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O07610

- LCFB_BACSU

UniProt

O07610 - LCFB_BACSU

Protein

Long-chain-fatty-acid--CoA ligase

Gene

lcfB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Involved in the degradation of long-chain fatty acids.

    Catalytic activityi

    ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU10270-MONOMER.
    RETL1328306-WGS:GSTH-5136-MONOMER.
    RETL1328306-WGS:GSTH-936-MONOMER.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
    Alternative name(s):
    Long-chain acyl-CoA synthetase
    Gene namesi
    Name:lcfB
    Synonyms:yhfL
    Ordered Locus Names:BSU10270
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU10270. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513Long-chain-fatty-acid--CoA ligasePRO_0000360675Add
    BLAST

    Proteomic databases

    PaxDbiO07610.

    Expressioni

    Inductioni

    Repressed by FadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize FadR as to its binding to FadR boxes on target DNA and thus derepress transcription.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU10270.

    Structurei

    3D structure databases

    ProteinModelPortaliO07610.
    SMRiO07610. Positions 1-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000229983.
    KOiK01897.
    OrthoDBiEOG6MH5BV.
    PhylomeDBiO07610.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020459. AMP-binding.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PRINTSiPR00154. AMPBINDING.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O07610-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLVSKLEET ASEKPDSIAC RFKDHMMTYQ ELNEYIQRFA DGLQEAGMEK    50
    GDHLALLLGN SPDFIIAFFG ALKAGIVVVP INPLYTPTEI GYMLTNGDVK 100
    AIVGVSQLLP LYESMHESLP KVELVILCQT GEAEPEAADP EVRMKMTTFA 150
    KILRPTSAAK QNQEPVPDDT AVILYTSGTT GKPKGAMLTH QNLYSNANDV 200
    AGYLGMDERD NVVCALPMFH VFCLTVCMNA PLMSGATVLI EPQFSPASVF 250
    KLVKQQQATI FAGVPTMYNY LFQHENGKKD DFSSIRLCIS GGASMPVALL 300
    TAFEEKFGVT ILEGYGLSEA SPVTCFNPFD RGRKPGSIGT SILHVENKVV 350
    DPLGRELPAH QVGELIVKGP NVMKGYYKMP METEHALKDG WLYTGDLARR 400
    DEDGYFYIVD RKKDMIIVGG YNVYPREVEE VLYSHPDVKE AVVIGVPDPQ 450
    SGEAVKGYVV PKRSGVTEED IMQHCEKHLA KYKRPAAITF LDDIPKNATG 500
    KMLRRALRDI LPQ 513
    Length:513
    Mass (Da):56,625
    Last modified:June 16, 2009 - v2
    Checksum:iD8BEBE46A9CB5183
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2191F → C in CAA74533. (PubMed:9579061)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14083 Genomic DNA. Translation: CAA74533.1.
    AL009126 Genomic DNA. Translation: CAB12867.2.
    PIRiA69831.
    RefSeqiNP_388908.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12867; CAB12867; BSU10270.
    GeneIDi939308.
    KEGGibsu:BSU10270.
    PATRICi18973752. VBIBacSub10457_1070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14083 Genomic DNA. Translation: CAA74533.1 .
    AL009126 Genomic DNA. Translation: CAB12867.2 .
    PIRi A69831.
    RefSeqi NP_388908.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali O07610.
    SMRi O07610. Positions 1-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU10270.

    Proteomic databases

    PaxDbi O07610.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12867 ; CAB12867 ; BSU10270 .
    GeneIDi 939308.
    KEGGi bsu:BSU10270.
    PATRICi 18973752. VBIBacSub10457_1070.

    Organism-specific databases

    GenoListi BSU10270. [Micado ]

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000229983.
    KOi K01897.
    OrthoDBi EOG6MH5BV.
    PhylomeDBi O07610.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci BSUB:BSU10270-MONOMER.
    RETL1328306-WGS:GSTH-5136-MONOMER.
    RETL1328306-WGS:GSTH-936-MONOMER.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020459. AMP-binding.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00154. AMPBINDING.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 219.
    4. "Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation."
      Matsuoka H., Hirooka K., Fujita Y.
      J. Biol. Chem. 282:5180-5194(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE NAME, INDUCTION.
      Strain: 168.

    Entry informationi

    Entry nameiLCFB_BACSU
    AccessioniPrimary (citable) accession number: O07610
    Secondary accession number(s): Q796T9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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