LPLJ_BACSU
ID LPLJ_BACSU Reviewed; 331 AA.
AC O07608; Q796U1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lipoate-protein ligase LplJ;
DE EC=6.3.1.20 {ECO:0000269|PubMed:21338420};
DE AltName: Full=Lipoate--protein ligase;
GN Name=lplJ; Synonyms=yhfJ; OrderedLocusNames=BSU10250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP GENE NAME, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=21338420; DOI=10.1111/j.1365-2958.2011.07597.x;
RA Martin N., Christensen Q.H., Mansilla M.C., Cronan J.E., de Mendoza D.;
RT "A novel two-gene requirement for the octanoyltransfer reaction of Bacillus
RT subtilis lipoic acid biosynthesis.";
RL Mol. Microbiol. 80:335-349(2011).
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes. Is also able to
CC use octanoate as substrate. {ECO:0000269|PubMed:21338420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC H(+); Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:456215; EC=6.3.1.20;
CC Evidence={ECO:0000269|PubMed:21338420};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC {ECO:0000269|PubMed:21338420}.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC {ECO:0000269|PubMed:21338420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally in minimal
CC medium in the absence of supplements and have a wild-type pattern of
CC lipoylated proteins. However, a double mutant strain lacking both lplJ
CC and lipM is unable to grow in minimal medium either in the presence or
CC in the absence of lipoic acid, indicating that LplJ is the sole
CC B.subtilis lipoic acid salvage enzyme. {ECO:0000269|PubMed:21338420}.
CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC lipoic acid is attached via an amide linkage to the epsilon-amino group
CC of a specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR EMBL; Y14083; CAA74531.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12865.1; -; Genomic_DNA.
DR PIR; G69830; G69830.
DR RefSeq; NP_388906.1; NC_000964.3.
DR RefSeq; WP_003244914.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07608; -.
DR SMR; O07608; -.
DR IntAct; O07608; 1.
DR MINT; O07608; -.
DR STRING; 224308.BSU10250; -.
DR PaxDb; O07608; -.
DR PRIDE; O07608; -.
DR EnsemblBacteria; CAB12865; CAB12865; BSU_10250.
DR GeneID; 939310; -.
DR KEGG; bsu:BSU10250; -.
DR PATRIC; fig|224308.179.peg.1101; -.
DR eggNOG; COG0095; Bacteria.
DR InParanoid; O07608; -.
DR OMA; CYLIPYD; -.
DR PhylomeDB; O07608; -.
DR BioCyc; BSUB:BSU10250-MON; -.
DR BioCyc; MetaCyc:BSU10250-MON; -.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0017118; F:lipoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; PTHR12561; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..331
FT /note="Lipoate-protein ligase LplJ"
FT /id="PRO_0000386531"
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 74..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 38020 MW; 062B2DB3A16E7CBC CRC64;
MLFIDNQNIN DPRINLAIEE YCVKHLDPEQ QYLLFYVNQP SIIIGKNQNT IEEINTKYVE
ENGIIVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFHNFK KFTEPVIQAL HQLGVEAELS
GRNDIVVDGR KISGNAQFAT KGRIFSHGTL MFDSAIDHVV SALKVKKDKI ESKGIKSIRS
RVANISEFLD DKMTTEEFRS HLLRHIFNTN DVGNVPEYKL TEKDWETIHQ ISKERYQNWD
WNYGRSPKFN LNHSKRYPVG SIDLHLEVKK GKIEDCKIFG DFFGVGDVSE IENLLVGKQY
ERSVIADVLE GVNLKHYFGN ITKEDFLDLI Y
