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P50743 (DER_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTPase Der
Alternative name(s):
GTP-binding protein EngA
Gene names
Name:der
Synonyms:engA, yphC
Ordered Locus Names:BSU22840
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase that plays an essential role in the late steps of ribosome biogenesis. Ref.5

Subunit structure

Cofractionates with the 70S ribosome; association is stabilized by the non-hydrolyzable GTP analog GMPPNP, and inhibited by GTP or GDP. Ref.5

Disruption phenotype

Essential for growth, it cannot be disrupted. Depletion experiments show that cells become longer and abnormally curved, with nucleoid condensation. Cells have many fewer 70S ribosomes; the large ribosomal subunit is 45S and is missing proteins L16, L27, L36 and interacts with 2 large non-ribosomal proteins. Ref.4

Miscellaneous

Estimated to be present at 7000 copies per cell.

Sequence similarities

Belongs to the Era/MnmE GTP-binding protein family. Der subfamily.

Contains 2 G (guanine nucleotide-binding) domains.

Contains 1 KH-like domain.

Sequence caution

The sequence U32164 differs from that shown. Reason: Frameshift at position 208.

Ontologies

Keywords
   Biological processRibosome biogenesis
   DomainRepeat
   LigandGTP-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436GTPase Der HAMAP-Rule MF_00195
PRO_0000178964

Regions

Domain15 – 120106G 1
Domain187 – 295109G 2
Domain351 – 43686KH-like
Nucleotide binding10 – 178GTP 1 Potential
Nucleotide binding57 – 615GTP 1 Potential
Nucleotide binding119 – 1224GTP 1 Potential
Nucleotide binding182 – 1898GTP 2 Potential
Nucleotide binding229 – 2335GTP 2 Potential
Nucleotide binding294 – 2974GTP 2 Potential

Experimental info

Sequence conflict186 – 1872VG → CR Ref.2

Secondary structure

............................................................................. 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50743 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A5CC7028FFB5A442

FASTA43648,770
        10         20         30         40         50         60 
MGKPVVAIVG RPNVGKSTIF NRIAGERISI VEDTPGVTRD RIYSSAEWLN YDFNLIDTGG 

        70         80         90        100        110        120 
IDIGDEPFLA QIRQQAEIAM DEADVIIFMV NGREGVTAAD EEVAKILYRT KKPVVLAVNK 

       130        140        150        160        170        180 
LDNTEMRANI YDFYSLGFGE PYPISGTHGL GLGDLLDAVA EHFKNIPETK YNEEVIQFCL 

       190        200        210        220        230        240 
IGRPNVGKSS LVNAMLGEER VIVSNVAGTT RDAVDTSFTY NQQEFVIVDT AGMRKKGKVY 

       250        260        270        280        290        300 
ETTEKYSVLR ALKAIDRSEV VAVVLDGEEG IIEQDKRIAG YAHEAGKAVV IVVNKWDAVD 

       310        320        330        340        350        360 
KDESTMKEFE ENIRDHFQFL DYAPILFMSA LTKKRIHTLM PAIIKASENH SLRVQTNVLN 

       370        380        390        400        410        420 
DVIMDAVAMN PTPTHNGSRL KIYYATQVSV KPPSFVVFVN DPELMHFSYE RFLENRIRDA 

       430 
FGFEGTPIKI FARARK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome."
Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P.
Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[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. expand/collapse author list , 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]"Synthesis of sn-glycerol 3-phosphate, a key precursor of membrane lipids, in Bacillus subtilis."
Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.
J. Bacteriol. 177:5899-5905(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-436.
Strain: 168.
[4]"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: GTP- AND GDP-BINDING, PROTEIN LEVELS, DISRUPTION PHENOTYPE.
Strain: CRK6000.
[5]"Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis."
Schaefer L., Uicker W.C., Wicker-Planquart C., Foucher A.-E., Jault J.-M., Britton R.A.
J. Bacteriol. 188:8252-8258(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE 50S RIBOSOMAL SUBUNIT, FUNCTION IN 50S RIBOSOMAL SUBUNIT BIOGENESIS.
Strain: RB247.
[6]"The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding."
Muench S.P., Xu L., Sedelnikova S.E., Rice D.W.
Proc. Natl. Acad. Sci. U.S.A. 103:12359-12364(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) BOUND TO GDP IN THE PROBABLE OFF STATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L47648 Genomic DNA. Translation: AAC83966.1.
AL009126 Genomic DNA. Translation: CAB14200.1.
U32164 Genomic DNA. No translation available.
PIRA69936.
RefSeqNP_390165.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HJGX-ray2.50A1-436[»]
4DCSX-ray2.25A1-436[»]
4DCTX-ray2.30A1-436[»]
4DCUX-ray2.00A1-436[»]
4DCVX-ray2.60A1-436[»]
ProteinModelPortalP50743.
SMRP50743. Positions 3-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU22840.

Proteomic databases

PaxDbP50743.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14200; CAB14200; BSU22840.
GeneID938988.
KEGGbsu:BSU22840.
PATRIC18976379. VBIBacSub10457_2380.

Organism-specific databases

GenoListBSU22840. [Micado]

Phylogenomic databases

eggNOGCOG1160.
HOGENOMHOG000242861.
KOK03977.
OMAYLENTYR.
OrthoDBEOG6DC6K1.
ProtClustDBPRK00093.

Enzyme and pathway databases

BioCycBSUB:BSU22840-MONOMER.

Family and domain databases

Gene3D3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_00195. GTPase_Der.
InterProIPR016484. GTP-bd_EngA.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERPTHR11649:SF5. PTHR11649:SF5. 1 hit.
PfamPF01926. MMR_HSR1. 2 hits.
[Graphical view]
PIRSFPIRSF006485. GTP-binding_EngA. 1 hit.
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03594. GTPase_EngA. 1 hit.
TIGR00231. small_GTP. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP50743.

Entry information

Entry nameDER_BACSU
AccessionPrimary (citable) accession number: P50743
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList