Reviewed, UniProtKB/Swiss-Prot Q1R257 (LPLA_ECOUT)

Names and origin

Protein names

Recommended name:
    Lipoate-protein ligase A
    EC=2.7.7.63
Alternative name(s):
    Lipoate--protein ligase

Gene names

Name:	lplA
Ordered Locus Names:	UTI89_C5157

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes By similarity.
Catalytic activity	ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP MF_01602
Pathway	Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 1/2. HAMAP MF_01602 Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 2/2.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes By similarity.
Sequence similarities	Belongs to the lplA family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	peptidyl-lysine lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate-protein ligase activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Lipoate-protein ligase A HAMAP MF_01602		PRO_1000069381
Regions
	Nucleotide binding	76 – 79	4	ATP By similarity
Sites
	Binding site	71	1	ATP By similarity
	Binding site	134	1	ATP By similarity
	Binding site	134	1	Lipoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R257-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 533244306A80DE54	FASTA	338	37,897
	10 20 30 40 50 60 MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR 70 80 90 100 110 120 MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVSAEASG 130 140 150 160 170 180 RNDLVVKTAE GDRKVSGSAY RETKDRGFHH GTLLLNSDLS RLANYLNPDK KKLAAKGITS 190 200 210 220 230 240 VRSRVTNLTE LLPGITHEQV CEAITEAFFA HYGERVEAEI ISPDKTPDLP NFAETFARQS 250 260 270 280 290 300 SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG 310 320 330 CLYRADMLQQ ECEALLVDFP EQEKELRELS AWIAGAVR

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000243 Genomic DNA. Translation: ABE10557.1.
RefSeq	YP_544088.1.
3D structure databases
SMR	Q1R257. Positions 2-338.
ModBase	Search...
Genome annotation databases
GeneID	3993548.
GenomeReviews	Gene locus UTI89_C5157 in contig CP000243_GR.
KEGG	eci:UTI89_C5157.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1R257.
OMA	Q1R257. YEQSHLE.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C5157-MON.
Family and domain databases
HAMAP	MF_01602. [Tree]
InterPro	IPR004143. BPL_LipA_LipB. IPR005107. CO_DH_flav_C. IPR019491. Lipoate_protein_ligase_C. IPR004562. LipoylTrfase_LipoateP_Ligase. [Graphical view]
Gene3D	G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
Pfam	PF03099. BPL_LipA_LipB. 1 hit. PF10437. Lip_prot_lig_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00545. lipoyltrans. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LPLA_ECOUT

Accession

Primary (citable) accession number: Q1R257

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)