O32129 (LIPA_BACSU) 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
Synonyms:	yutB
Ordered Locus Names:	BSU32330

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.2
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]. Ref.2
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00206.
Disruption phenotype	Disruption of this gene interrupts lipoate-dependent reactions, which strongly inhibits growth in minimal medium, impairing the generation of branched-chain fatty acids and leading to accumulation of copious amounts of straight-chain saturated fatty acids in B.subtilis membranes. Ref.2
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 Reference proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from genetic interaction Ref.2. Source: UniProtKB
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 genetic interaction Ref.2. Source: UniProtKB 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 – 298	298	Lipoyl synthase HAMAP-Rule MF_00206		PRO_0000102288
Sites
	Metal binding	40	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	45	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	67	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	71	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	74	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O32129 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: E6BEEB81C6ECC6FF	FASTA	298	33,921
	10 20 30 40 50 60 MAKKDEHLRK PEWLKIKLNT NENYTGLKKL MRENNLHTVC EEAKCPNIHE CWAVRRTATF 70 80 90 100 110 120 MILGSVCTRA CRFCAVKTGL PTELDLQEPE RVADSVALMN LKHAVITAVA RDDQKDGGAG 130 140 150 160 170 180 IFAETVRAIR RKSPFTTIEV LPSDMGGNYD NLKTLMDTRP DILNHNIETV RRLTPRVRAR 190 200 210 220 230 240 ATYDRSLEFL RRAKEMQPDI PTKSSIMIGL GETKEEIIEV MDDLLANNVD IMAIGQYLQP 250 260 270 280 290 TKKHLKVQKY YHPDEFAELK EIAMQKGFSH CEAGPLVRSS YHADEQVNEA SKKRQAQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis." Martin N., Lombardia E., Altabe S.G., de Mendoza D., Mansilla M.C. J. Bacteriol. 191:7447-7455(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A LIPOYL SYNTHASE, PATHWAY, DISRUPTION PHENOTYPE. Strain: 168 / JH642.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL009126 Genomic DNA. Translation: CAB15223.2.
PIR	D70023.
RefSeq	NP_391113.2. NC_000964.3.
3D structure databases
ProteinModelPortal	O32129.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU32330.
Proteomic databases
PaxDb	O32129.
Protocols and materials databases
DNASU	938861.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB15223; CAB15223; BSU32330.
GeneID	938861.
KEGG	bsu:BSU32330.
PATRIC	18978438. VBIBacSub10457_3382.
Organism-specific databases
GenoList	BSU32330. [Micado]
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OMA	EEYVTPE.
ProtClustDB	PRK05481.
Enzyme and pathway databases
BioCyc	BSUB:BSU32330-MONOMER. MetaCyc:BSU32330-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_BACSU

Accession

Primary (citable) accession number: O32129

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program