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A1KRF9 (EFTU_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Elongation factor Tu

Short name=EF-Tu
Gene names
Name:tuf1
Ordered Locus Names:NMC0116
AND
Name:tuf2
Ordered Locus Names:NMC0128
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis By similarity. HAMAP-Rule MF_00118

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00118.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337441

Regions

Nucleotide binding19 – 268GTP By similarity
Nucleotide binding81 – 855GTP By similarity
Nucleotide binding136 – 1394GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KRF9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0C571C3D20CBE944

FASTA39442,909
        10         20         30         40         50         60 
MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTTILAKKF GGAAKAYDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI 

       130        140        150        160        170        180 
LLARQVGVPY IIVFMNKCDM VDDAELLELV EMEIRDLLSS YDFPGDDCPI VQGSALKALE 

       190        200        210        220        230        240 
GDAAYEEKIF ELAAALDSYI PTPERAVDKP FLLPIEDVFS ISGRGTVVTG RVERGIIHVG 

       250        260        270        280        290        300 
DEIEIVGLKE TQKTTCTGVE MFRKLLDEGQ AGDNVGVLLR GTKREDVERG QVLAKPGTIT 

       310        320        330        340        350        360 
PHTKFKAEVY VLSKEEGGRH TPFFANYRPQ FYFRTTDVTG AVTLEEGVEM VMPGENVTIT 

       370        380        390 
VELIAPIAME EGLRFAIREG GRTVGAGVVS SVIA 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM09435.1.
AM421808 Genomic DNA. Translation: CAM09447.1.
RefSeqYP_974247.1. NC_008767.1.
YP_974259.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KRF9.
SMRA1KRF9. Positions 2-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC0128.

Proteomic databases

PRIDEA1KRF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09435; CAM09435; NMC0116.
CAM09447; CAM09447; NMC0128.
GeneID4675020.
4676668.
KEGGnmc:NMC0116.
nmc:NMC0128.
PATRIC20349729. VBINeiMen17609_0130.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAGTEMCMP.
OrthoDBEOG6R5C6X.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-117-MONOMER.
NMEN272831:GJDX-130-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004541. Transl_elong_EFTu/EF1A_bac/org.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEFTU_NEIMF
AccessionPrimary (citable) accession number: A1KRF9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 58 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