A6QFD6 (LIPA_STAAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase
EC=2.8.1.8

Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA

Gene names

Name:	lipA
Ordered Locus Names:	NWMN_0796

Organism

Staphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]

Taxonomic identifier

426430 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives By similarity. HAMAP-Rule MF_00206
Catalytic activity	Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_00206
Cofactor	Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]. HAMAP-Rule MF_00206
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00206.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from electronic annotation. Source: HAMAP metal ion binding 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 – 305	305	Lipoyl synthase HAMAP-Rule MF_00206		PRO_1000071730
Sites
	Metal binding	41	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	46	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	52	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	68	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	72	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	75	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6QFD6 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 0911CD221177702B	FASTA	305	34,885
	10 20 30 40 50 60 MATKNEEILR KPDWLKIKLN TNENYTGLKK MMREKNLNTV CEEAKCPNIH ECWGARRTAT 70 80 90 100 110 120 FMILGAVCTR ACRFCAVKTG LPNELDLNEP ERVAESVELM NLKHVVITAV ARDDLRDAGS 130 140 150 160 170 180 NVYAETVRKV RERNPFTTIE ILPSDMGGDY DALETLMASR PDILNHNIET VRRLTPRVRA 190 200 210 220 230 240 RATYDRTLEF LRRSKELQPD IPTKSSIMVG LGETIEEIYE TMDDLRANDV DILTIGQYLQ 250 260 270 280 290 300 PSRKHLKVQK YYTPLEFGKL RKVAMDKGFK HCQAGPLVRS SYHADEQVNE AAKEKQRQGE AQLNS

References

[1]

"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands." Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K. J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Newman.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009351 Genomic DNA. Translation: BAF67068.1.
RefSeq	YP_001331830.1. NC_009641.1.
3D structure databases
ProteinModelPortal	A6QFD6.
ModBase	Search...
Protein-protein interaction databases
STRING	426430.NWMN_0796.
Proteomic databases
PRIDE	A6QFD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAF67068; BAF67068; NWMN_0796.
GeneID	5330470.
KEGG	sae:NWMN_0796.
PATRIC	19585073. VBIStaAur133992_0865.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OMA	EEYVTPE.
ProtClustDB	PRK05481.
Enzyme and pathway databases
BioCyc	SAUR426430:GIXC-797-MONOMER.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR003698. Lipoyl_synth. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005963. Lipoyl_synth. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LIPA_STAAE

Accession

Primary (citable) accession number: A6QFD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program