Q92QK2 (LFTR_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	R01318
ORF Names:	SMc01346

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium › Rhizobium meliloti

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Inferred 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 + protein = tRNA + L-leucyl-protein. HAMAP-Rule MF_00688 L-phenylalanyl-tRNA + protein = tRNA + L-phenylalanyl-protein. HAMAP-Rule MF_00688
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the L/F-transferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	leucyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688		PRO_0000207239

Sequences

	Sequence		Length	Mass (Da)
	Q92QK2 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: AE0FB1A54664C2A7	FASTA	204	22,784
	10 20 30 40 50 60 MKETRSKQPD ITPDMLLRAY SIGLFPMADS ADDPELFWVE PEIRGIIPLD RFHVSRSLAK 70 80 90 100 110 120 AIRRRPFDIR FDTAFAEVME GCAQPAPDRP TTWINDTIRS LYAALHNMGH AHSVEAWEGD 130 140 150 160 170 180 ALVGGLYGVS LGAAFFGESM FSRRTGASKI CLVHLVERLR SKGFQLLDTQ FTTEHLKSFG 190 200 AVDVPKAQYE VLLAKAIASP NLEF

References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC45897.1.
RefSeq	NP_385424.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92QK2.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMc01346.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC45897; CAC45897; SMc01346.
GeneID	1232966.
KEGG	sme:SMc01346.
PATRIC	23631951. VBISinMel96828_2732.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2360.
HOGENOM	HOG000102326.
KO	K00684.
OMA	MFYGESM.
ProtClustDB	PRK00301.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-1348-MONOMER.
Family and domain databases
HAMAP	MF_00688. Leu_Phe_trans.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR004616. Leu/Phe-tRNA_Trfase. [Graphical view]
Pfam	PF03588. Leu_Phe_trans. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMs	TIGR00667. aat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LFTR_RHIME

Accession

Primary (citable) accession number: Q92QK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program