aat:Gene Product(s)

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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

Aat

Synonyms

leucyl/phenylalanyl-tRNA-protein transferase[1], B0885[2][1], YcaA[2][1], Aat[2][1] , ECK0876, JW0868, ycaA, b0885

Product description

leucyl, phenylalanyl-tRNA-protein transferase[2][3]

Leucyl, phenylalanyl-tRNA-protein transferase; L/F-transferase; transfers Leu or Phe to N-terminal Arg or Lys residues; required for the N-end rule degradation by ClpAP protease[4]

EC number (for enzymes)
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Notes

Function

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

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00688

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0030163

protein catabolic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00688

P

Seeded from EcoCyc (v14.0)

complete

GO:0030163

protein catabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004616

P

Seeded from EcoCyc (v14.0)

complete

GO:0008914

leucyltransferase activity

PMID:4909560[5]

IDA: Inferred from Direct Assay

F

complete

GO:0008914

leucyltransferase activity

PMID:7657641[6]

IDA: Inferred from Direct Assay

F

Table 1

complete

GO:0005737

cytoplasm

PMID:4909560[5]

IDA: Inferred from Direct Assay

C

complete

GO:0016755

transferase activity, transferring amino-acyl groups

PMID:4909560[5]

IDA: Inferred from Direct Assay

F

Aat catalyzes the transfer of both leucine and phenylalanine from tRNAs to protein. Specificity for leucyl- and phenyl-tRNAs is presented in Table II.

complete

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

Partner Type Partner Notes References Evidence

Protein

yjdA

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

infA

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

bglX

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

speA

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

groL

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

ninE

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

kdpB

PMID:16606699[7]

Experiment(s):EBI-1138274

Protein

galF

PMID:19402753[8]

MALDI(Z-score):28.162890

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Notes

Localization

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

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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

Name
Sequence

at EcoCyc 

MRLVQLSRHS IAFPSPEGAL REPNGLLALG GDLSPARLLM AYQRGIFPWF SPGDPILWWS
PDPRAVLWPE SLHISRSMKR FHKRSPYRVT MNYAFGQVIE GCASDREEGT WITRGVVEAY
HRLHELGHAH SIEVWREDEL VGGMYGVAQG TLFCGESMFS RMENASKTAL LVFCEEFIGH
GGKLIDCQVL NDHTASLGAC EIPRRDYLNY LNQMRLGRLP NNFWVPRCLF SPQE
Length

234

Mol. Wt

26.618 kDa

pI

7.2 (calculated)

Extinction coefficient

48,930 - 49,680 (calc based on 7 Y, 7 W, and 6 C residues)

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Domains/Motifs/Modification Sites

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

Type Residues Description Notes References

Domain

34..204

PF03588 Leucyl/phenylalanyl-tRNA protein transferase

PMID:19920124[9]

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

Structures

<beststructure> gene=aat taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128852

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945490

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0003009

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A8P1

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11112

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11112

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945490

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001098

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1103

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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

  1. ↑ 1.0 1.1 1.2 1.3 1.4 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 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 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 Leibowitz, MJ & Soffer, RL (1970) Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli. J. Biol. Chem. 245 2066-73 PubMed
  6. ↑ Abramochkin, G & Shrader, TE (1995) The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure. J. Biol. Chem. 270 20621-8 PubMed
  7. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  8. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  9. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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