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Protein

GTPase Obg

Gene

obg

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications
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.UniRule annotation

Cofactori

Mg2+UniRule annotation1 Publication

Enzyme regulationi

Inhibited by GDP; less than 20 µM ppGpp stimulates the GTPase, while higher concentrations inhibit.2 Publications

Kineticsi

Turnover number of 0.0061/min.

  1. KM=5.4 µM for GTP1 Publication
  1. Vmax=127 pmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721MagnesiumUniRule annotation
Metal bindingi192 – 1921MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1728GTPUniRule annotation
Nucleotide bindingi190 – 1945GTPUniRule annotation
Nucleotide bindingi212 – 2154GTPUniRule annotation
Nucleotide bindingi282 – 2854GTPUniRule annotation
Nucleotide bindingi310 – 3123GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sporulation

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU27920-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase ObgUniRule annotation (EC:3.6.5.-UniRule annotation1 Publication)
Alternative name(s):
GTP-binding protein Obg1 PublicationUniRule annotation
OrfA
Spo0B-associated GTP-binding protein
Gene namesi
Name:obgUniRule annotation
Ordered Locus Names:BSU27920
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

  • Note: Cofractionates with the ribosome and stress response regulators RsbR, RsbS and RsbT in size fractionation columns; binds to ribosomal protein L13.2 Publications

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Essential for growth, it cannot be disrupted. In depletion experiments cells become over 3-fold longer, are abnormally curved and nucleoids condense.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 846GRNADD → ERNADN: Stops growing at 45 degrees Celsius, shows sporulation onset defects. KM for GTP is 2.3 uM, turnover number is 0.015/min. 1 Publication
Mutagenesisi92 – 921G → D: Grows slowly, very reduced association with ribosomes, fewer 70S ribosomes in cells. No effect on sporulation or the general stress response. 1 Publication
Mutagenesisi407 – 42822RERGA…FEFID → SCRRASRIPAHWRPLLVDPS SVPSLA: No effect on growth or ribosomes, eliminates sporulation onset. Also decreases the general stress response to physical stress. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428GTPase ObgPRO_0000205432Add
BLAST

Proteomic databases

PaxDbiP20964.

Expressioni

Inductioni

Part of an operon with spo0B.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with TasA (AC P54507) in pull-down experiments.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiP20964. 1 interaction.
MINTiMINT-8366614.
STRINGi224308.Bsubs1_010100015261.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Beta strandi26 – 283Combined sources
Beta strandi44 – 485Combined sources
Helixi57 – 593Combined sources
Beta strandi63 – 653Combined sources
Beta strandi85 – 895Combined sources
Beta strandi93 – 975Combined sources
Turni98 – 1003Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi113 – 1175Combined sources
Helixi126 – 1283Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi148 – 1569Combined sources
Beta strandi161 – 1666Combined sources
Helixi171 – 1777Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi207 – 2126Combined sources
Helixi213 – 2197Combined sources
Turni223 – 2264Combined sources
Helixi227 – 23610Combined sources
Beta strandi239 – 2479Combined sources
Helixi254 – 26714Combined sources
Turni272 – 2743Combined sources
Beta strandi279 – 2824Combined sources
Helixi289 – 29911Combined sources
Helixi318 – 32811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNZX-ray2.60A/B1-342[»]
ProteinModelPortaliP20964.
SMRiP20964. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20964.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 329171OBG-type GUniRule annotationAdd
BLAST

Domaini

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 assocation, but eliminates sporulation and reduces the GSR, showing for the first time that growth promotion and the GSR phenotypes are separable.1 Publication

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.UniRule annotation
Contains 1 OBG-type G (guanine nucleotide-binding) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C9R. Bacteria.
COG0536. LUCA.
HOGENOMiHOG000019083.
InParanoidiP20964.
KOiK03979.
OMAiSKNQHGR.
OrthoDBiEOG6H1Q1M.
PhylomeDBiP20964.

Family and domain databases

Gene3Di2.70.210.12. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01454. GTPase_Obg.
InterProiIPR031167. G_OBG.
IPR014100. GTP-bd_Obg/CgtA.
IPR015349. GTP-bd_prot_GTP1/OBG_C.
IPR006074. GTP1-OBG_CS.
IPR006169. GTP1_OBG_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERiPTHR11702:SF3. PTHR11702:SF3. 2 hits.
PfamiPF09269. DUF1967. 1 hit.
PF01018. GTP1_OBG. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF002401. GTP_bd_Obg/CgtA. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF102741. SSF102741. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF82051. SSF82051. 1 hit.
TIGRFAMsiTIGR02729. Obg_CgtA. 1 hit.
TIGR03595. Obg_CgtA_exten. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
PS00905. GTP1_OBG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVDQVKVYV KGGDGGNGMV AFRREKYVPK GGPAGGDGGK GGDVVFEVDE
60 70 80 90 100
GLRTLMDFRY KKHFKAIRGE HGMSKNQHGR NADDMVIKVP PGTVVTDDDT
110 120 130 140 150
KQVIADLTEH GQRAVIARGG RGGRGNSRFA TPANPAPQLS ENGEPGKERY
160 170 180 190 200
IVLELKVLAD VGLVGFPSVG KSTLLSVVSS AKPKIADYHF TTLVPNLGMV
210 220 230 240 250
ETDDGRSFVM ADLPGLIEGA HQGVGLGHQF LRHIERTRVI VHVIDMSGLE
260 270 280 290 300
GRDPYDDYLT INQELSEYNL RLTERPQIIV ANKMDMPEAA ENLEAFKEKL
310 320 330 340 350
TDDYPVFPIS AVTREGLREL LFEVANQLEN TPEFPLYDEE ELTQNRVMYT
360 370 380 390 400
MENEEVPFNI TRDPDGVFVL SGDSLERLFK MTDFSRDESV KRFARQMRGM
410 420
GVDEALRERG AKDGDIIRLL EFEFEFID
Length:428
Mass (Da):47,689
Last modified:February 1, 1991 - v1
Checksum:iE57F6A88A80B0392
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24537 Genomic DNA. Translation: AAA22505.1.
AL009126 Genomic DNA. Translation: CAB14752.1.
X02655 Genomic DNA. Translation: CAA26490.1.
PIRiB32804.
RefSeqiNP_390670.1. NC_000964.3.
WP_003246161.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14752; CAB14752; BSU27920.
GeneIDi937502.
KEGGibsu:BSU27920.
PATRICi18977454. VBIBacSub10457_2916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24537 Genomic DNA. Translation: AAA22505.1.
AL009126 Genomic DNA. Translation: CAB14752.1.
X02655 Genomic DNA. Translation: CAA26490.1.
PIRiB32804.
RefSeqiNP_390670.1. NC_000964.3.
WP_003246161.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LNZX-ray2.60A/B1-342[»]
ProteinModelPortaliP20964.
SMRiP20964. Positions 1-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP20964. 1 interaction.
MINTiMINT-8366614.
STRINGi224308.Bsubs1_010100015261.

Proteomic databases

PaxDbiP20964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14752; CAB14752; BSU27920.
GeneIDi937502.
KEGGibsu:BSU27920.
PATRICi18977454. VBIBacSub10457_2916.

Phylogenomic databases

eggNOGiENOG4105C9R. Bacteria.
COG0536. LUCA.
HOGENOMiHOG000019083.
InParanoidiP20964.
KOiK03979.
OMAiSKNQHGR.
OrthoDBiEOG6H1Q1M.
PhylomeDBiP20964.

Enzyme and pathway databases

BioCyciBSUB:BSU27920-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP20964.

Family and domain databases

Gene3Di2.70.210.12. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01454. GTPase_Obg.
InterProiIPR031167. G_OBG.
IPR014100. GTP-bd_Obg/CgtA.
IPR015349. GTP-bd_prot_GTP1/OBG_C.
IPR006074. GTP1-OBG_CS.
IPR006169. GTP1_OBG_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERiPTHR11702:SF3. PTHR11702:SF3. 2 hits.
PfamiPF09269. DUF1967. 1 hit.
PF01018. GTP1_OBG. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF002401. GTP_bd_Obg/CgtA. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF102741. SSF102741. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF82051. SSF82051. 1 hit.
TIGRFAMsiTIGR02729. Obg_CgtA. 1 hit.
TIGR03595. Obg_CgtA_exten. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
PS00905. GTP1_OBG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein."
    Trach K., Hoch J.A.
    J. Bacteriol. 171:1362-1371(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GTP-BINDING, OPERON STRUCTURE, DISRUPTION PHENOTYPE.
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    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.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Sequence analysis of the spo0B locus reveals a polycistronic transcription unit."
    Ferrari F.A., Trach K.A., Hoch J.A.
    J. Bacteriol. 161:556-562(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
    Strain: 168.
  4. "Effects on Bacillus subtilis of a conditional lethal mutation in the essential GTP-binding protein Obg."
    Kok J., Trach K.A., Hoch J.A.
    J. Bacteriol. 176:7155-7160(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 79-GLY--ASP-84.
    Strain: 168 / JH642.
  5. "Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis."
    Welsh K.M., Trach K.A., Folger C., Hoch J.A.
    J. Bacteriol. 176:7161-7168(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GTP-BINDING, GTPASE ACTIVITY, POSSIBLE COFACTOR, ENZYME REGULATION.
    Strain: 168.
  6. "Possible role for the essential GTP-binding protein Obg in regulating the initiation of sporulation in Bacillus subtilis."
    Vidwans S.J., Ireton K., Grossman A.D.
    J. Bacteriol. 177:3308-3311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION IN SPORULATION.
    Strain: 168 / JH642.
  7. "Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma(B)."
    Scott J.M., Haldenwang W.G.
    J. Bacteriol. 181:4653-4660(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STRESS RESPONSE.
    Strain: PY22.
  8. "The Bacillus subtilis GTP binding protein obg and regulators of the sigma(B) stress response transcription factor cofractionate with ribosomes."
    Scott J.M., Ju J., Mitchell T., Haldenwang W.G.
    J. Bacteriol. 182:2771-2777(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, RIBOSOMAL ASSOCIATION, BINDING TO L13.
    Strain: PY22.
  9. "Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis."
    Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S., Ogasawara N.
    Microbiology 148:3539-3552(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN LEVELS, DISRUPTION PHENOTYPE.
    Strain: CRK6000.
  10. "Guanine nucleotides stabilize the binding of Bacillus subtilis Obg to ribosomes."
    Zhang S., Haldenwang W.G.
    Biochem. Biophys. Res. Commun. 322:565-569(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: RIBOSOMAL ASSOCIATION.
    Strain: PY22.
  11. "The growth-promoting and stress response activities of the Bacillus subtilis GTP binding protein Obg are separable by mutation."
    Kuo S., Demeler B., Haldenwang W.G.
    J. Bacteriol. 190:6625-6635(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF GLY-92 AND 407-ARG--ASP-428.
    Strain: 168 / BSA46.
  12. "Molecular modeling study for interaction between Bacillus subtilis Obg and nucleotides."
    Lee Y., Bang W.Y., Kim S., Lazar P., Kim C.W., Bahk J.D., Lee K.W.
    PLoS ONE 5:E12597-E12597(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MOLECULAR DYNAMIC SIMULATIONS.
  13. "Structural and biochemical analysis of the Obg GTP binding protein."
    Buglino J., Shen V., Hakimian P., Lima C.D.
    Structure 10:1581-1592(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-342 BOUND OR NOT BOUND TO NUCLEOTIDE, ENZYME REGULATION BY PPGPP, SUBUNIT, POSSIBLE INTERACTION WITH TASA.
  14. "The Obg subfamily of bacterial GTP-binding proteins: essential proteins of largely unknown functions that are evolutionarily conserved from bacteria to humans."
    Czyz A., Wegrzyn G.
    Acta Biochim. Pol. 52:35-43(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. "Obg/CtgA, a signaling protein that controls replication, translation, and morphological development?"
    Michel B.
    Dev. Cell 8:300-301(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiOBG_BACSU
AccessioniPrimary (citable) accession number: P20964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 17, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Estimated to be present at 6000 copies per cell.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.