). Binds to mouse lung alveolar type II cells that are
CC rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-
CC binding protein, which binds to amylose (pure alpha-(1,4)-linked
CC glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6)
CC branch points), pullulan (linear polymer of mixed alpha-(1,4)- and
CC alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with
CC more frequent alpha-(1,6) branch points) in vitro. Does not bind to
CC dextran (a linear polymer of alpha-(1,6)-linked glucose)
CC (PubMed:17187076). {ECO:0000250|UniProtKB:A0A0H2ZL64,
CC ECO:0000269|PubMed:17187076, ECO:0000269|PubMed:20497336,
CC ECO:0000269|PubMed:21565699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan,
CC amylopectin and glycogen, and in the alpha- and beta-limit dextrins
CC of amylopectin and glycogen.; EC=3.2.1.41;
CC Evidence={ECO:0000269|PubMed:20497336, ECO:0000269|PubMed:21565699};
CC -!- ACTIVITY REGULATION: Inhibited by 4-O-alpha-D-glucopyranosylmoranoline
CC (G1M). {ECO:0000269|PubMed:21565699}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=360 uM for para-nitrophenyl-alpha-D-maltopentaoside (pNP-M5) (at
CC 25 degrees Celsius) {ECO:0000269|PubMed:21565699};
CC Note=kcat is 270 min(-1) for pNP-M5. {ECO:0000269|PubMed:21565699};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Cell surface {ECO:0000250|UniProtKB:Q9F930}.
CC Note=Localizes to cytoplasm in the lung alveolar type II cells of the
CC mouse and human hosts. {ECO:0000269|PubMed:17187076,
CC ECO:0000269|PubMed:21565699}.
CC -!- DOMAIN: The N-terminal tandem family 41 carbohydrate-binding modules
CC (CBM) are involved in carbohydrate binding (PubMed:17187076,
CC PubMed:21565699). The C-terminal glycosyl hydrolase 13 (GH13) domain is
CC involved in catalysis (PubMed:21565699). {ECO:0000269|PubMed:17187076,
CC ECO:0000269|PubMed:21565699}.
CC -!- DISRUPTION PHENOTYPE: Grows readily on glucose and maltotriose, but not
CC on glycogen. No soluble alpha-glucooligosaccharides detected in the
CC culture supernatant. {ECO:0000269|PubMed:20497336}.
CC -!- BIOTECHNOLOGY: This protein may have potential in the disruption of
CC glycogen adherence of the pneumococci to the host cell or disruption of
CC glycogen breakdown in the host cells by the bacteria and thus could be
CC useful in treating streptococcal lung infections.
CC {ECO:0000305|PubMed:17187076}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AE005672; AAK74446.1; -; Genomic_DNA.
DR RefSeq; WP_001232766.1; NZ_AKVY01000001.1.
DR PDB; 2J44; X-ray; 2.10 A; A=135-353.
DR PDB; 2YA0; X-ray; 1.85 A; A=437-1150.
DR PDB; 2YA1; X-ray; 2.25 A; A=135-1143.
DR PDB; 2YA2; X-ray; 2.37 A; A=436-1143.
DR PDBsum; 2J44; -.
DR PDBsum; 2YA0; -.
DR PDBsum; 2YA1; -.
DR PDBsum; 2YA2; -.
DR AlphaFoldDB; A0A0H2UNG0; -.
DR SMR; A0A0H2UNG0; -.
DR STRING; 170187.SP_0268; -.
DR EnsemblBacteria; AAK74446; AAK74446; SP_0268.
DR KEGG; spn:SP_0268; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR OMA; KMNEVWI; -.
DR PhylomeDB; A0A0H2UNG0; -.
DR BioCyc; SPNE170187:G1FZB-275-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:2001066; F:amylopectin binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:2001069; F:glycogen binding; IDA:UniProtKB.
DR GO; GO:0010303; F:limit dextrinase activity; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR GO; GO:2001067; F:pullulan binding; IDA:UniProtKB.
DR GO; GO:0051060; F:pullulanase activity; IDA:UniProtKB.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IDA:UniProtKB.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 2.60.40.1220; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011838; Pullulan_Gpos.
DR InterPro; IPR040806; SpuA_C.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF18033; SpuA_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF49452; SSF49452; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02102; pullulan_Gpos; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall; Glycosidase; Hydrolase; Metal-binding;
KW Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..1280
FT /note="Pullulanase A"
FT /evidence="ECO:0000255"
FT /id="PRO_5002599297"
FT PROPEP 1250..1280
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_5018350525"
FT REGION 42..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1246..1250
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 42..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 778
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21565699"
FT ACT_SITE 807
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:21565699"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 263..265
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17187076,
FT ECO:0000269|PubMed:21565699, ECO:0007744|PDB:2J44,
FT ECO:0007744|PDB:2YA1"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA0"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA0"
FT BINDING 667..668
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 743
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 809
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 828
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA2"
FT BINDING 831
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA2"
FT BINDING 832
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA2"
FT BINDING 839
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 842
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 849
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 882
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA2"
FT BINDING 886
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA2"
FT BINDING 896
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 969
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1"
FT BINDING 989..991
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA1, ECO:0007744|PDB:2YA2"
FT BINDING 992
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21565699,
FT ECO:0007744|PDB:2YA0"
FT SITE 895
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:21565699"
FT MOD_RES 1249
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 1..445
FT /note="Missing: Catalyzes the hydrolysis of a glycosidic
FT bond, but is roughly half as effective as wild-type at
FT releasing maltotriose (M3) to maltooctaose (M8)
FT oligosaccharides from glycogen. Has 6-fold increase in KM
FT for the para-nitrophenyl-alpha-D-maltopentaoside (pNP-M5)
FT substrate and 5 to 8-fold decrease in binding affinity to a
FT synthetic alpha-glucanase inhibitor."
FT /evidence="ECO:0000269|PubMed:21565699"
FT MUTAGEN 778
FT /note="D->A: Loss of catalytic activity. Does not degrade
FT glycogen."
FT /evidence="ECO:0000269|PubMed:21565699"
FT MUTAGEN 807
FT /note="E->A: Loss of catalytic activity. Does not degrade
FT glycogen."
FT /evidence="ECO:0000269|PubMed:21565699"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2J44"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:2J44"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2J44"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:2J44"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2J44"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:2YA1"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2YA1"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:2YA1"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:2YA1"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 461..467
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 520..527
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 595..599
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 605..607
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 615..619
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 631..636
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 688..702
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 720..723
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 753..770
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 785..798
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 825..830
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 832..837
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 839..846
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 857..860
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 865..872
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:2YA1"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 887..889
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 899..907
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 914..933
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 934..941
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 942..947
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 963..965
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 970..974
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 980..988
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 995..998
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1002..1006
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 1008..1010
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1012..1029
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1032..1035
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1039..1045
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1046..1050
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1059..1069
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1075..1081
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1083..1085
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1087..1090
FT /evidence="ECO:0007829|PDB:2YA0"
FT TURN 1092..1095
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1096..1100
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1102..1105
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1119..1123
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1125..1130
FT /evidence="ECO:0007829|PDB:2YA0"
FT STRAND 1134..1140
FT /evidence="ECO:0007829|PDB:2YA0"
FT HELIX 1142..1144
FT /evidence="ECO:0007829|PDB:2YA0"
SQ SEQUENCE 1280 AA; 142619 MW; A209B802A8E0B328 CRC64;
MRKTPSHTEK KMVYSIRSLK NGTGSVLIGA SLVLLAMATP TISSDESTPT TNEPNNRNTT
TLAQPLTDTA AGSGKNESDI SSPGNANASL EKTEEKPAAS PADPAPQTGQ DRSSEPTTST
SPVTTETKAE EPIEDNYFRI HVKKLPEENK DAQGLWTWDD VEKPSENWPN GALSFKDAKK
DDYGYYLDVK LKGEQAKKIS FLINNTAGKN LTGDKSVEKL VPKMNEAWLD QDYKVFSYEP
QPAGTVRVNY YRTDGNYDKK SLWYWGDVKN PSSAQWPDGT DFTATGKYGR YIDIPLNEAA
REFGFLLLDE SKQGDDVKIR KENYKFTDLK NHSQIFLKDD DESIYTNPYY VHDIRMTGAQ
HVGTSSIESS FSTLVGAKKE DILKHSNITN HLGNKVTITD VAIDEAGKKV TYSGDFSDTK
HPYTVSYNSD QFTTKTSWRL KDETYSYDGK LGADLKEEGK QVDLTLWSPS ADKVSVVVYD
KNDPDKVVGT VALEKGERGT WKQTLDSTNK LGITDFTGYY YQYQIERQGK TVLALDPYAK
SLAAWNSDDS KIDDAHKVAK AAFVDPAKLG PQDLTYGKIH NFKTREDAVI YEAHVRDFTS
DPAIAKDLTK PFGTFEAFIE KLDYLKDLGV THIQLLPVLS YYFVNELKNH ERLSDYASSN
SNYNWGYDPQ NYFSLTGMYS SDPKNPEKRI AEFKNLINEI HKRGMGAILD VVYNHTAKVD
LFEDLEPNYY HFMDADGTPR TSFGGGRLGT THHMTKRLLI DSIKYLVDTY KVDGFRFDMM
GDHDAASIEE AYKAARALNP NLIMLGEGWR TYAGDENMPT KAADQDWMKH TDTVAVFSDD
IRNNLKSGYP NEGQPAFITG GKRDVNTIFK NLIAQPTNFE ADSPGDVIQY IAAHDNLTLF
DIIAQSIKKD PSKAENYAEI HRRLRLGNLM VLTAQGTPFI HSGQEYGRTK QFRDPAYKTP
VAEDKVPNKS HLLRDKDGNP FDYPYFIHDS YDSSDAVNKF DWTKATDGKA YPENVKSRDY
MKGLIALRQS TDAFRLKSLQ DIKDRVHLIT VPGQNGVEKE DVVIGYQITA PNGDIYAVFV
NADEKAREFN LGTAFAHLRN AEVLADENQA GPVGIANPKG LEWTEKGLKL NALTATVLRV
SQNGTSHEST AEEKPDSTPS KPEHQNEASH PAHQDPAPEA RPDSTKPDAK VADAENKPSQ
ATADSQAEQP AQEAQASSVK EAVRNESVEN SSKENIPATP DKQAELPNTG IKNENKLLFA
GISLLALLGL GFLLKNKKEN
