EcoliHub logo

Try the new EcoliHub and let us know what you'd like to see.

tufA:Gene Product(s)

From EcoliWiki

Jump to: navigation, search


Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

protein chain elongation factor EF-Tu

Synonyms

protein chain elongation factor EF-Tu (duplicate of tufB)[1], protein chain elongation factor EF-Tu (duplicate of tufA)[1], B3339[2][1], PulT[2][1], KirT[2][1], TufA[2][1], EF-Tu[2][1]

Product description

elongation factor Tu[2][3]

EF-Tu, Elongation Factor-Translation, unstable; GTP-dependent binding of aa-tRNA to the A-site of ribosomes; has intrinsic GTPase activity when bound to kirromycin[4]

EC number (for enzymes)


Notes

Function

[back to top]


Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0046677

response to antibiotic

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0046

P

Seeded from EcoCyc [5]

complete

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc [5]

complete

GO:0006414

translational elongation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004541

P

Seeded from EcoCyc [5]

complete

GO:0006412

translation

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0648

P

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0005525

GTP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR000795
InterPro:IPR004160
InterPro:IPR004161
InterPro:IPR004541
InterPro:IPR005225
SP_KW:KW-0342
HAMAP:MF_00118

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003924

GTPase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000795

F

Seeded from EcoCyc [5]

complete

GO:0003746

translation elongation factor activity

GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR004541
SP_KW:KW-0251
HAMAP:MF_00118

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [5]

complete

GO:0006970

response to osmotic stress

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0005515

protein binding

PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]
PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P00956
UniProtKB:P04951
UniProtKB:P0A6P1
UniProtKB:P0A6Y5
UniProtKB:P0A6Z6
UniProtKB:P0A8J4
UniProtKB:P0A959
UniProtKB:P0ADX9
UniProtKB:P0AFQ7
UniProtKB:P0AG30
UniProtKB:P10441
UniProtKB:P15038
UniProtKB:P17888
UniProtKB:P22634
UniProtKB:P23367
UniProtKB:P23909
UniProtKB:P30750
UniProtKB:P33590
UniProtKB:P39408
UniProtKB:P61517
UniProtKB:P63389
UniProtKB:P76251
UniProtKB:P77756

F

Seeded from EcoCyc [5]

complete

GO:0005622

intracellular

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004541

C

Seeded from EcoCyc [5]

complete

GO:0005886

plasma membrane

GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-1003
SP_SL:SL-0039

C

Seeded from EcoCyc [5]

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner TypePartnerNotesReferencesEvidence

Protein

tsf

PMID:16606699[8]

Experiment(s):EBI-1145593, EBI-1145593

Protein

acrF

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

fbpC

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

ydhQ

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

rpsB

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

valS

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

xylA

PMID:15690043[7]

Experiment(s):EBI-894882

Protein

yaaA

PMID:15690043[7]

Experiment(s):EBI-894882

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Cytoplasm

PMID:7525272[9], PMID:7021545[10]

EchoLocation:tufA


Notes

Structure and Physical Properties

[back to top]


Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc

MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
Length

394

Mol. Wt

43.283 kDa

pI

5.3 (calculated)

Extinction coefficient

20,400 - 20,775 (calc based on 10 Y, 1 W, and 3 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

TypeResiduesDescriptionNotesReferences

Initiator Methionine

1

Removed

UniProt:P0A6N1

Modification Site

62

phosphorylation site at T62

probability greater than 75%

PMID:17938405[11]

Modification Site

159

phosphorylation site at S159

probability greater than 75%

PMID:17938405[11]

Modification Site

168

phosphorylation site at T168

probability less than 75%

PMID:17938405[11]

Modification Site

66

phosphorylation site at S66

probability less than 75%

PMID:17938405[11]

Modification Site

174

phosphorylation site at S174

probability less than 75%

PMID:17938405[11]

Modification Site

222

phosphorylation site at S222

probability greater than 75%

PMID:17938405[11]

Modification Site

65

phosphorylation site at T65

probability less than 75%

PMID:17938405[11]

Modification Site

313

phosphorylation site at S313

probability greater than 75%

PMID:17938405[11]

Modification Site

332

phosphorylation site at Y332

probability greater than 75%

PMID:17938405[11]


rectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglerectanglemotifs

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures
Models

View models at:

Structure figures

Notes

Gene Product Resources

[back to top]


See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource typeSourceNotes/Reference

Notes

Accessions in Other Databases

[back to top]


See Help:Gene_accessions for help with entering information into the Gene Accessions table.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:EG11036-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A6N1

PFAM (EcoliWiki Page)

PFAM:PF00009

RefSeq (EcoliWiki Page)

RefSeq:NP_417798


Notes

Links

[back to top]




References

[back to top]


See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 5.8 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. 6.0 6.1 6.2 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 7.11 7.12 7.13 7.14 7.15 7.16 7.17 7.18 7.19 7.20 7.21 7.22 7.23 7.24 7.25 7.26 7.27 7.28 7.29 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
  8. Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  9. Mesters JR et al. (1994) The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli. EMBO J 13: 4877-85 PubMed EcoliWiki page
  10. Laursen RA et al. (1981) The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence. J Biol Chem 256: 8102-9 PubMed EcoliWiki page
  11. 11.0 11.1 11.2 11.3 11.4 11.5 11.6 11.7 11.8 Macek B et al. (2007) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics PubMed EcoliWiki page

Categories

[back to top]

Personal tools