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O07608

- LPLJ_BACSU

UniProt

O07608 - LPLJ_BACSU

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Protein

Lipoate-protein ligase LplJ

Gene

lplJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 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

Pathwayi

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

  1. ATP binding Source: UniProtKB-KW
  2. lipoate-protein ligase activity Source: UniProtKB
  3. lipoyltransferase activity Source: UniProtKB

GO - Biological processi

  1. protein lipoylation Source: UniProtKB
Complete GO annotation...

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: Chromosome

Organism-specific databases

GenoListiBSU10250. [Micado]

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

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.BSU10250.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the LplA family.Curated

Phylogenomic databases

eggNOGiCOG0095.
HOGENOMiHOG000260593.
InParanoidiO07608.
KOiK03800.
OMAiRAQIFTD.
OrthoDBiEOG6038ZS.
PhylomeDBiO07608.

Family and domain databases

InterProiIPR004143. BPL_LipA_LipB.
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.

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:
EMBL
GenBank
DDBJ
Links Updated
Y14083 Genomic DNA. Translation: CAA74531.1.
AL009126 Genomic DNA. Translation: CAB12865.1.
PIRiG69830.
RefSeqiNP_388906.1. NC_000964.3.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y14083 Genomic DNA. Translation: CAA74531.1 .
AL009126 Genomic DNA. Translation: CAB12865.1 .
PIRi G69830.
RefSeqi NP_388906.1. NC_000964.3.

3D structure databases

ProteinModelPortali O07608.
SMRi O07608. Positions 1-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O07608. 1 interaction.
MINTi MINT-8366807.
STRINGi 224308.BSU10250.

Proteomic databases

PaxDbi O07608.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12865 ; CAB12865 ; BSU10250 .
GeneIDi 939310.
KEGGi bsu:BSU10250.
PATRICi 18973748. VBIBacSub10457_1068.

Organism-specific databases

GenoListi BSU10250. [Micado ]

Phylogenomic databases

eggNOGi COG0095.
HOGENOMi HOG000260593.
InParanoidi O07608.
KOi K03800.
OMAi RAQIFTD.
OrthoDBi EOG6038ZS.
PhylomeDBi O07608.

Enzyme and pathway databases

UniPathwayi UPA00537 ; UER00594 .
UPA00537 ; UER00595 .
BioCyci BSUB:BSU10250-MONOMER.
MetaCyc:BSU10250-MONOMER.

Family and domain databases

InterProi IPR004143. BPL_LipA_LipB.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view ]
Pfami PF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00545. lipoyltrans. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: October 29, 2014
This is version 86 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