Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KRA7 (LFTR_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:
Leucyl/phenylalanyl-tRNA--protein transferase

EC=2.3.2.6
Alternative name(s):
L/F-transferase
Leucyltransferase
Phenyalanyltransferase
Gene names
Name:aat
Ordered Locus Names:VC_1735
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine By similarity. HAMAP-Rule MF_00688

Catalytic activity

L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + L-leucyl-[protein]. HAMAP-Rule MF_00688

L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein]. HAMAP-Rule MF_00688

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00688.

Sequence similarities

Belongs to the L/F-transferase family.

Sequence caution

The sequence AAB87633.1 differs from that shown. Reason: Frameshift at position 206.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein catabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from sequence or structural similarity Ref.1. Source: TIGR

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionleucyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

peptidase activity

Inferred from sequence or structural similarity Ref.1. Source: TIGR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_0000207247

Sequences

Sequence LengthMass (Da)Tools
Q9KRA7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 24AF885AE888D515

FASTA24327,569
        10         20         30         40         50         60 
MAIYLTELSP ETLTFPSPFT ALDDPNGLLA FGGDLRLERI WAAYQQGIFP WYGPEDPILW 

        70         80         90        100        110        120 
WSPSPRAVFD PTRFQPAKSV KKFQRKHQYR VSVNHATSQV IEQCALTRPA DQRWLNDSMR 

       130        140        150        160        170        180 
HAYGELAKQG RCHSVEVWQG EQLVGGLYGI SVGQLFCGES MFSLATNASK IALWYFCDHF 

       190        200        210        220        230        240 
SRHQGQLIDC QVMNPHLQSL GATTLSREQF IQSLLSFKEK QVLSGCFETQ WLATPTSPCA 


FED 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.
[2]"Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase. Conservation within the enzyme family and localization to the trypsin-resistant domain."
Ichetovkin I.E., Abramochkin G., Shrader T.E.
J. Biol. Chem. 272:33009-33014(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94885.1.
AF035002 Genomic DNA. Translation: AAB87633.1. Frameshift.
PIRG82163.
RefSeqNP_231371.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KRA7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC1735.

Protocols and materials databases

DNASU2613740.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94885; AAF94885; VC_1735.
GeneID2613740.
KEGGvch:VC1735.
PATRIC20082524. VBIVibCho83274_1658.

Phylogenomic databases

eggNOGCOG2360.
KOK00684.
OMAYRQGIFP.
OrthoDBEOG6WX4R3.
ProtClustDBPRK00301.

Enzyme and pathway databases

BioCycVCHO:VC1735-MONOMER.

Family and domain databases

HAMAPMF_00688. Leu_Phe_trans.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR00667. aat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLFTR_VIBCH
AccessionPrimary (citable) accession number: Q9KRA7
Secondary accession number(s): O50259
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 70 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