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Q9X1F8 (DER_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=TmDer
Alternative name(s):
GTP-binding protein EngA
Gene names
Name:der
Synonyms:engA
Ordered Locus Names:TM_1446
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length439 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 By similarity. Has GTPase activity but no ATPase activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and UTP compete for GTP binding. HAMAP-Rule MF_00195

Subunit structure

Associates with the 50S ribosomal subunit By similarity.

Domain

Each G (guanine nucleotide-binding) domain has activity on its own; domain 1 is twice as active as domain 2. The G domains do not interact, instead each contacts the C-terminal KH-like domain which lies between them. Ref.3

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.

Contains 2 EngA-type G (guanine nucleotide-binding) domains.

Contains 1 KH-like domain.

Biophysicochemical properties

Kinetic parameters:

At pH 7.5, 70 degrees Celsius, 5 mM MgCl2 and 400 mM KCl.

KM=110 µM for GTP Ref.2

Vmax=0.35 µmol/min/µg enzyme

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 – 439439GTPase Der HAMAP-Rule MF_00195
PRO_0000179064

Regions

Domain2 – 168167EngA-type G 1
Domain181 – 357177EngA-type G 2
Domain358 – 43982KH-like
Nucleotide binding8 – 158GTP 1 Potential
Nucleotide binding55 – 595GTP 1 Potential
Nucleotide binding118 – 1214GTP 1 Potential
Nucleotide binding190 – 1945GTP 2 HAMAP-Rule MF_00195
Nucleotide binding300 – 3034GTP 2 HAMAP-Rule MF_00195
Nucleotide binding336 – 3372GTP 2 HAMAP-Rule MF_00195

Experimental info

Mutagenesis1181N → D: 10% of GTPase activity remains. Ref.3
Mutagenesis3001N → D: Slight increase of GTPase activity. Ref.3

Secondary structure

................................................................................ 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X1F8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 29CA321453249B58

FASTA43950,015
        10         20         30         40         50         60 
MATVLIVGRP NVGKSTLFNK LVKKKKAIVE DEEGVTRDPV QDTVEWYGKT FKLVDTCGVF 

        70         80         90        100        110        120 
DNPQDIISQK MKEVTLNMIR EADLVLFVVD GKRGITKEDE SLADFLRKST VDTILVANKA 

       130        140        150        160        170        180 
ENLREFEREV KPELYSLGFG EPIPVSAEHN INLDTLLETI IKKLEEKGLD LESKPEITDA 

       190        200        210        220        230        240 
IKVAIVGRPN VGKSTLFNAI LNKERALVSP IPGTTRDPVD DEVFIDGRKY VFVDTAGLRR 

       250        260        270        280        290        300 
KSRVEPRTVE KYSNYRVVDS IEKADVVVIV LDATQGITRQ DQRIAGLVER RGRASVVVFN 

       310        320        330        340        350        360 
KWDLVEHREK RYDEFTKLFR EKLYFIDYSP LIFTSADKGW NIDRVIDAIN LAYASYTTKV 

       370        380        390        400        410        420 
PSSAINSALQ KVLAFTNLPR GLKIFFGLQV DIKPPTFLFF VNSIEKVKNP QKIFLRKLIR 

       430 
DYVFPFEGSP IFLKFKRSR 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"An essential GTPase, der, containing double GTP-binding domains from Escherichia coli and Thermotoga maritima."
Hwang J., Inouye M.
J. Biol. Chem. 276:31415-31421(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
[3]"Domain arrangement of Der, a switch protein containing two GTPase domains."
Robinson V.L., Hwang J., Fox E., Inouye M., Stock A.M.
Structure 10:1649-1658(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GDP, GTPASE ACTIVITY, GTP-BINDING, DOMAINS, MUTAGENESIS OF ASN-118 AND ASN-300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36514.1.
PIRB72253.
RefSeqNP_229245.1. NC_000853.1.
YP_007977801.1. NC_021214.1.
YP_008991465.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKYX-ray1.90A1-439[»]
ProteinModelPortalQ9X1F8.
SMRQ9X1F8. Positions 2-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1446.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36514; AAD36514; TM_1446.
GeneID898030.
KEGGtma:TM1446.
tmi:THEMA_07085.
tmm:Tmari_1452.
PATRIC23937844. VBITheMar51294_1460.

Phylogenomic databases

eggNOGCOG1160.
KOK03977.
OMASQGRGIN.
OrthoDBEOG6DC6K1.

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.
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03594. GTPase_EngA. 1 hit.
TIGR00231. small_GTP. 2 hits.
PROSITEPS51712. G_ENGA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9X1F8.

Entry information

Entry nameDER_THEMA
AccessionPrimary (citable) accession number: Q9X1F8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 107 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