OBG_BACSU
ID OBG_BACSU Reviewed; 428 AA.
AC P20964;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:7961487};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000303|PubMed:2537815};
DE AltName: Full=OrfA;
DE AltName: Full=Spo0B-associated GTP-binding protein;
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=BSU27920;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GTP-BINDING, OPERON STRUCTURE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=2537815; DOI=10.1128/jb.171.3.1362-1371.1989;
RA Trach K., Hoch J.A.;
RT "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an
RT essential GTP-binding protein.";
RL J. Bacteriol. 171:1362-1371(1989).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RC STRAIN=168;
RX PubMed=3918016; DOI=10.1128/jb.161.2.556-562.1985;
RA Ferrari F.A., Trach K.A., Hoch J.A.;
RT "Sequence analysis of the spo0B locus reveals a polycistronic transcription
RT unit.";
RL J. Bacteriol. 161:556-562(1985).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 79-GLY--ASP-84.
RC STRAIN=168 / JH642;
RX PubMed=7961486; DOI=10.1128/jb.176.23.7155-7160.1994;
RA Kok J., Trach K.A., Hoch J.A.;
RT "Effects on Bacillus subtilis of a conditional lethal mutation in the
RT essential GTP-binding protein Obg.";
RL J. Bacteriol. 176:7155-7160(1994).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GTP-BINDING, GTPASE ACTIVITY,
RP POSSIBLE COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=168;
RX PubMed=7961487; DOI=10.1128/jb.176.23.7161-7168.1994;
RA Welsh K.M., Trach K.A., Folger C., Hoch J.A.;
RT "Biochemical characterization of the essential GTP-binding protein Obg of
RT Bacillus subtilis.";
RL J. Bacteriol. 176:7161-7168(1994).
RN [6]
RP POSSIBLE FUNCTION IN SPORULATION.
RC STRAIN=168 / JH642;
RX PubMed=7768831; DOI=10.1128/jb.177.11.3308-3311.1995;
RA Vidwans S.J., Ireton K., Grossman A.D.;
RT "Possible role for the essential GTP-binding protein Obg in regulating the
RT initiation of sporulation in Bacillus subtilis.";
RL J. Bacteriol. 177:3308-3311(1995).
RN [7]
RP FUNCTION IN STRESS RESPONSE.
RC STRAIN=PY22;
RX PubMed=10419966; DOI=10.1128/jb.181.15.4653-4660.1999;
RA Scott J.M., Haldenwang W.G.;
RT "Obg, an essential GTP binding protein of Bacillus subtilis, is necessary
RT for stress activation of transcription factor sigma(B).";
RL J. Bacteriol. 181:4653-4660(1999).
RN [8]
RP SUBCELLULAR LOCATION, RIBOSOMAL ASSOCIATION, AND BINDING TO L13.
RC STRAIN=PY22;
RX PubMed=10781545; DOI=10.1128/jb.182.10.2771-2777.2000;
RA Scott J.M., Ju J., Mitchell T., Haldenwang W.G.;
RT "The Bacillus subtilis GTP binding protein obg and regulators of the
RT sigma(B) stress response transcription factor cofractionate with
RT ribosomes.";
RL J. Bacteriol. 182:2771-2777(2000).
RN [9]
RP PROTEIN LEVELS, AND DISRUPTION PHENOTYPE.
RC STRAIN=CRK6000;
RX PubMed=12427945; DOI=10.1099/00221287-148-11-3539;
RA Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
RA Ogasawara N.;
RT "Six GTP-binding proteins of the Era/Obg family are essential for cell
RT growth in Bacillus subtilis.";
RL Microbiology 148:3539-3552(2002).
RN [10]
RP RIBOSOMAL ASSOCIATION.
RC STRAIN=PY22;
RX PubMed=15325267; DOI=10.1016/j.bbrc.2004.07.154;
RA Zhang S., Haldenwang W.G.;
RT "Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to
RT ribosomes.";
RL Biochem. Biophys. Res. Commun. 322:565-569(2004).
RN [11]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF GLY-92 AND 407-ARG--ASP-428.
RC STRAIN=168 / BSA46;
RX PubMed=18689482; DOI=10.1128/jb.00799-08;
RA Kuo S., Demeler B., Haldenwang W.G.;
RT "The growth-promoting and stress response activities of the Bacillus
RT subtilis GTP binding protein Obg are separable by mutation.";
RL J. Bacteriol. 190:6625-6635(2008).
RN [12]
RP MOLECULAR DYNAMIC SIMULATIONS.
RX PubMed=20830302; DOI=10.1371/journal.pone.0012597;
RA Lee Y., Bang W.Y., Kim S., Lazar P., Kim C.W., Bahk J.D., Lee K.W.;
RT "Molecular modeling study for interaction between Bacillus subtilis Obg and
RT nucleotides.";
RL PLoS ONE 5:E12597-E12597(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-342 BOUND OR NOT BOUND TO
RP NUCLEOTIDE, ACTIVITY REGULATION BY PPGPP, SUBUNIT, AND POSSIBLE INTERACTION
RP WITH TASA.
RX PubMed=12429099; DOI=10.1016/s0969-2126(02)00882-1;
RA Buglino J., Shen V., Hakimian P., Lima C.D.;
RT "Structural and biochemical analysis of the Obg GTP binding protein.";
RL Structure 10:1581-1592(2002).
RN [14]
RP REVIEW.
RX PubMed=15827604;
RA Czyz A., Wegrzyn G.;
RT "The Obg subfamily of bacterial GTP-binding proteins: essential proteins of
RT largely unknown functions that are evolutionarily conserved from bacteria
RT to humans.";
RL Acta Biochim. Pol. 52:35-43(2005).
RN [15]
RP REVIEW.
RX PubMed=15737924; DOI=10.1016/j.devcel.2005.02.002;
RA Michel B.;
RT "Obg/CtgA, a signaling protein that controls replication, translation, and
RT morphological development?";
RL Dev. Cell 8:300-301(2005).
CC -!- FUNCTION: Necessary for the transition from vegetative growth to stage
CC 0 or stage II of sporulation, but sporulation subsequent to these
CC stages is unaffected at 45 degrees Celsius. This ts effect is probably
CC due solely to the E-79 mutation. Required for expression of early
CC sporulation genes, further suggesting a role in the induction of
CC sporulation. Depletion effects on sporulation can be partially
CC suppressed by missense mutations in spo0A. Strains depleted for obg
CC stop growing after about 3 hours and do not induce the sigma-B factor
CC following ethanol stress. It cofractionates with the ribosome and
CC upstream stress response regulators RsbR, RsbS and RsbT in size
CC fractionation columns, suggesting the ribosome might serve as a
CC possible mediator of the activity of obg and the stress induction of
CC sigma-B. In glycerol gradients partially associates with ribosomes;
CC this is stabilized by a nonhydrolyzable GTP-analog and to a lesser
CC extent GTP and GDP. {ECO:0000269|PubMed:10419966,
CC ECO:0000269|PubMed:18689482, ECO:0000269|PubMed:7768831,
CC ECO:0000269|PubMed:7961486, ECO:0000269|PubMed:7961487}.
CC -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly
CC (p)ppGpp with moderate affinity, with high nucleotide exchange rates
CC and a fairly low GTP hydrolysis rate. Plays a role in control of the
CC cell cycle, stress response, ribosome biogenesis and in those bacteria
CC that undergo differentiation, in morphogenesis control.
CC {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000305|PubMed:7961487};
CC -!- ACTIVITY REGULATION: Inhibited by GDP; less than 20 uM ppGpp stimulates
CC the GTPase, while higher concentrations inhibit.
CC {ECO:0000269|PubMed:12429099, ECO:0000269|PubMed:7961487}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for GTP {ECO:0000269|PubMed:7961487};
CC Vmax=127 pmol/min/mg enzyme {ECO:0000269|PubMed:7961487};
CC Note=Turnover number of 0.0061/min.;
CC -!- SUBUNIT: Monomer. Interacts with TasA (AC P54507) in pull-down
CC experiments. {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:12429099, ECO:0000269|PubMed:7961487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:10781545}. Note=Cofractionates with the ribosome and
CC stress response regulators RsbR, RsbS and RsbT in size fractionation
CC columns; binds to ribosomal protein L13. {ECO:0000269|PubMed:10781545,
CC ECO:0000269|PubMed:15325267}.
CC -!- INDUCTION: Part of an operon with spo0B. {ECO:0000269|PubMed:2537815}.
CC -!- DOMAIN: A mutant in the N-terminal obg domain (Asp-92) impairs growth
CC and ribosome association but has no effect on sporulation or the
CC general stress regulon (GSR). Replacing the last 22 amino acids has no
CC effect on growth or ribosome association, but eliminates sporulation
CC and reduces the GSR, showing for the first time that growth promotion
CC and the GSR phenotypes are separable. {ECO:0000269|PubMed:18689482}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. In
CC depletion experiments cells become over 3-fold longer, are abnormally
CC curved and nucleoids condense. {ECO:0000269|PubMed:12427945,
CC ECO:0000269|PubMed:2537815}.
CC -!- MISCELLANEOUS: Estimated to be present at 6000 copies per cell.
CC {ECO:0000269|PubMed:12427945}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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DR EMBL; M24537; AAA22505.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14752.1; -; Genomic_DNA.
DR EMBL; X02655; CAA26490.1; -; Genomic_DNA.
DR PIR; B32804; B32804.
DR RefSeq; NP_390670.1; NC_000964.3.
DR RefSeq; WP_003246161.1; NZ_JNCM01000036.1.
DR PDB; 1LNZ; X-ray; 2.60 A; A/B=1-342.
DR PDBsum; 1LNZ; -.
DR AlphaFoldDB; P20964; -.
DR SMR; P20964; -.
DR IntAct; P20964; 1.
DR MINT; P20964; -.
DR STRING; 224308.BSU27920; -.
DR DrugBank; DB04022; Guanosine tetraphosphate.
DR jPOST; P20964; -.
DR PaxDb; P20964; -.
DR PRIDE; P20964; -.
DR EnsemblBacteria; CAB14752; CAB14752; BSU_27920.
DR GeneID; 937502; -.
DR KEGG; bsu:BSU27920; -.
DR PATRIC; fig|224308.179.peg.3033; -.
DR eggNOG; COG0536; Bacteria.
DR InParanoid; P20964; -.
DR OMA; VVFDWEP; -.
DR PhylomeDB; P20964; -.
DR BioCyc; BSUB:BSU27920-MON; -.
DR EvolutionaryTrace; P20964; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.30.300.350; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01454; GTPase_Obg; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR015349; OCT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF09269; DUF1967; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF102741; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
DR PROSITE; PS51881; OCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Sporulation.
FT CHAIN 1..428
FT /note="GTPase Obg"
FT /id="PRO_0000205432"
FT DOMAIN 1..158
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 159..329
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 350..428
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 117..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 282..285
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 310..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT MUTAGEN 79..84
FT /note="GRNADD->ERNADN: Stops growing at 45 degrees Celsius,
FT shows sporulation onset defects. KM for GTP is 2.3 uM,
FT turnover number is 0.015/min."
FT /evidence="ECO:0000269|PubMed:7961486"
FT MUTAGEN 92
FT /note="G->D: Grows slowly, very reduced association with
FT ribosomes, fewer 70S ribosomes in cells. No effect on
FT sporulation or the general stress response."
FT /evidence="ECO:0000269|PubMed:18689482"
FT MUTAGEN 407..428
FT /note="RERGAKDGDIIRLLEFEFEFID->SCRRASRIPAHWRPLLVDPSSVPSLA:
FT No effect on growth or ribosomes, eliminates sporulation
FT onset. Also decreases the general stress response to
FT physical stress."
FT /evidence="ECO:0000269|PubMed:18689482"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1LNZ"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1LNZ"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:1LNZ"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:1LNZ"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:1LNZ"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1LNZ"
SQ SEQUENCE 428 AA; 47689 MW; E57F6A88A80B0392 CRC64;
MFVDQVKVYV KGGDGGNGMV AFRREKYVPK GGPAGGDGGK GGDVVFEVDE GLRTLMDFRY
KKHFKAIRGE HGMSKNQHGR NADDMVIKVP PGTVVTDDDT KQVIADLTEH GQRAVIARGG
RGGRGNSRFA TPANPAPQLS ENGEPGKERY IVLELKVLAD VGLVGFPSVG KSTLLSVVSS
AKPKIADYHF TTLVPNLGMV ETDDGRSFVM ADLPGLIEGA HQGVGLGHQF LRHIERTRVI
VHVIDMSGLE GRDPYDDYLT INQELSEYNL RLTERPQIIV ANKMDMPEAA ENLEAFKEKL
TDDYPVFPIS AVTREGLREL LFEVANQLEN TPEFPLYDEE ELTQNRVMYT MENEEVPFNI
TRDPDGVFVL SGDSLERLFK MTDFSRDESV KRFARQMRGM GVDEALRERG AKDGDIIRLL
EFEFEFID
