ID BGLR_ECOLI Reviewed; 603 AA.
AC P05804;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 24-JAN-2024, entry version 182.
DE RecName: Full=Beta-glucuronidase {ECO:0000303|PubMed:26364932, ECO:0000303|PubMed:3105604};
DE Short=GUS {ECO:0000303|PubMed:26364932};
DE EC=3.2.1.31 {ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068, ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:3105604};
DE AltName: Full=Beta-D-glucuronoside glucuronosohydrolase;
DE AltName: Full=EcGUS {ECO:0000303|PubMed:26364932};
DE AltName: Full=UID {ECO:0000303|PubMed:3105604};
GN Name=uidA; Synonyms=gurA, gusA; OrderedLocusNames=b1617, JW1609;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
RX PubMed=3534890; DOI=10.1073/pnas.83.22.8447;
RA Jefferson R.A., Burgess S.M., Hirsh D.;
RT "Beta-glucuronidase from Escherichia coli as a gene-fusion marker.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8447-8451(1986).
RN [2]
RP SEQUENCE REVISION TO 279.
RX PubMed=8125312; DOI=10.1016/0378-1119(94)90820-6;
RA Schlaman H.R., Risseeuw E., Franke-Van Dijk M.E., Hooykaas P.J.;
RT "Nucleotide sequence corrections of the uidA open reading frame encoding
RT beta-glucuronidase.";
RL Gene 138:259-260(1994).
RN [3]
RP SEQUENCE REVISION TO 420-425.
RX PubMed=2103475; DOI=10.1007/bf00039422;
RA Farrell L.B., Beachy R.N.;
RT "Manipulation of beta-glucuronidase for use as a reporter in vacuolar
RT targeting studies.";
RL Plant Mol. Biol. 15:821-825(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=3105604; DOI=10.1016/0300-9084(87)90248-3;
RA Blanco C., Nemoz G.;
RT "One step purification of Escherichia coli beta-glucuronidase.";
RL Biochimie 69:157-161(1987).
RN [8]
RP CHARACTERIZATION.
RA Jefferson R.A.;
RL Thesis (1985), University of Colorado, United States.
RN [9] {ECO:0007744|PDB:3K46, ECO:0007744|PDB:3K4A, ECO:0007744|PDB:3K4D, ECO:0007744|PDB:3LPF, ECO:0007744|PDB:3LPG}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF APOENZYME AND COMPLEXES WITH
RP GLUCARO-D-LACTAM INHIBITOR AND OTHER INHIBITORS, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=21051639; DOI=10.1126/science.1191175;
RA Wallace B.D., Wang H., Lane K.T., Scott J.E., Orans J., Koo J.S.,
RA Venkatesh M., Jobin C., Yeh L.A., Mani S., Redinbo M.R.;
RT "Alleviating cancer drug toxicity by inhibiting a bacterial enzyme.";
RL Science 330:831-835(2010).
RN [10] {ECO:0007744|PDB:4JHZ}
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 1-601 IN COMPLEX WITH AN
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=23690068; DOI=10.1124/mol.113.085852;
RA Roberts A.B., Wallace B.D., Venkatesh M.K., Mani S., Redinbo M.R.;
RT "Molecular insights into microbial beta-glucuronidase inhibition to
RT abrogate CPT-11 toxicity.";
RL Mol. Pharmacol. 84:208-217(2013).
RN [11] {ECO:0007744|PDB:5CZK}
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) IN COMPLEX WITH INHIBITOR R1, N-K
RP MOTIF, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=26364932; DOI=10.1016/j.chembiol.2015.08.005;
RA Wallace B.D., Roberts A.B., Pollet R.M., Ingle J.D., Biernat K.A.,
RA Pellock S.J., Venkatesh M.K., Guthrie L., O'Neal S.K., Robinson S.J.,
RA Dollinger M., Figueroa E., McShane S.R., Cohen R.D., Jin J., Frye S.V.,
RA Zamboni W.C., Pepe-Ranney C., Mani S., Kelly L., Redinbo M.R.;
RT "Structure and Inhibition of Microbiome beta-Glucuronidases Essential to
RT the Alleviation of Cancer Drug Toxicity.";
RL Chem. Biol. 22:1238-1249(2015).
RN [12] {ECO:0007744|PDB:6LEG, ECO:0007744|PDB:6LEJ, ECO:0007744|PDB:6LEL, ECO:0007744|PDB:6LEM}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEXES WITH INHIBITORS,
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=33664385; DOI=10.1038/s42003-021-01815-w;
RA Lin H.Y., Chen C.Y., Lin T.C., Yeh L.F., Hsieh W.C., Gao S., Burnouf P.A.,
RA Chen B.M., Hsieh T.J., Dashnyam P., Kuo Y.H., Tu Z., Roffler S.R.,
RA Lin C.H.;
RT "Entropy-driven binding of gut bacterial beta-glucuronidase inhibitors
RT ameliorates irinotecan-induced toxicity.";
RL Commun. Biol. 4:280-280(2021).
RN [13] {ECO:0007744|PDB:7PR6}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COVALENT COMPLEX WITH AN
RP INHIBITOR, AND ACTIVE SITE.
RX PubMed=35881786; DOI=10.1073/pnas.2203167119;
RA de Boer C., Armstrong Z., Lit V.A.J., Barash U., Ruijgrok G., Boyango I.,
RA Weitzenberg M.M., Schroeder S.P., Sarris A.J.C., Meeuwenoord N.J., Bule P.,
RA Kayal Y., Ilan N., Codee J.D.C., Vlodavsky I., Overkleeft H.S.,
RA Davies G.J., Wu L.;
RT "Mechanism-based heparanase inhibitors reduce cancer metastasis in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:e2203167119-e2203167119(2022).
CC -!- FUNCTION: Displays beta-glucuronidase activity with the artificial
CC substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-
CC methylumbelliferyl-glucuronide (PubMed:26364932, PubMed:3105604,
CC PubMed:21051639, PubMed:23690068, PubMed:33664385). Is likely capable
CC of scavenging glucuronate from a range of chemically distinct
CC xenobiotic and endobiotic glucuronides present in the gastrointestinal
CC (GI) tract, to be able to utilize these diverse sources of carbon. As
CC part of the GI microbiome, this enzyme is able to reactivate
CC glucuronide drug conjugates, such reactivated compounds can
CC significantly damage the GI tract (PubMed:26364932).
CC {ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068,
CC ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:3105604,
CC ECO:0000269|PubMed:33664385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC Evidence={ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068,
CC ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:3105604,
CC ECO:0000269|PubMed:33664385};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634;
CC Evidence={ECO:0000305|PubMed:26364932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferone beta-D-glucuronate + H2O = 4-
CC methylumbelliferone + D-glucuronate; Xref=Rhea:RHEA:76111,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17224, ChEBI:CHEBI:58720,
CC ChEBI:CHEBI:144582; Evidence={ECO:0000269|PubMed:21051639,
CC ECO:0000269|PubMed:33664385};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76112;
CC Evidence={ECO:0000305|PubMed:21051639};
CC -!- ACTIVITY REGULATION: Potently inhibited by a set of synthetic compounds
CC like thio-urea derivatives and analogs, and uronic isofagomine (UIFG)
CC derivatives. Inhibitors of gut microbial beta-glucuronidases block the
CC reactivation of glucuronidated cancer drugs, and thereby alleviate
CC drug-induced GI toxicity. {ECO:0000269|PubMed:21051639,
CC ECO:0000269|PubMed:23690068, ECO:0000269|PubMed:26364932,
CC ECO:0000269|PubMed:33664385}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for p-nitrophenyl-beta-D-glucuronide
CC {ECO:0000269|PubMed:26364932};
CC Note=kcat is 120 sec(-1) with p-nitrophenyl-beta-D-glucuronide as
CC substrate. {ECO:0000269|PubMed:26364932};
CC pH dependence:
CC Optimum pH is 5.0-7.5.;
CC Temperature dependence:
CC Resistant to thermal inactivation at 50 degrees Celsius.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21051639,
CC ECO:0000269|PubMed:3105604}.
CC -!- DOMAIN: The N-K motif seems to be a discriminant that could be employed
CC as a fingerprint to identify beta-glucuronidases from the large GH2
CC family of proteins. {ECO:0000305|PubMed:26364932}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; M14641; AAA68923.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S69414; AAB30197.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74689.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15368.1; -; Genomic_DNA.
DR PIR; C64918; GBECGC.
DR RefSeq; NP_416134.1; NC_000913.3.
DR RefSeq; WP_000945878.1; NZ_SSZK01000001.1.
DR PDB; 3K46; X-ray; 2.50 A; A/B=1-603.
DR PDB; 3K4A; X-ray; 2.90 A; A/B=1-603.
DR PDB; 3K4D; X-ray; 2.39 A; A/B=1-603.
DR PDB; 3LPF; X-ray; 2.26 A; A/B=1-603.
DR PDB; 3LPG; X-ray; 2.42 A; A/B=1-603.
DR PDB; 4JHZ; X-ray; 2.83 A; A/B=1-601.
DR PDB; 5CZK; X-ray; 2.39 A; A/B=1-603.
DR PDB; 6LEG; X-ray; 2.60 A; A/B/C/D=1-603.
DR PDB; 6LEJ; X-ray; 2.62 A; A/B=1-603.
DR PDB; 6LEL; X-ray; 2.50 A; A/B=1-603.
DR PDB; 6LEM; X-ray; 3.19 A; A/B=1-603.
DR PDB; 7PR6; X-ray; 1.99 A; AAA/BBB=18-599.
DR PDBsum; 3K46; -.
DR PDBsum; 3K4A; -.
DR PDBsum; 3K4D; -.
DR PDBsum; 3LPF; -.
DR PDBsum; 3LPG; -.
DR PDBsum; 4JHZ; -.
DR PDBsum; 5CZK; -.
DR PDBsum; 6LEG; -.
DR PDBsum; 6LEJ; -.
DR PDBsum; 6LEL; -.
DR PDBsum; 6LEM; -.
DR PDBsum; 7PR6; -.
DR AlphaFoldDB; P05804; -.
DR SMR; P05804; -.
DR BioGRID; 4263483; 12.
DR DIP; DIP-11086N; -.
DR IntAct; P05804; 2.
DR STRING; 511145.b1617; -.
DR BindingDB; P05804; -.
DR ChEMBL; CHEMBL3217380; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR jPOST; P05804; -.
DR PaxDb; 511145-b1617; -.
DR EnsemblBacteria; AAC74689; AAC74689; b1617.
DR GeneID; 75204461; -.
DR GeneID; 946149; -.
DR KEGG; ecj:JW1609; -.
DR KEGG; eco:b1617; -.
DR PATRIC; fig|1411691.4.peg.644; -.
DR EchoBASE; EB1048; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_6_1_6; -.
DR InParanoid; P05804; -.
DR OMA; IHDHVGW; -.
DR OrthoDB; 9758603at2; -.
DR PhylomeDB; P05804; -.
DR BioCyc; EcoCyc:BETA-GLUCURONID-MONOMER; -.
DR BioCyc; MetaCyc:BETA-GLUCURONID-MONOMER; -.
DR BRENDA; 3.2.1.31; 2026.
DR SABIO-RK; P05804; -.
DR EvolutionaryTrace; P05804; -.
DR PRO; PR:P05804; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0004566; F:beta-glucuronidase activity; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019391; P:glucuronoside catabolic process; IMP:EcoCyc.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..603
FT /note="Beta-glucuronidase"
FT /id="PRO_0000057680"
FT MOTIF 566..568
FT /note="N-K motif"
FT /evidence="ECO:0000305|PubMed:26364932"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21051639"
FT ACT_SITE 504
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:35881786,
FT ECO:0000305|PubMed:21051639"
FT BINDING 163
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 412
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 466
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 472
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 504
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 549
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT BINDING 568
FT /ligand="D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58720"
FT /evidence="ECO:0000305|PubMed:21051639,
FT ECO:0007744|PDB:3K4D"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5CZK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3K46"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6LEM"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3LPG"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3K46"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6LEM"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6LEL"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3LPG"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 421..435
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3K46"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:3LPF"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 478..496
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3K4D"
FT HELIX 523..537
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:3K4A"
FT STRAND 562..566
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:3LPF"
FT HELIX 580..590
FT /evidence="ECO:0007829|PDB:3LPF"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:3K4A"
SQ SEQUENCE 603 AA; 68447 MW; E769C8D61A3B9A76 CRC64;
MLRPVETPTR EIKKLDGLWA FSLDRENCGI DQRWWESALQ ESRAIAVPGS FNDQFADADI
RNYAGNVWYQ REVFIPKGWA GQRIVLRFDA VTHYGKVWVN NQEVMEHQGG YTPFEADVTP
YVIAGKSVRI TVCVNNELNW QTIPPGMVIT DENGKKKQSY FHDFFNYAGI HRSVMLYTTP
NTWVDDITVV THVAQDCNHA SVDWQVVANG DVSVELRDAD QQVVATGQGT SGTLQVVNPH
LWQPGEGYLY ELCVTAKSQT ECDIYPLRVG IRSVAVKGEQ FLINHKPFYF TGFGRHEDAD
LRGKGFDNVL MVHDHALMDW IGANSYRTSH YPYAEEMLDW ADEHGIVVID ETAAVGFNLS
LGIGFEAGNK PKELYSEEAV NGETQQAHLQ AIKELIARDK NHPSVVMWSI ANEPDTRPQG
AREYFAPLAE ATRKLDPTRP ITCVNVMFCD AHTDTISDLF DVLCLNRYYG WYVQSGDLET
AEKVLEKELL AWQEKLHQPI IITEYGVDTL AGLHSMYTDM WSEEYQCAWL DMYHRVFDRV
SAVVGEQVWN FADFATSQGI LRVGGNKKGI FTRDRKPKSA AFLLQKRWTG MNFGEKPQQG
GKQ
//
