Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O07608

- LPLJ_BACSU

UniProt

O07608 - LPLJ_BACSU

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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.
    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

    MLFIDNQNIN DPRINLAIEE YCVKHLDPEQ QYLLFYVNQP SIIIGKNQNT    50
    IEEINTKYVE ENGIIVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFHNFK 100
    KFTEPVIQAL HQLGVEAELS GRNDIVVDGR KISGNAQFAT KGRIFSHGTL 150
    MFDSAIDHVV SALKVKKDKI ESKGIKSIRS RVANISEFLD DKMTTEEFRS 200
    HLLRHIFNTN DVGNVPEYKL TEKDWETIHQ ISKERYQNWD WNYGRSPKFN 250
    LNHSKRYPVG SIDLHLEVKK GKIEDCKIFG DFFGVGDVSE IENLLVGKQY 300
    ERSVIADVLE GVNLKHYFGN ITKEDFLDLI Y 331
    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.
    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

    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 1, 2014
    This is version 85 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