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GTPase Obg (EC 3.6.5.-) (GTP-binding protein Obg) (OrfA) (Spo0B-associated GTP-binding protein)

 OBG_BACSU               Reviewed;         428 AA.
P20964;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
22-NOV-2017, entry version 139.
RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:7961487};
AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000303|PubMed:2537815};
AltName: Full=OrfA;
AltName: Full=Spo0B-associated GTP-binding protein;
Name=obg {ECO:0000255|HAMAP-Rule:MF_01454};
OrderedLocusNames=BSU27920;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GTP-BINDING, OPERON STRUCTURE, AND
DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=2537815; DOI=10.1128/jb.171.3.1362-1371.1989;
Trach K., Hoch J.A.;
"The Bacillus subtilis spo0B stage 0 sporulation operon encodes an
essential GTP-binding protein.";
J. Bacteriol. 171:1362-1371(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
STRAIN=168;
PubMed=3918016;
Ferrari F.A., Trach K.A., Hoch J.A.;
"Sequence analysis of the spo0B locus reveals a polycistronic
transcription unit.";
J. Bacteriol. 161:556-562(1985).
[4]
FUNCTION, AND MUTAGENESIS OF 79-GLY--ASP-84.
STRAIN=168 / JH642;
PubMed=7961486; DOI=10.1128/jb.176.23.7155-7160.1994;
Kok J., Trach K.A., Hoch J.A.;
"Effects on Bacillus subtilis of a conditional lethal mutation in the
essential GTP-binding protein Obg.";
J. Bacteriol. 176:7155-7160(1994).
[5]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GTP-BINDING, GTPASE ACTIVITY,
POSSIBLE COFACTOR, AND ENZYME REGULATION.
STRAIN=168;
PubMed=7961487; DOI=10.1128/jb.176.23.7161-7168.1994;
Welsh K.M., Trach K.A., Folger C., Hoch J.A.;
"Biochemical characterization of the essential GTP-binding protein Obg
of Bacillus subtilis.";
J. Bacteriol. 176:7161-7168(1994).
[6]
POSSIBLE FUNCTION IN SPORULATION.
STRAIN=168 / JH642;
PubMed=7768831; DOI=10.1128/jb.177.11.3308-3311.1995;
Vidwans S.J., Ireton K., Grossman A.D.;
"Possible role for the essential GTP-binding protein Obg in regulating
the initiation of sporulation in Bacillus subtilis.";
J. Bacteriol. 177:3308-3311(1995).
[7]
FUNCTION IN STRESS RESPONSE.
STRAIN=PY22;
PubMed=10419966;
Scott J.M., Haldenwang W.G.;
"Obg, an essential GTP binding protein of Bacillus subtilis, is
necessary for stress activation of transcription factor sigma(B).";
J. Bacteriol. 181:4653-4660(1999).
[8]
SUBCELLULAR LOCATION, RIBOSOMAL ASSOCIATION, AND BINDING TO L13.
STRAIN=PY22;
PubMed=10781545; DOI=10.1128/JB.182.10.2771-2777.2000;
Scott J.M., Ju J., Mitchell T., Haldenwang W.G.;
"The Bacillus subtilis GTP binding protein obg and regulators of the
sigma(B) stress response transcription factor cofractionate with
ribosomes.";
J. Bacteriol. 182:2771-2777(2000).
[9]
PROTEIN LEVELS, AND DISRUPTION PHENOTYPE.
STRAIN=CRK6000;
PubMed=12427945;
Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
Ogasawara N.;
"Six GTP-binding proteins of the Era/Obg family are essential for cell
growth in Bacillus subtilis.";
Microbiology 148:3539-3552(2002).
[10]
RIBOSOMAL ASSOCIATION.
STRAIN=PY22;
PubMed=15325267; DOI=10.1016/j.bbrc.2004.07.154;
Zhang S., Haldenwang W.G.;
"Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to
ribosomes.";
Biochem. Biophys. Res. Commun. 322:565-569(2004).
[11]
FUNCTION, DOMAIN, AND MUTAGENESIS OF GLY-92 AND 407-ARG--ASP-428.
STRAIN=168 / BSA46;
PubMed=18689482; DOI=10.1128/JB.00799-08;
Kuo S., Demeler B., Haldenwang W.G.;
"The growth-promoting and stress response activities of the Bacillus
subtilis GTP binding protein Obg are separable by mutation.";
J. Bacteriol. 190:6625-6635(2008).
[12]
MOLECULAR DYNAMIC SIMULATIONS.
PubMed=20830302; DOI=10.1371/journal.pone.0012597;
Lee Y., Bang W.Y., Kim S., Lazar P., Kim C.W., Bahk J.D., Lee K.W.;
"Molecular modeling study for interaction between Bacillus subtilis
Obg and nucleotides.";
PLoS ONE 5:E12597-E12597(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-342 BOUND OR NOT BOUND TO
NUCLEOTIDE, ENZYME REGULATION BY PPGPP, SUBUNIT, AND POSSIBLE
INTERACTION WITH TASA.
PubMed=12429099; DOI=10.1016/S0969-2126(02)00882-1;
Buglino J., Shen V., Hakimian P., Lima C.D.;
"Structural and biochemical analysis of the Obg GTP binding protein.";
Structure 10:1581-1592(2002).
[14]
REVIEW.
PubMed=15827604;
Czyz A., Wegrzyn G.;
"The Obg subfamily of bacterial GTP-binding proteins: essential
proteins of largely unknown functions that are evolutionarily
conserved from bacteria to humans.";
Acta Biochim. Pol. 52:35-43(2005).
[15]
REVIEW.
PubMed=15737924; DOI=10.1016/j.devcel.2005.02.002;
Michel B.;
"Obg/CtgA, a signaling protein that controls replication, translation,
and morphological development?";
Dev. Cell 8:300-301(2005).
-!- FUNCTION: Necessary for the transition from vegetative growth to
stage 0 or stage II of sporulation, but sporulation subsequent to
these stages is unaffected at 45 degrees Celsius. This ts effect
is probably due solely to the E-79 mutation. Required for
expression of early sporulation genes, further suggesting a role
in the induction of sporulation. Depletion effects on sporulation
can be partially suppressed by missense mutations in spo0A.
Strains depleted for obg stop growing after about 3 hours and do
not induce the sigma-B factor following ethanol stress. It
cofractionates with the ribosome and upstream stress response
regulators RsbR, RsbS and RsbT in size fractionation columns,
suggesting the ribosome might serve as a possible mediator of the
activity of obg and the stress induction of sigma-B. In glycerol
gradients partially associates with ribosomes; this is stabilized
by a nonhydrolyzable GTP-analog and to a lesser extent GTP and
GDP. {ECO:0000269|PubMed:10419966, ECO:0000269|PubMed:18689482,
ECO:0000269|PubMed:7768831, ECO:0000269|PubMed:7961486,
ECO:0000269|PubMed:7961487}.
-!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly
(p)ppGpp with moderate affinity, with high nucleotide exchange
rates and a fairly low GTP hydrolysis rate. Plays a role in
control of the cell cycle, stress response, ribosome biogenesis
and in those bacteria that undergo differentiation, in
morphogenesis control. {ECO:0000255|HAMAP-Rule:MF_01454}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01454,
ECO:0000305|PubMed:7961487};
-!- ENZYME REGULATION: Inhibited by GDP; less than 20 uM ppGpp
stimulates the GTPase, while higher concentrations inhibit.
{ECO:0000269|PubMed:12429099, ECO:0000269|PubMed:7961487}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.4 uM for GTP {ECO:0000269|PubMed:7961487};
Vmax=127 pmol/min/mg enzyme {ECO:0000269|PubMed:7961487};
Note=Turnover number of 0.0061/min.;
-!- SUBUNIT: Monomer. Interacts with TasA (AC P54507) in pull-down
experiments. {ECO:0000255|HAMAP-Rule:MF_01454,
ECO:0000269|PubMed:12429099, ECO:0000269|PubMed:7961487}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
ECO:0000269|PubMed:10781545}. Note=Cofractionates with the
ribosome and stress response regulators RsbR, RsbS and RsbT in
size fractionation columns; binds to ribosomal protein L13.
{ECO:0000269|PubMed:10781545, ECO:0000269|PubMed:15325267}.
-!- INDUCTION: Part of an operon with spo0B.
{ECO:0000269|PubMed:2537815}.
-!- DOMAIN: A mutant in the N-terminal obg domain (Asp-92) impairs
growth and ribosome association but has no effect on sporulation
or the general stress regulon (GSR). Replacing the last 22 amino
acids has no effect on growth or ribosome association, but
eliminates sporulation and reduces the GSR, showing for the first
time that growth promotion and the GSR phenotypes are separable.
{ECO:0000269|PubMed:18689482}.
-!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be
disrupted. In depletion experiments cells become over 3-fold
longer, are abnormally curved and nucleoids condense.
{ECO:0000269|PubMed:12427945, ECO:0000269|PubMed:2537815}.
-!- MISCELLANEOUS: Estimated to be present at 6000 copies per cell.
{ECO:0000269|PubMed:12427945}.
-!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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EMBL; M24537; AAA22505.1; -; Genomic_DNA.
EMBL; AL009126; CAB14752.1; -; Genomic_DNA.
EMBL; X02655; CAA26490.1; -; Genomic_DNA.
PIR; B32804; B32804.
RefSeq; NP_390670.1; NC_000964.3.
RefSeq; WP_003246161.1; NZ_JNCM01000036.1.
PDB; 1LNZ; X-ray; 2.60 A; A/B=1-342.
PDBsum; 1LNZ; -.
ProteinModelPortal; P20964; -.
SMR; P20964; -.
IntAct; P20964; 1.
MINT; MINT-8366614; -.
STRING; 224308.Bsubs1_010100015261; -.
PaxDb; P20964; -.
EnsemblBacteria; CAB14752; CAB14752; BSU27920.
GeneID; 937502; -.
KEGG; bsu:BSU27920; -.
PATRIC; fig|224308.179.peg.3033; -.
eggNOG; ENOG4105C9R; Bacteria.
eggNOG; COG0536; LUCA.
HOGENOM; HOG000019083; -.
InParanoid; P20964; -.
KO; K03979; -.
OMA; PHVGIVH; -.
PhylomeDB; P20964; -.
BioCyc; BSUB:BSU27920-MONOMER; -.
EvolutionaryTrace; P20964; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
CDD; cd01898; Obg; 1.
Gene3D; 2.70.210.12; -; 1.
HAMAP; MF_01454; GTPase_Obg; 1.
InterPro; IPR031167; G_OBG.
InterPro; IPR035101; GTP-bd_Obg.
InterPro; IPR014100; GTP-bd_Obg/CgtA.
InterPro; IPR015349; GTP-bd_prot_GTP1/OBG_C.
InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
InterPro; IPR006074; GTP1-OBG_CS.
InterPro; IPR006169; GTP1_OBG_dom.
InterPro; IPR036726; GTP1_OBG_dom_sf.
InterPro; IPR006073; GTP_binding_domain.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
Pfam; PF09269; DUF1967; 1.
Pfam; PF01018; GTP1_OBG; 1.
Pfam; PF01926; MMR_HSR1; 1.
PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
PRINTS; PR00326; GTP1OBG.
SUPFAM; SSF102741; SSF102741; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF82051; SSF82051; 1.
TIGRFAMs; TIGR02729; Obg_CgtA; 1.
TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51710; G_OBG; 1.
PROSITE; PS00905; GTP1_OBG; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; GTP-binding; Hydrolase;
Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
Sporulation.
CHAIN 1 428 GTPase Obg.
/FTId=PRO_0000205432.
DOMAIN 159 329 OBG-type G. {ECO:0000255|HAMAP-
Rule:MF_01454}.
NP_BIND 165 172 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 190 194 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 212 215 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 282 285 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 310 312 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
METAL 172 172 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01454}.
METAL 192 192 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01454}.
MUTAGEN 79 84 GRNADD->ERNADN: Stops growing at 45
degrees Celsius, shows sporulation onset
defects. KM for GTP is 2.3 uM, turnover
number is 0.015/min.
{ECO:0000269|PubMed:7961486}.
MUTAGEN 92 92 G->D: Grows slowly, very reduced
association with ribosomes, fewer 70S
ribosomes in cells. No effect on
sporulation or the general stress
response. {ECO:0000269|PubMed:18689482}.
MUTAGEN 407 428 RERGAKDGDIIRLLEFEFEFID->SCRRASRIPAHWRPLLV
DPSSVPSLA: No effect on growth or
ribosomes, eliminates sporulation onset.
Also decreases the general stress
response to physical stress.
{ECO:0000269|PubMed:18689482}.
STRAND 2 11 {ECO:0000244|PDB:1LNZ}.
STRAND 26 28 {ECO:0000244|PDB:1LNZ}.
STRAND 44 48 {ECO:0000244|PDB:1LNZ}.
HELIX 57 59 {ECO:0000244|PDB:1LNZ}.
STRAND 63 65 {ECO:0000244|PDB:1LNZ}.
STRAND 86 89 {ECO:0000244|PDB:1LNZ}.
STRAND 93 97 {ECO:0000244|PDB:1LNZ}.
TURN 98 100 {ECO:0000244|PDB:1LNZ}.
STRAND 103 107 {ECO:0000244|PDB:1LNZ}.
STRAND 113 117 {ECO:0000244|PDB:1LNZ}.
HELIX 126 128 {ECO:0000244|PDB:1LNZ}.
STRAND 134 136 {ECO:0000244|PDB:1LNZ}.
STRAND 148 156 {ECO:0000244|PDB:1LNZ}.
STRAND 161 166 {ECO:0000244|PDB:1LNZ}.
HELIX 171 177 {ECO:0000244|PDB:1LNZ}.
STRAND 178 181 {ECO:0000244|PDB:1LNZ}.
STRAND 184 187 {ECO:0000244|PDB:1LNZ}.
STRAND 203 205 {ECO:0000244|PDB:1LNZ}.
STRAND 207 209 {ECO:0000244|PDB:1LNZ}.
HELIX 213 219 {ECO:0000244|PDB:1LNZ}.
TURN 223 226 {ECO:0000244|PDB:1LNZ}.
HELIX 227 236 {ECO:0000244|PDB:1LNZ}.
STRAND 239 245 {ECO:0000244|PDB:1LNZ}.
HELIX 254 267 {ECO:0000244|PDB:1LNZ}.
TURN 272 274 {ECO:0000244|PDB:1LNZ}.
STRAND 279 282 {ECO:0000244|PDB:1LNZ}.
HELIX 289 299 {ECO:0000244|PDB:1LNZ}.
HELIX 318 328 {ECO:0000244|PDB:1LNZ}.
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


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EIAAB33940 DXS8237E,G patch domain-containing protein 9,GPATC9,GPATCH9,Homo sapiens,Human,KIAA0122,RBM10,RNA-binding motif protein 10,RNA-binding protein 10,RNA-binding protein S1-1,S1-1
EIAAB10707 Damage-specific DNA-binding protein 1,DDB p127 subunit,DDB1,DDBa,DNA damage-binding protein 1,DNA damage-binding protein a,HBV X-associated protein 1,Homo sapiens,Human,UV-damaged DNA-binding factor,U


 

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