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
//