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Database: UniProt
Entry: A0A0R2D5L4_9LACO
LinkDB: A0A0R2D5L4_9LACO
Original site: A0A0R2D5L4_9LACO 
ID   A0A0R2D5L4_9LACO        Unreviewed;       337 AA.
AC   A0A0R2D5L4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=FC24_GL000469 {ECO:0000313|EMBL:KRM99272.1};
OS   Lactobacillus rennini DSM 20253.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM99272.1, ECO:0000313|Proteomes:UP000051638};
RN   [1] {ECO:0000313|EMBL:KRM99272.1, ECO:0000313|Proteomes:UP000051638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM99272.1,
RC   ECO:0000313|Proteomes:UP000051638};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier
CC       protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine
CC       + AMP + diphosphate. {ECO:0000256|SAAS:SAAS00603726}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|SAAS:SAAS00701662}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRM99272.1}.
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DR   EMBL; AYYI01000017; KRM99272.1; -; Genomic_DNA.
DR   RefSeq; WP_057873327.1; NZ_AYYI01000017.1.
DR   EnsemblBacteria; KRM99272; KRM99272; FC24_GL000469.
DR   PATRIC; fig|1423796.3.peg.483; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000051638; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
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   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00428641};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051638};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KRM99272.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051638}.
FT   DOMAIN       26    209       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   337 AA;  38419 MW;  7473A217B257EFD3 CRC64;
     MYYIAMKSRD IRQNLATEQY LMNEKEFDAP LLLFYIEGPS IIVGRNQNTL EEVNQKYVRE
     HNITVTRRLS GGGAVYHDLG NLCFSFVVDA KDEKFGNFKA FTQPIVDALH ELGATSAEVS
     GRNDMLIDGK KFSGSAMYTK RGKTFSHGTL MLDVDLNVVT HALNVPEDKI KSKGIKSVRS
     RVTNLRPYLS PEYADITTEQ FRDLLIQRLL GVDSLAAAKP HAYQLTPEDE KEITKIRKQY
     YDNWDWVYGH SPEFTVKKRQ HFDMGTIDAR FLIHDGKIAN VVFYGDFFGA GDASELAEKL
     KGVVYDRQHV EQVLQQVDTQ KYFNGIPETD LLNLLVE
//
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