OGA_CLOP1
ID OGA_CLOP1 Reviewed; 1001 AA.
AC Q0TR53;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=O-GlcNAcase NagJ;
DE EC=3.2.1.169 {ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600};
DE AltName: Full=Beta-N-acetylglucosaminidase;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase;
DE AltName: Full=GH84C {ECO:0000303|PubMed:19193644};
DE AltName: Full=Hexosaminidase B;
DE AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE Flags: Precursor;
GN Name=nagJ; OrderedLocusNames=CPF_1442;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1] {ECO:0000312|EMBL:ABG84519.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-624 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG PUGNAC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP ASP-297; ASP-298; TYR-335; ASN-390; ASN-396; ASP-401 AND TRP-490, FUNCTION,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16541109; DOI=10.1038/sj.emboj.7601026;
RA Rao F.V., Dorfmueller H.C., Villa F., Allwood M., Eggleston I.M.,
RA van Aalten D.M.;
RT "Structural insights into the mechanism and inhibition of eukaryotic O-
RT GlcNAc hydrolysis.";
RL EMBO J. 25:1569-1578(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 625-767 IN COMPLEX WITH GALACTOSE
RP AND N-ACETYL-ALPHA-D-GLUCOSAMINE, AND FUNCTION.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16990278; DOI=10.1074/jbc.m606126200;
RA Ficko-Blean E., Boraston A.B.;
RT "The interaction of a carbohydrate-binding module from a Clostridium
RT perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor.";
RL J. Biol. Chem. 281:37748-37757(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-624 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG STREPTOZOTOCIN, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=18721751; DOI=10.1016/j.chembiol.2008.06.010;
RA Pathak S., Dorfmueller H.C., Borodkin V.S., van Aalten D.M.;
RT "Chemical dissection of the link between streptozotocin, O-GlcNAc, and
RT pancreatic cell death.";
RL Chem. Biol. 15:799-807(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 765-1001.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=19193644; DOI=10.1074/jbc.m808954200;
RA Ficko-Blean E., Gregg K.J., Adams J.J., Hehemann J.H., Czjzek M.,
RA Smith S.P., Boraston A.B.;
RT "Portrait of an enzyme, a complete structural analysis of a multimodular
RT {beta}-N-acetylglucosaminidase from Clostridium perfringens.";
RL J. Biol. Chem. 284:9876-9884(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 31-618 OF MUTANT ASN-298 IN
RP COMPLEX WITH N-ACETYL-D-GLUCOSAMINE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP ASP-298.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=22365600; DOI=10.1016/j.chembiol.2012.01.011;
RA Schimpl M., Borodkin V.S., Gray L.J., van Aalten D.M.;
RT "Synergy of peptide and sugar in O-GlcNAcase substrate recognition.";
RL Chem. Biol. 19:173-178(2012).
CC -!- FUNCTION: Binds carbohydrates (PubMed:16990278). Capable of hydrolyzing
CC the glycosidic link of O-GlcNAcylated proteins. Can bind and
CC deglycosylate O-glycosylated peptides from mammals.
CC {ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:16990278,
CC ECO:0000269|PubMed:18721751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O =
CC L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227;
CC EC=3.2.1.169; Evidence={ECO:0000269|PubMed:16541109,
CC ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O
CC = L-threonyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840,
CC ChEBI:CHEBI:506227; EC=3.2.1.169;
CC Evidence={ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751,
CC ECO:0000269|PubMed:22365600};
CC -!- ACTIVITY REGULATION: Inhibited by O-(2-acetamido-2-deoxy-D-
CC glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and
CC streptozotocin. {ECO:0000269|PubMed:16541109,
CC ECO:0000269|PubMed:18721751}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 uM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
CC (4MU-NAG) {ECO:0000269|PubMed:16541109};
CC -!- MISCELLANEOUS: Metal-binding observed in X-ray crystal structures is
CC artifactual. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000255}.
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DR EMBL; CP000246; ABG84519.1; -; Genomic_DNA.
DR RefSeq; WP_003456570.1; NC_008261.1.
DR PDB; 2CBI; X-ray; 2.25 A; A/B=31-624.
DR PDB; 2CBJ; X-ray; 2.35 A; A/B=31-624.
DR PDB; 2J1A; X-ray; 1.49 A; A=625-767.
DR PDB; 2J1E; X-ray; 2.40 A; A=625-767.
DR PDB; 2J62; X-ray; 2.26 A; A/B=31-624.
DR PDB; 2J7M; X-ray; 2.30 A; A=625-767.
DR PDB; 2JH2; X-ray; 2.50 A; A/B/C=768-909.
DR PDB; 2O4E; NMR; -; A=768-909.
DR PDB; 2OZN; X-ray; 1.60 A; A=768-909.
DR PDB; 2V5C; X-ray; 2.10 A; A/B=31-624.
DR PDB; 2V5D; X-ray; 3.30 A; A=31-767.
DR PDB; 2VUR; X-ray; 2.20 A; A/B=31-624.
DR PDB; 2W1N; X-ray; 1.80 A; A=765-1001.
DR PDB; 2WB5; X-ray; 2.31 A; A/B=31-624.
DR PDB; 2X0Y; X-ray; 2.25 A; A/B=31-624.
DR PDB; 2XPK; X-ray; 2.40 A; A/B=31-624.
DR PDB; 2YDQ; X-ray; 2.60 A; A=31-618.
DR PDB; 2YDR; X-ray; 2.75 A; A=31-618.
DR PDB; 2YDS; X-ray; 2.55 A; A=31-618.
DR PDB; 4ZXL; X-ray; 2.60 A; A=39-617.
DR PDB; 5OXD; X-ray; 2.60 A; A=31-618.
DR PDB; 6RHE; X-ray; 3.10 A; A=31-619.
DR PDB; 7KHV; X-ray; 2.30 A; A/B/C/D/E/F=31-624.
DR PDBsum; 2CBI; -.
DR PDBsum; 2CBJ; -.
DR PDBsum; 2J1A; -.
DR PDBsum; 2J1E; -.
DR PDBsum; 2J62; -.
DR PDBsum; 2J7M; -.
DR PDBsum; 2JH2; -.
DR PDBsum; 2O4E; -.
DR PDBsum; 2OZN; -.
DR PDBsum; 2V5C; -.
DR PDBsum; 2V5D; -.
DR PDBsum; 2VUR; -.
DR PDBsum; 2W1N; -.
DR PDBsum; 2WB5; -.
DR PDBsum; 2X0Y; -.
DR PDBsum; 2XPK; -.
DR PDBsum; 2YDQ; -.
DR PDBsum; 2YDR; -.
DR PDBsum; 2YDS; -.
DR PDBsum; 4ZXL; -.
DR PDBsum; 5OXD; -.
DR PDBsum; 6RHE; -.
DR PDBsum; 7KHV; -.
DR AlphaFoldDB; Q0TR53; -.
DR BMRB; Q0TR53; -.
DR SMR; Q0TR53; -.
DR STRING; 195103.CPF_1442; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR DNASU; 4202790; -.
DR EnsemblBacteria; ABG84519; ABG84519; CPF_1442.
DR GeneID; 29571445; -.
DR KEGG; cpf:CPF_1442; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_001501_2_0_9; -.
DR OMA; ARMEEAC; -.
DR OrthoDB; 1158117at2; -.
DR BRENDA; 3.2.1.169; 1503.
DR SABIO-RK; Q0TR53; -.
DR EvolutionaryTrace; Q0TR53; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102571; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR GO; GO:0006517; P:protein deglycosylation; IMP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1001
FT /note="O-GlcNAcase NagJ"
FT /id="PRO_0000257985"
FT DOMAIN 916..1001
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 179..469
FT /note="Catalytic domain"
FT /evidence="ECO:0000255"
FT COILED 515..543
FT /evidence="ECO:0000255"
FT COILED 573..597
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 394..396
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 297
FT /note="D->A: 99% decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 298
FT /note="D->N: 99% decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109,
FT ECO:0000269|PubMed:22365600"
FT MUTAGEN 335
FT /note="Y->F: Strongly decreases affinity for 4MU-NAG. 99%
FT decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 390
FT /note="N->A: No change in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 396
FT /note="N->A: Strongly decreases affinity for 4MU-NAG. 99%
FT decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 401
FT /note="D->A: Strongly decreases affinity for 4MU-NAG. 99%
FT decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT MUTAGEN 490
FT /note="W->A: Strongly decreases affinity for 4MU-NAG. 97%
FT decrease in activity for 4MU-NAG."
FT /evidence="ECO:0000269|PubMed:16541109"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2V5C"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2VUR"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2WB5"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2V5D"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2J62"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2V5C"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 268..285
FT /evidence="ECO:0007829|PDB:2V5C"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2X0Y"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:2V5D"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 434..449
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 472..479
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 499..512
FT /evidence="ECO:0007829|PDB:2V5C"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 519..542
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 545..576
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 580..599
FT /evidence="ECO:0007829|PDB:2V5C"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:2V5C"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:2V5C"
FT STRAND 628..634
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:2J1A"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 671..688
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 697..719
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 727..747
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 749..752
FT /evidence="ECO:0007829|PDB:2V5D"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 759..766
FT /evidence="ECO:0007829|PDB:2J1A"
FT STRAND 776..782
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 785..788
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:2O4E"
FT STRAND 792..804
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 808..815
FT /evidence="ECO:0007829|PDB:2OZN"
FT TURN 818..820
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 821..827
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 832..840
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 843..854
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 858..869
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 873..886
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:2O4E"
FT STRAND 892..894
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 898..905
FT /evidence="ECO:0007829|PDB:2OZN"
FT STRAND 918..925
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 930..935
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 943..950
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 953..959
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 975..984
FT /evidence="ECO:0007829|PDB:2W1N"
FT STRAND 993..998
FT /evidence="ECO:0007829|PDB:2W1N"
SQ SEQUENCE 1001 AA; 111080 MW; 3B918C7DB544A2DC CRC64;
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP ENLEVVGDGF
KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN STTLIIGEVD DDIPELDEAL
NGTTAENLKE EGYALVSNDG KIAIEGKDGD GTFYGVQTFK QLVKESNIPE VNITDYPTVS
ARGIVEGFYG TPWTHQDRLD QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ
ELINASAENK VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT RIFAETVDPS
IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT DYFKGKLALG PMHGLDKGLN
QYVDFFTVNP MEHAELSKIS IHTAADYSWN MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN
HSTRMDNKTW AKSGREDAPE LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK
ANLPEVALEE CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD GDMNTFWHSK
WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG YKVSVSLDGE NFTEVKTGTL
EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ ANGRGKFATA AEVNVHGKLK ENAEVTGSVS
LEALEEVQVG ENLEVGVGID ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE
DGKVRVLVSS LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK DGKKVAEIGK
DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA R
