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O07608 (LPLJ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Lipoate-protein ligase LplJ

EC=2.7.7.63
Alternative name(s):
Lipoate--protein ligase
Gene names
Name:lplJ
Synonyms:yhfJ
Ordered Locus Names:BSU10250
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Is also able to use octanoate as substrate. Ref.3

Catalytic activity

ATP + lipoate = diphosphate + lipoyl-AMP. Ref.3

Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. Ref.3

Pathway

Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. Ref.3

Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.

Subcellular location

Cytoplasm By similarity.

Disruption phenotype

Cells lacking this gene grow normally in minimal medium in the absence of supplements and have a wild-type pattern of lipoylated proteins. However, a double mutant strain lacking both lplJ and lipM is unable to grow in minimal medium either in the presence or in the absence of lipoic acid, indicating that LplJ is the sole B.subtilis lipoic acid salvage enzyme. Ref.3

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 componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate-protein ligase activity

Inferred from direct assay Ref.3. Source: UniProtKB

lipoyltransferase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Lipoate-protein ligase LplJ
PRO_0000386531

Regions

Nucleotide binding74 – 774ATP By similarity

Sites

Binding site691ATP By similarity
Binding site1311ATP By similarity
Binding site1311Lipoate By similarity

Sequences

Sequence LengthMass (Da)Tools
O07608 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 062B2DB3A16E7CBC

FASTA33138,020
        10         20         30         40         50         60 
MLFIDNQNIN DPRINLAIEE YCVKHLDPEQ QYLLFYVNQP SIIIGKNQNT IEEINTKYVE 

        70         80         90        100        110        120 
ENGIIVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFHNFK KFTEPVIQAL HQLGVEAELS 

       130        140        150        160        170        180 
GRNDIVVDGR KISGNAQFAT KGRIFSHGTL MFDSAIDHVV SALKVKKDKI ESKGIKSIRS 

       190        200        210        220        230        240 
RVANISEFLD DKMTTEEFRS HLLRHIFNTN DVGNVPEYKL TEKDWETIHQ ISKERYQNWD 

       250        260        270        280        290        300 
WNYGRSPKFN LNHSKRYPVG SIDLHLEVKK GKIEDCKIFG DFFGVGDVSE IENLLVGKQY 

       310        320        330 
ERSVIADVLE GVNLKHYFGN ITKEDFLDLI Y 

« Hide

References

« Hide 'large scale' references
[1]"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"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. expand/collapse author list , 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.
[3]"A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis."
Martin N., Christensen Q.H., Mansilla M.C., Cronan J.E., de Mendoza D.
Mol. Microbiol. 80:335-349(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.
Strain: 168 / JH642.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14083 Genomic DNA. Translation: CAA74531.1.
AL009126 Genomic DNA. Translation: CAB12865.1.
PIRG69830.
RefSeqNP_388906.1. NC_000964.3.

3D structure databases

ProteinModelPortalO07608.
SMRO07608. Positions 1-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO07608. 1 interaction.
MINTMINT-8366807.
STRING224308.BSU10250.

Proteomic databases

PaxDbO07608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12865; CAB12865; BSU10250.
GeneID939310.
KEGGbsu:BSU10250.
PATRIC18973748. VBIBacSub10457_1068.

Organism-specific databases

GenoListBSU10250. [Micado]

Phylogenomic databases

eggNOGCOG0095.
HOGENOMHOG000260593.
KOK03800.
OMARYQNWDW.
OrthoDBEOG6038ZS.
ProtClustDBCLSK2391267.

Enzyme and pathway databases

BioCycBSUB:BSU10250-MONOMER.
MetaCyc:BSU10250-MONOMER.
UniPathwayUPA00537; UER00594.
UPA00537; UER00595.

Family and domain databases

InterProIPR004143. BPL_LipA_LipB.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
PfamPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00545. lipoyltrans. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPLJ_BACSU
AccessionPrimary (citable) accession number: O07608
Secondary accession number(s): Q796U1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 13, 2009
Last sequence update: July 1, 1997
Last modified: November 13, 2013
This is version 82 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList