KPRS_BACSU
ID KPRS_BACSU Reviewed; 317 AA.
AC P14193;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:2169413};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16008562};
DE Short=PPRibP synthase {ECO:0000303|PubMed:2169413};
DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:3038693};
GN OrderedLocusNames=BSU00510;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2555671; DOI=10.1007/bf00332425;
RA Nilsson D., Hove-Jensen B., Arnvig K.;
RT "Primary structure of the tms and prs genes of Bacillus subtilis.";
RL Mol. Gen. Genet. 218:565-571(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=2169413; DOI=10.1111/j.1432-1033.1990.tb19214.x;
RA Arnvig K., Hove-Jensen B., Switzer R.L.;
RT "Purification and properties of phosphoribosyl-diphosphate synthetase from
RT Bacillus subtilis.";
RL Eur. J. Biochem. 192:195-200(1990).
RN [5]
RP FUNCTION, AND NOMENCLATURE.
RX PubMed=3038693; DOI=10.1016/0378-1119(87)90013-8;
RA Nilsson D., Hove-Jensen B.;
RT "Phosphoribosylpyrophosphate synthetase of Bacillus subtilis. Cloning,
RT characterization and chromosomal mapping of the prs gene.";
RL Gene 53:247-255(1987).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-198; ARG-200; ARG-202;
RP ASN-204 AND GLU-207, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP PATHWAY, AND ACTIVE SITE.
RX PubMed=16008562; DOI=10.1111/j.1742-4658.2005.04785.x;
RA Hove-Jensen B., Bentsen A.K., Harlow K.W.;
RT "Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl
RT diphosphate synthase. Alanine-scanning mutagenesis of the flexible
RT catalytic loop.";
RL FEBS J. 272:3631-3639(2005).
RN [7]
RP REVIEW, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=28031352; DOI=10.1128/mmbr.00040-16;
RA Hove-Jensen B., Andersen K.R., Kilstrup M., Martinussen J., Switzer R.L.,
RA Willemoes M.;
RT "Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization,
RT and metabolic significance.";
RL Microbiol. Mol. Biol. Rev. 81:E00040-E00040(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND
RP ALLOSTERIC INHIBITOR, FUNCTION, AND SUBUNIT.
RX PubMed=10742175; DOI=10.1038/74069;
RA Eriksen T.A., Kadziola A., Bentsen A.-K., Harlow K.W., Larsen S.;
RT "Structural basis for the function of Bacillus subtilis phosphoribosyl-
RT pyrophosphate synthetase.";
RL Nat. Struct. Biol. 7:303-308(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS;
RP ALLOSTERIC INHIBITOR AND CADMIUM IONS, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=11790837; DOI=10.1110/ps.28502;
RA Eriksen T.A., Kadziola A., Larsen S.;
RT "Binding of cations in Bacillus subtilis phosphoribosyldiphosphate
RT synthetase and their role in catalysis.";
RL Protein Sci. 11:271-279(2002).
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837,
CC ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413,
CC ECO:0000269|PubMed:3038693, ECO:0000305|PubMed:10742175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00583, ECO:0000269|PubMed:16008562,
CC ECO:0000269|PubMed:2169413};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000269|PubMed:2169413, ECO:0000303|PubMed:28031352};
CC Note=Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one
CC residue (His-136 and Asp-175, respectively) of this protein, however
CC the magnesium ions also bind substrates and water molecules to complete
CC their coordination spheres (PubMed:2169413, PubMed:11790837). Can also
CC use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained
CC with Mg(2+) ions (PubMed:2169413, PubMed:11790837).
CC {ECO:0000269|PubMed:11790837, ECO:0000269|PubMed:2169413,
CC ECO:0000303|PubMed:28031352};
CC -!- ACTIVITY REGULATION: Activated by inorganic phosphate, and to a lesser
CC extent by sulfate ions (PubMed:2169413). In addition to form a complex
CC with ATP, Mg(2+) also acts as a cofactor (PubMed:2169413). Strongly
CC inhibited by ADP through competitive binding at the activation site and
CC at a specific allosteric site (PubMed:2169413, PubMed:16008562). Less
CC strongly inhibited by alpha,beta-methylene ATP (mADP), AMP, GDP, GMP
CC and UTP (PubMed:2169413, PubMed:16008562).
CC {ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=191 uM for ATP (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16008562};
CC KM=230 uM for Rib-5-P (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16008562};
CC KM=480 uM for Rib-5-P (at pH 8.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2169413};
CC KM=660 uM for ATP (at pH 8.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2169413};
CC Vmax=108 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16008562};
CC Vmax=250 umol/min/mg enzyme (at pH 8.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2169413};
CC pH dependence:
CC Optimum pH is 8-8.5. Activities at pH 7 and pH 9.5 are 35% and 85% of
CC the maximal activity, respectively. {ECO:0000269|PubMed:2169413};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00583, ECO:0000305|PubMed:16008562,
CC ECO:0000305|PubMed:2169413}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000269|PubMed:10742175,
CC ECO:0000269|PubMed:11790837, ECO:0000303|PubMed:28031352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- MISCELLANEOUS: This enzyme uses a steady state ordered mechanism, where
CC Mg(2+) binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.
CC {ECO:0000269|PubMed:16008562}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000303|PubMed:28031352}.
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DR EMBL; X16518; CAA34523.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05286.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11827.1; -; Genomic_DNA.
DR PIR; S05372; KIBSRS.
DR RefSeq; NP_387932.1; NC_000964.3.
DR RefSeq; WP_003218353.1; NZ_JNCM01000028.1.
DR PDB; 1DKR; X-ray; 2.30 A; A/B=1-317.
DR PDB; 1DKU; X-ray; 2.20 A; A/B=1-317.
DR PDB; 1IBS; X-ray; 2.80 A; A/B=1-317.
DR PDBsum; 1DKR; -.
DR PDBsum; 1DKU; -.
DR PDBsum; 1IBS; -.
DR AlphaFoldDB; P14193; -.
DR SMR; P14193; -.
DR IntAct; P14193; 2.
DR MINT; P14193; -.
DR STRING; 224308.BSU00510; -.
DR DrugBank; DB03148; Adenosine 5'-methylenediphosphate.
DR DrugBank; DB02798; Alpha-Methylene Adenosine Monophosphate.
DR jPOST; P14193; -.
DR PaxDb; P14193; -.
DR PRIDE; P14193; -.
DR EnsemblBacteria; CAB11827; CAB11827; BSU_00510.
DR GeneID; 50135225; -.
DR GeneID; 64301872; -.
DR GeneID; 936985; -.
DR KEGG; bsu:BSU00510; -.
DR PATRIC; fig|224308.179.peg.51; -.
DR eggNOG; COG0462; Bacteria.
DR InParanoid; P14193; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; P14193; -.
DR BioCyc; BSUB:BSU00510-MON; -.
DR SABIO-RK; P14193; -.
DR UniPathway; UPA00087; UER00172.
DR EvolutionaryTrace; P14193; -.
DR PRO; PR:P14193; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2169413"
FT CHAIN 2..317
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141110"
FT ACT_SITE 198
FT /evidence="ECO:0000303|PubMed:28031352,
FT ECO:0000305|PubMed:16008562"
FT BINDING 43..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000305|PubMed:10742175"
FT BINDING 102..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS"
FT BINDING 106
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU"
FT BINDING 110
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837,
FT ECO:0007744|PDB:1IBS"
FT BINDING 141
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU"
FT BINDING 149..150
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837,
FT ECO:0007744|PDB:1IBS"
FT BINDING 200
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-
FT Rule:MF_00583"
FT BINDING 224
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-
FT Rule:MF_00583"
FT BINDING 228..232
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837,
FT ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS"
FT BINDING 311..313
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:10742175,
FT ECO:0007744|PDB:1DKU"
FT MUTAGEN 198
FT /note="K->A: Strong decrease of the Vmax value compared to
FT that of the wild-type. The affinity binding for ATP and
FT Rib-5-P are slightly altered compared to the wild-type. The
FT cooperativity of ADP binding is reduced."
FT /evidence="ECO:0000269|PubMed:16008562"
FT MUTAGEN 200
FT /note="R->A: Strong decrease of the Vmax value compared to
FT that of the wild-type enzyme. The affinity binding for ATP
FT and Rib-5-P are slightly altered compared to the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:16008562"
FT MUTAGEN 202
FT /note="R->A: 3-fold decrease in the affinity binding for
FT ATP. Slight decrease of the Vmax value."
FT /evidence="ECO:0000269|PubMed:16008562"
FT MUTAGEN 204
FT /note="N->A: 4.5-fold decrease in the affinity binding for
FT ATP. Slight decrease of the Vmax value."
FT /evidence="ECO:0000269|PubMed:16008562"
FT MUTAGEN 207
FT /note="E->A: 2.5-fold decrease in the affinity binding for
FT ATP. Slight decrease of the Vmax value."
FT /evidence="ECO:0000269|PubMed:16008562"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1IBS"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 69..85
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:1DKU"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1DKU"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:1DKU"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:1DKU"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1DKU"
SQ SEQUENCE 317 AA; 34868 MW; 0D37FC81668111EB CRC64;
MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI EESIRGCDCY
IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY ARQDRKARSR EPITAKLFAN
LLETAGATRV IALDLHAPQI QGFFDIPIDH LMGVPILGEY FEGKNLEDIV IVSPDHGGVT
RARKLADRLK APIAIIDKRR PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL
VENGAKEVYA CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA
EAIIRVHEQQ SVSYLFS
