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Protein

Lipoate-protein ligase LplJ

Gene

lplJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + lipoate = diphosphate + lipoyl-AMP.1 Publication
Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP.1 Publication

Pathway: protein lipoylation via exogenous pathway

This protein is involved in step 1 and 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lipoate-protein ligase LplJ (lplJ)
  2. Lipoate-protein ligase LplJ (lplJ)
This subpathway is part of the pathway protein lipoylation via exogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate, the pathway protein lipoylation via exogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691ATPBy similarity
Binding sitei131 – 1311ATPBy similarity
Binding sitei131 – 1311LipoateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 774ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • lipoate-protein ligase activity Source: UniProtKB
  • lipoyltransferase activity Source: UniProtKB

GO - Biological processi

  • protein lipoylation Source: UniProtKB

Keywords - Molecular functioni

Ligase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU10250-MONOMER.
MetaCyc:BSU10250-MONOMER.
UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoate-protein ligase LplJ (EC:2.7.7.63)
Alternative name(s):
Lipoate--protein ligase
Gene namesi
Name:lplJ
Synonyms:yhfJ
Ordered Locus Names:BSU10250
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU10250. [Micado]

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Lipoate-protein ligase LplJPRO_0000386531Add
BLAST

Proteomic databases

PaxDbiO07608.

Interactioni

Protein-protein interaction databases

IntActiO07608. 1 interaction.
MINTiMINT-8366807.
STRINGi224308.Bsubs1_010100005691.

Structurei

3D structure databases

ProteinModelPortaliO07608.
SMRiO07608. Positions 1-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 214188BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the LplA family.Curated
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0095.
HOGENOMiHOG000260593.
InParanoidiO07608.
KOiK03800.
OMAiVRSEVTN.
OrthoDBiEOG6038ZS.
PhylomeDBiO07608.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O07608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFIDNQNIN DPRINLAIEE YCVKHLDPEQ QYLLFYVNQP SIIIGKNQNT
60 70 80 90 100
IEEINTKYVE ENGIIVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFHNFK
110 120 130 140 150
KFTEPVIQAL HQLGVEAELS GRNDIVVDGR KISGNAQFAT KGRIFSHGTL
160 170 180 190 200
MFDSAIDHVV SALKVKKDKI ESKGIKSIRS RVANISEFLD DKMTTEEFRS
210 220 230 240 250
HLLRHIFNTN DVGNVPEYKL TEKDWETIHQ ISKERYQNWD WNYGRSPKFN
260 270 280 290 300
LNHSKRYPVG SIDLHLEVKK GKIEDCKIFG DFFGVGDVSE IENLLVGKQY
310 320 330
ERSVIADVLE GVNLKHYFGN ITKEDFLDLI Y
Length:331
Mass (Da):38,020
Last modified:July 1, 1997 - v1
Checksum:i062B2DB3A16E7CBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14083 Genomic DNA. Translation: CAA74531.1.
AL009126 Genomic DNA. Translation: CAB12865.1.
PIRiG69830.
RefSeqiNP_388906.1. NC_000964.3.
WP_003244914.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12865; CAB12865; BSU10250.
GeneIDi939310.
KEGGibsu:BSU10250.
PATRICi18973748. VBIBacSub10457_1068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14083 Genomic DNA. Translation: CAA74531.1.
AL009126 Genomic DNA. Translation: CAB12865.1.
PIRiG69830.
RefSeqiNP_388906.1. NC_000964.3.
WP_003244914.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO07608.
SMRiO07608. Positions 1-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO07608. 1 interaction.
MINTiMINT-8366807.
STRINGi224308.Bsubs1_010100005691.

Proteomic databases

PaxDbiO07608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12865; CAB12865; BSU10250.
GeneIDi939310.
KEGGibsu:BSU10250.
PATRICi18973748. VBIBacSub10457_1068.

Organism-specific databases

GenoListiBSU10250. [Micado]

Phylogenomic databases

eggNOGiCOG0095.
HOGENOMiHOG000260593.
InParanoidiO07608.
KOiK03800.
OMAiVRSEVTN.
OrthoDBiEOG6038ZS.
PhylomeDBiO07608.

Enzyme and pathway databases

UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.
BioCyciBSUB:BSU10250-MONOMER.
MetaCyc:BSU10250-MONOMER.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiLPLJ_BACSU
AccessioniPrimary (citable) accession number: O07608
Secondary accession number(s): Q796U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 13, 2009
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.