Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi172MagnesiumUniRule annotation1
Metal bindingi192MagnesiumUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi165 – 172GTPUniRule annotation8
Nucleotide bindingi190 – 194GTPUniRule annotation5
Nucleotide bindingi212 – 215GTPUniRule annotation4
Nucleotide bindingi282 – 285GTPUniRule annotation4
Nucleotide bindingi310 – 312GTPUniRule annotation3

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)DescriptionActionsGraphical viewLength
Mutagenesisi79 – 84GRNADD → 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 Publication6
Mutagenesisi92G → D: Grows slowly, very reduced association with ribosomes, fewer 70S ribosomes in cells. No effect on sporulation or the general stress response. 1 Publication1
Mutagenesisi407 – 428RERGA…FEFID → SCRRASRIPAHWRPLLVDPS SVPSLA: No effect on growth or ribosomes, eliminates sporulation onset. Also decreases the general stress response to physical stress. 1 PublicationAdd BLAST22

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002054321 – 428GTPase ObgAdd BLAST428

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 interactor.
MINTiMINT-8366614.
STRINGi224308.Bsubs1_010100015261.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 11Combined sources10
Beta strandi26 – 28Combined sources3
Beta strandi44 – 48Combined sources5
Helixi57 – 59Combined sources3
Beta strandi63 – 65Combined sources3
Beta strandi85 – 89Combined sources5
Beta strandi93 – 97Combined sources5
Turni98 – 100Combined sources3
Beta strandi103 – 107Combined sources5
Beta strandi113 – 117Combined sources5
Helixi126 – 128Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi148 – 156Combined sources9
Beta strandi161 – 166Combined sources6
Helixi171 – 177Combined sources7
Beta strandi178 – 181Combined sources4
Beta strandi184 – 187Combined sources4
Beta strandi197 – 201Combined sources5
Beta strandi203 – 205Combined sources3
Beta strandi207 – 212Combined sources6
Helixi213 – 219Combined sources7
Turni223 – 226Combined sources4
Helixi227 – 236Combined sources10
Beta strandi239 – 247Combined sources9
Helixi254 – 267Combined sources14
Turni272 – 274Combined sources3
Beta strandi279 – 282Combined sources4
Helixi289 – 299Combined sources11
Helixi318 – 328Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20964.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini159 – 329OBG-type GUniRule annotationAdd BLAST171

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 association, 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.
PhylomeDBiP20964.

Family and domain databases

Gene3Di2.70.210.12. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01454. GTPase_Obg. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LNZX-ray2.60A/B1-342[»]
ProteinModelPortaliP20964.
SMRiP20964.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP20964. 1 interactor.
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.
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. 1 hit.
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...

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: November 30, 2016
This is version 131 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.