Skip Header

Contribute Send feedback
Read comments (?) or add your own

C8TZR2 (C8TZR2_ECO10) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 32. Feed History...

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

Names and origin

Protein namesRecommended name:
Elongation factor Tu HAMAP-Rule MF_00118
Short name=EF-Tu HAMAP-Rule MF_00118
Gene names
Name:tufB EMBL BAI33424.1
Synonyms:tuf HAMAP-Rule MF_00118
Ordered Locus Names:ECO103_4729 EMBL BAI33424.1
OrganismEscherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP] EMBL BAI33424.1
Taxonomic identifier585395 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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. RuleBase RU000325 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. RuleBase RU000325 HAMAP-Rule MF_00118

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding19 – 268GTP By similarity HAMAP-Rule MF_00118
Nucleotide binding81 – 855GTP By similarity HAMAP-Rule MF_00118
Nucleotide binding136 – 1394GTP By similarity HAMAP-Rule MF_00118

Amino acid modifications

Modified residue3141N6-acetyllysine By similarity HAMAP-Rule MF_00118

Sequences

Sequence LengthMass (Da)Tools
C8TZR2 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 6EDA60255F43358F

FASTA39443,314
        10         20         30         40         50         60 
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG 

        70         80         90        100        110        120 
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI 

       130        140        150        160        170        180 
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE 

       190        200        210        220        230        240 
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG 

       250        260        270        280        290        300 
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK 

       310        320        330        340        350        360 
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV 

       370        380        390 
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12009 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010958 Genomic DNA. Translation: BAI33424.1.
RefSeqYP_003224558.1. NC_013353.1.

3D structure databases

ProteinModelPortalC8TZR2.
SMRC8TZR2. Positions 9-394.
ModBaseSearch...

Protein-protein interaction databases

STRING585395.ECO103_4729.
C8TZR2.

Proteomic databases

PRIDEC8TZR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI33424; BAI33424; ECO103_4729.
GeneID8476931.
KEGGeoh:ECO103_4729.
PATRIC32101668. VBIEscCol146794_4956.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
KOK02358.
OMACEFVGYN.
ProtClustDBPRK12735.

Enzyme and pathway databases

BioCycECOL585395:GJA9-4907-MONOMER.

Family and domain databases

HAMAPMF_00118_B. EF_Tu_B.
InterProIPR000795. EF_GTP-bd_dom.
IPR005225. Small_GTP-bd_dom.
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.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC8TZR2_ECO10
AccessionPrimary (citable) accession number: C8TZR2
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info