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A5I7K8 (EFTU_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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
Synonyms:tufA
Ordered Locus Names:CBO3482, CLC_3427
AND
Name:tuf2
Synonyms:tufB
Ordered Locus Names:CBO3496, CLC_3441
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length397 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
Reference 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 – 397397Elongation factor Tu HAMAP-Rule MF_00118
PRO_0000337357

Regions

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

Sequences

Sequence LengthMass (Da)Tools
A5I7K8 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 75AD3C5B65D90FA8

FASTA39743,483
        10         20         30         40         50         60 
MAKAKFERSK PHVNIGTIGH VDHGKTTLTA AITTVLAQKG GASATKYDEI DKAPEEKERG 

        70         80         90        100        110        120 
ITINTSHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI 

       130        140        150        160        170        180 
LLASRVGVQY IVVFLNKADQ VDDPELIELV EMEVRELLNE YGFPGDDTPI VVGSALEVLE 

       190        200        210        220        230        240 
NQDNAEKTKC IDELMEAIDS YIPTPERATD QPFLMPVEDV FTITGRGTVA TGRVERGVLH 

       250        260        270        280        290        300 
TGDEVELIGM KQEVSKTVCT GIEMFRKILD EAMAGDNIGA LLRGIQRDEI QRGQVLAKPG 

       310        320        330        340        350        360 
SVTPHKKFVG QVYVLKKEEG GRHTPFFNGY RPQFYFRTTD VTGSINLPEG VEMVMPGDHI 

       370        380        390 
DMAVELITPV AMHENLRFAI REGGRTVGSG VVTTISE 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS37793.1.
CP000727 Genomic DNA. Translation: ABS39226.1.
AM412317 Genomic DNA. Translation: CAL85043.1.
AM412317 Genomic DNA. Translation: CAL85057.1.
RefSeqYP_001255964.1. NC_009495.1.
YP_001255978.1. NC_009495.1.
YP_001389205.1. NC_009698.1.
YP_001389219.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I7K8.
SMRA5I7K8. Positions 2-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413999.CBO3496.

Proteomic databases

PRIDEA5I7K8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS37793; ABS37793; CLC_3441.
ABS39226; ABS39226; CLC_3427.
GeneID5187735.
5187740.
5401095.
5401647.
KEGGcbh:CLC_3427.
cbh:CLC_3441.
cbo:CBO3482.
cbo:CBO3496.

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMAVTPHTEF.
OrthoDBEOG6R5C6X.
ProtClustDBPRK00049.

Enzyme and pathway databases

BioCycCBOT413999:GJ72-3616-MONOMER.
CBOT413999:GJ72-3630-MONOMER.
CBOT441771:GIWX-3374-MONOMER.
CBOT441771:GIWX-3388-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_CLOBH
AccessionPrimary (citable) accession number: A5I7K8
Secondary accession number(s): A7G8U0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 49 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