(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 152.
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;
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;
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}.
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   SMR; P20964; -.
DR   IntAct; P20964; 1.
DR   MINT; P20964; -.
DR   STRING; 224308.BSU27920; -.
DR   DrugBank; DB04022; Guanosine-5',3'-Tetraphosphate.
DR   jPOST; P20964; -.
DR   PaxDb; P20964; -.
DR   PRIDE; P20964; -.
DR   EnsemblBacteria; CAB14752; CAB14752; BSU27920.
DR   GeneID; 937502; -.
DR   KEGG; bsu:BSU27920; -.
DR   PATRIC; fig|224308.179.peg.3033; -.
DR   eggNOG; ENOG4105C9R; Bacteria.
DR   eggNOG; COG0536; LUCA.
DR   HOGENOM; HOG000019083; -.
DR   InParanoid; P20964; -.
DR   KO; K03979; -.
DR   OMA; VVFDWEP; -.
DR   PhylomeDB; P20964; -.
DR   BioCyc; BSUB:BSU27920-MONOMER; -.
DR   EvolutionaryTrace; P20964; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
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; 2.40.240.60; -; 1.
DR   Gene3D; 2.70.210.12; -; 1.
DR   HAMAP; MF_01454; GTPase_Obg; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR035101; GTP-bd_Obg.
DR   InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR   InterPro; IPR015349; GTP-bd_prot_GTP1/OBG_C.
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; IPR006073; GTP_binding_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
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;
DR   PRODOM; P20964.
DR   SWISS-2DPAGE; P20964.
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   NP_BIND         165..172
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         190..194
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         212..215
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         282..285
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         310..312
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   METAL           172
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   METAL           192
FT                   /note="Magnesium"
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:0000244|PDB:1LNZ"
FT   STRAND          26..28
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          44..48
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           57..59
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          63..65
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          85..89
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          93..97
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   TURN            98..100
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          103..107
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          113..117
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           126..128
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          134..136
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          148..156
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          161..166
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           171..177
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          178..181
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          184..187
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          197..201
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          203..205
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          207..212
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           213..219
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   TURN            223..226
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           227..236
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          239..247
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           254..267
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   TURN            272..274
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   STRAND          279..282
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           289..299
FT                   /evidence="ECO:0000244|PDB:1LNZ"
FT   HELIX           318..328
FT                   /evidence="ECO:0000244|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
//

If you have problems or comments...

PBIL Back to PBIL home page