NADE_BACSU
ID NADE_BACSU Reviewed; 272 AA.
AC P08164;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000303|PubMed:7890752};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:7890752};
DE AltName: Full=General stress protein 38;
DE Short=GSP38;
DE AltName: Full=Spore outgrowth factor B;
DE AltName: Full=Sporulation protein OutB;
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193};
GN Synonyms=outB {ECO:0000303|PubMed:2435704}; OrderedLocusNames=BSU03130;
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=2435704; DOI=10.1128/jb.169.4.1480-1484.1987;
RA Albertini A.M., Caramori T., Henner D.J., Ferrari E., Galizzi A.;
RT "Nucleotide sequence of the outB locus of Bacillus subtilis and regulation
RT of its expression.";
RL J. Bacteriol. 169:1480-1484(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 2-19.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-11, AND PHOSPHORYLATION.
RX PubMed=1556067; DOI=10.1128/jb.174.8.2474-2477.1992;
RA Mitchell C., Morris P.W., Vary J.C.;
RT "Identification of proteins phosphorylated by ATP during sporulation of
RT Bacillus subtilis.";
RL J. Bacteriol. 174:2474-2477(1992).
RN [6]
RP SIMILARITY TO E.COLI NADE.
RX PubMed=2118513; DOI=10.1128/jb.172.9.5482-5485.1990;
RA Albertini A.M., Galizzi A.;
RT "The Bacillus subtilis outB gene is highly homologous to an Escherichia
RT coli ntr-like gene.";
RL J. Bacteriol. 172:5482-5485(1990).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=7890752; DOI=10.1074/jbc.270.11.6181;
RA Nessi C., Albertini A.M., Speranza M.L., Galizzi A.;
RT "The outB gene of Bacillus subtilis codes for NAD synthetase.";
RL J. Biol. Chem. 270:6181-6185(1995).
RN [8] {ECO:0007744|PDB:1NSY}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH AMP; ATP AND
RP DIPHOSPHATE, AND SUBUNIT.
RX PubMed=8895556; DOI=10.1002/j.1460-2075.1996.tb00896.x;
RA Rizzi M., Nessi C., Mattevi A., Coda A., Bolognesi M., Galizzi A.;
RT "Crystal structure of NH3-dependent NAD+ synthetase from Bacillus
RT subtilis.";
RL EMBO J. 15:5125-5134(1996).
RN [9] {ECO:0007744|PDB:2NSY}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH AMP; NAD AND
RP DIPHOSPHATE, AND SUBUNIT.
RX PubMed=9753692; DOI=10.1016/s0969-2126(98)00114-2;
RA Rizzi M., Bolognesi M., Coda A.;
RT "A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate
RT intermediate in the NAD+ synthetase structure.";
RL Structure 6:1129-1140(1998).
RN [10] {ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1IH8}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH AMP; ATP; NAD AND
RP DIPHOSPHATE, AND SUBUNIT.
RX PubMed=11375500; DOI=10.1107/s0907444901003523;
RA Devedjiev Y., Symersky J., Singh R., Jedrzejas M., Brouillette C.,
RA Brouillette W., Muccio D., Chattopadhyay D., DeLucas L.;
RT "Stabilization of active-site loops in NH3-dependent NAD+ synthetase from
RT Bacillus subtilis.";
RL Acta Crystallogr. D 57:806-812(2001).
RN [11] {ECO:0007744|PDB:1KQP}
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH
RP NICOTINAMIDE-ADENINE-DINUCLEOTIDE-ADENYLATE INTERMEDIATE AND DIPHOSPHATE,
RP AND SUBUNIT.
RX PubMed=12077433; DOI=10.1107/s0907444902006698;
RA Symersky J., Devedjiev Y., Moore K., Brouillette C., DeLucas L.;
RT "NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.";
RL Acta Crystallogr. D 58:1138-1146(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000269|PubMed:7890752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00193,
CC ECO:0000269|PubMed:7890752};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.62 mM for NH(4)(+) {ECO:0000269|PubMed:7890752};
CC KM=0.28 mM for deamido-NAD {ECO:0000269|PubMed:7890752};
CC KM=0.21 mM for ATP {ECO:0000269|PubMed:7890752};
CC pH dependence:
CC Optimum pH is 8.2-8.7. {ECO:0000269|PubMed:7890752};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:7890752};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000269|PubMed:7890752}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193,
CC ECO:0000269|PubMed:11375500, ECO:0000269|PubMed:12077433,
CC ECO:0000269|PubMed:7890752, ECO:0000269|PubMed:8895556,
CC ECO:0000269|PubMed:9753692}.
CC -!- DEVELOPMENTAL STAGE: Synthesis starts during germination and outgrowth,
CC and is highest at the end of exponential growth. Present in dormant
CC spores. {ECO:0000269|PubMed:7890752}.
CC -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC limitation and oxygen limitation.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:1556067}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000305}.
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DR EMBL; M15811; AAA22635.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08947.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12107.1; -; Genomic_DNA.
DR PIR; A26936; A26936.
DR RefSeq; NP_388195.1; NC_000964.3.
DR RefSeq; WP_003246440.1; NZ_JNCM01000030.1.
DR PDB; 1EE1; X-ray; 2.06 A; A/B=2-272.
DR PDB; 1FYD; X-ray; 2.25 A; A/B=2-272.
DR PDB; 1IFX; X-ray; 2.25 A; A/B=2-272.
DR PDB; 1IH8; X-ray; 1.90 A; A/B=2-272.
DR PDB; 1KQP; X-ray; 1.03 A; A/B=2-272.
DR PDB; 1NSY; X-ray; 2.00 A; A/B=2-272.
DR PDB; 2NSY; X-ray; 2.00 A; A/B=2-272.
DR PDBsum; 1EE1; -.
DR PDBsum; 1FYD; -.
DR PDBsum; 1IFX; -.
DR PDBsum; 1IH8; -.
DR PDBsum; 1KQP; -.
DR PDBsum; 1NSY; -.
DR PDBsum; 2NSY; -.
DR AlphaFoldDB; P08164; -.
DR BMRB; P08164; -.
DR SMR; P08164; -.
DR STRING; 224308.BSU03130; -.
DR BindingDB; P08164; -.
DR ChEMBL; CHEMBL4615; -.
DR DrugBank; DB02596; alpha,beta-Methyleneadenosine 5'-triphosphate.
DR DrugBank; DB04099; Deamido-Nad.
DR DrugBank; DB00798; Gentamicin.
DR jPOST; P08164; -.
DR PaxDb; P08164; -.
DR PRIDE; P08164; -.
DR EnsemblBacteria; CAB12107; CAB12107; BSU_03130.
DR GeneID; 938339; -.
DR KEGG; bsu:BSU03130; -.
DR PATRIC; fig|224308.179.peg.327; -.
DR eggNOG; COG0171; Bacteria.
DR InParanoid; P08164; -.
DR OMA; MAFLYDY; -.
DR PhylomeDB; P08164; -.
DR BioCyc; BSUB:BSU03130-MON; -.
DR BRENDA; 6.3.1.5; 658.
DR SABIO-RK; P08164; -.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; P08164; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sporulation; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1556067,
FT ECO:0000269|PubMed:9298659"
FT CHAIN 2..272
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152159"
FT BINDING 33
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD,
FT ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY,
FT ECO:0007744|PDB:2NSY"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD,
FT ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD,
FT ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY"
FT BINDING 138
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY,
FT ECO:0007744|PDB:2NSY"
FT BINDING 171
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY"
FT BINDING 178
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD,
FT ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD,
FT ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1NSY,
FT ECO:0007744|PDB:2NSY"
FT BINDING 224
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP,
FT ECO:0007744|PDB:2NSY"
FT BINDING 258..259
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX,
FT ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 129..151
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1KQP"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1KQP"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:1KQP"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:1KQP"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:1KQP"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1IH8"
SQ SEQUENCE 272 AA; 30395 MW; 8021E88B5946C2E0 CRC64;
MSMQEKIMRE LHVKPSIDPK QEIEDRVNFL KQYVKKTGAK GFVLGISGGQ DSTLAGRLAQ
LAVESIREEG GDAQFIAVRL PHGTQQDEDD AQLALKFIKP DKSWKFDIKS TVSAFSDQYQ
QETGDQLTDF NKGNVKARTR MIAQYAIGGQ EGLLVLGTDH AAEAVTGFFT KYGDGGADLL
PLTGLTKRQG RTLLKELGAP ERLYLKEPTA DLLDEKPQQS DETELGISYD EIDDYLEGKE
VSAKVSEALE KRYSMTEHKR QVPASMFDDW WK
