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Protein

GTPase Obg

Gene

obg

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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

Keywordsi

Molecular functionHydrolase
Biological processSporulation
LigandGTP-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

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
PRIDEiP20964

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
MINTiP20964
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

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

Phylogenomic databases

eggNOGiENOG4105C9R Bacteria
COG0536 LUCA
HOGENOMiHOG000019083
InParanoidiP20964
KOiK03979
OMAiPHVGIVH
PhylomeDBiP20964

Family and domain databases

CDDicd01898 Obg, 1 hit
Gene3Di2.40.240.60, 1 hit
2.70.210.12, 1 hit
HAMAPiMF_01454 GTPase_Obg, 1 hit
InterProiView protein in InterPro
IPR031167 G_OBG
IPR035101 GTP-bd_Obg
IPR014100 GTP-bd_Obg/CgtA
IPR015349 GTP-bd_prot_GTP1/OBG_C
IPR036346 GTP-bd_prot_GTP1/OBG_C_sf
IPR006074 GTP1-OBG_CS
IPR006169 GTP1_OBG_dom
IPR036726 GTP1_OBG_dom_sf
IPR006073 GTP_binding_domain
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
PfamiView protein in Pfam
PF09269 DUF1967, 1 hit
PF01018 GTP1_OBG, 1 hit
PF01926 MMR_HSR1, 1 hit
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
PROSITEiView protein in PROSITE
PS51710 G_OBG, 1 hit
PS00905 GTP1_OBG, 1 hit

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
PATRICifig|224308.179.peg.3033

Similar proteinsi

Entry informationi

Entry nameiOBG_BACSU
AccessioniPrimary (citable) accession number: P20964
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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