P20964 (OBG_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTPase ObgE

Alternative name(s):
GTP-binding protein obg
OrfA
Spo0B-associated GTP-binding protein

Gene names

Name:	obg
Ordered Locus Names:	BSU27920

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7
Cofactor	Magnesium Probable. Ref.5
Enzyme regulation	Inhibited by GDP; less than 20 µM ppGpp stimulates the GTPase, while higher concentrations inhibit. Ref.5 Ref.12
Subunit structure	Monomer. Interacts with TasA (AC P54507) in pull-down experiments. Ref.5 Ref.12
Subcellular location	Cytoplasm. Note: Cofractionates with the ribosome and stress response regulators RsbR, RsbS and RsbT in size fractionation columns; binds to ribosomal protein L13. Ref.8
Induction	Part of an operon with spo0B. Ref.5 Ref.12
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 assocation, but eliminates sporulation and reduces the GSR, showing for the first time that growth promotion and the GSR phenotypes are separable. HAMAP-Rule MF_01454
Disruption phenotype	Essential for growth, it cannot be disrupted. In depletion experiments cells become over 3-fold longer, are abnormally curved and nucleoids condense. Ref.1 Ref.9
Miscellaneous	Estimated to be present at 6000 copies per cell. HAMAP-Rule MF_01454
Sequence similarities	Belongs to the GTP1/OBG family. Contains 1 G (guanine nucleotide-binding) domain.
Biophysicochemical properties	Kinetic parameters: Turnover number of 0.0061/min. KM=5.4 µM for GTP Ref.5 Vmax=127 pmol/min/mg enzyme

Ontologies

Keywords
Biological process	Sporulation
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

GTPase ObgE HAMAP-Rule MF_01454

PRO_0000205432

Regions

Domain

170 – 283

114

G

Nucleotide binding

165 – 172

8

GTP By similarity

Nucleotide binding

212 – 216

5

GTP By similarity

Nucleotide binding

282 – 285

4

GTP By similarity

Experimental info

Mutagenesis

79 – 84

6

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. Ref.4

Mutagenesis

92

1

G → D: Grows slowly, very reduced association with ribosomes, fewer 70S ribosomes in cells. No effect on sporulation or the general stress response. Ref.11

Mutagenesis

407 – 428

22

RERGA…FEFID → SCRRASRIPAHWRPLLVDPS SVPSLA: No effect on growth or ribosomes, eliminates sporulation onset. Also decreases the general stress response to physical stress. Ref.11

Secondary structure

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428

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Beta strand

26 – 28

3

Beta strand

44 – 48

5

Helix

57 – 59

3

Beta strand

63 – 65

3

Beta strand

85 – 89

5

Beta strand

93 – 97

5

Turn

98 – 100

3

Beta strand

103 – 107

5

Beta strand

113 – 117

5

Helix

126 – 128

3

Beta strand

134 – 136

3

Beta strand

148 – 156

9

Beta strand

161 – 166

6

Helix

171 – 177

7

Beta strand

178 – 181

4

Beta strand

184 – 187

4

Beta strand

197 – 201

5

Beta strand

203 – 205

3

Beta strand

207 – 212

6

Helix

213 – 219

7

Turn

223 – 226

4

Helix

227 – 236

10

Beta strand

239 – 247

9

Helix

254 – 267

14

Turn

272 – 274

3

Beta strand

279 – 282

4

Helix

289 – 299

11

Helix

318 – 328

11

Sequences

	Sequence		Length	Mass (Da)
	P20964 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: E57F6A88A80B0392	FASTA	428	47,689
	10 20 30 40 50 60 MFVDQVKVYV KGGDGGNGMV AFRREKYVPK GGPAGGDGGK GGDVVFEVDE GLRTLMDFRY 70 80 90 100 110 120 KKHFKAIRGE HGMSKNQHGR NADDMVIKVP PGTVVTDDDT KQVIADLTEH GQRAVIARGG 130 140 150 160 170 180 RGGRGNSRFA TPANPAPQLS ENGEPGKERY IVLELKVLAD VGLVGFPSVG KSTLLSVVSS 190 200 210 220 230 240 AKPKIADYHF TTLVPNLGMV ETDDGRSFVM ADLPGLIEGA HQGVGLGHQF LRHIERTRVI 250 260 270 280 290 300 VHVIDMSGLE GRDPYDDYLT INQELSEYNL RLTERPQIIV ANKMDMPEAA ENLEAFKEKL 310 320 330 340 350 360 TDDYPVFPIS AVTREGLREL LFEVANQLEN TPEFPLYDEE ELTQNRVMYT MENEEVPFNI 370 380 390 400 410 420 TRDPDGVFVL SGDSLERLFK MTDFSRDESV KRFARQMRGM GVDEALRERG AKDGDIIRLL EFEFEFID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 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: MUTAGENESIS OF GLY-92 AND 407-ARG--ASP-428. Strain: 168 / BSA46.
[12]	"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.
[13]	"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.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M24537 Genomic DNA. Translation: AAA22505.1.
AL009126 Genomic DNA. Translation: CAB14752.1.
X02655 Genomic DNA. Translation: CAA26490.1.

PIR

B32804.

RefSeq

NP_390670.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LNZ	X-ray	2.60	A/B	1-342	[»]

ProteinModelPortal

P20964.

SMR

P20964. Positions 1-428.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU27920.

Proteomic databases

PaxDb

P20964.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14752; CAB14752; BSU27920.

GeneID

937502.

KEGG

bsu:BSU27920.

PATRIC

18977454. VBIBacSub10457_2916.

Organism-specific databases

GenoList

BSU27920. [Micado]

Phylogenomic databases

eggNOG

COG0536.

HOGENOM

HOG000019083.

KO

K03979.

OMA

NRNRAPE.

ProtClustDB

PRK12297.

Enzyme and pathway databases

BioCyc

BSUB:BSU27920-MONOMER.

Family and domain databases

Gene3D

2.70.210.12. 1 hit.

HAMAP

MF_01454. GTPase_Obg.

InterPro

IPR014100. GTP-bd_Obg/CgtA.
IPR015349. GTP-bd_prot_GTP1/OBG_C.
IPR006074. GTP1-OBG_CS.
IPR006169. GTP1_OBG_dom.
IPR006073. GTP_binding_domain.
IPR005225. Small_GTP-bd_dom.
[Graphical view]

PANTHER

PTHR11702:SF3. PTHR11702:SF3. 1 hit.

Pfam

PF09269. DUF1967. 1 hit.
PF01018. GTP1_OBG. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]

PIRSF

PIRSF002401. GTP_bd_Obg/CgtA. 1 hit.

PRINTS

PR00326. GTP1OBG.

SUPFAM

SSF102741. GTP-bd_prot_GTP1/OBG_C. 1 hit.
SSF82051. GTP1_OBG_sub. 1 hit.

TIGRFAMs

TIGR02729. Obg_CgtA. 1 hit.
TIGR03595. Obg_CgtA_exten. 1 hit.
TIGR00231. small_GTP. 1 hit.

PROSITE

PS00905. GTP1_OBG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20964.

Entry information

Entry name

OBG_BACSU

Accession

Primary (citable) accession number: P20964

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program