UniProt: X0QHC2

Database: UniProt
Entry: X0QHC2_9LACO

LinkDB:  X0QHC2_9LACO 
Original site:  X0QHC2_9LACO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (15)   

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ID   X0QHC2_9LACO            Unreviewed;       327 AA.
AC   X0QHC2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=FD41_GL001089 {ECO:0000313|EMBL:KRM03762.1}, JCM14108_3081
GN   {ECO:0000313|EMBL:GAF37990.1};
OS   Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF37990.1, ECO:0000313|Proteomes:UP000019488};
RN   [1] {ECO:0000313|EMBL:GAF37990.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF37990.1};
RA   Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT   14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT   Shochu Residue.";
RL   Genome Announc. 2:e00257-14(2014).
RN   [2] {ECO:0000313|EMBL:KRM03762.1, ECO:0000313|Proteomes:UP000051966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM03762.1,
RC   ECO:0000313|Proteomes:UP000051966};
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., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC         diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC         protein]; 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:0000256|ARBA:ARBA00043803};
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005124}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005085}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAF37990.1}.
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DR   EMBL; BAKI01000060; GAF37990.1; -; Genomic_DNA.
DR   EMBL; AZFY01000125; KRM03762.1; -; Genomic_DNA.
DR   RefSeq; WP_035181336.1; NZ_BAKI01000060.1.
DR   AlphaFoldDB; X0QHC2; -.
DR   STRING; 1423743.FD41_GL001089; -.
DR   PATRIC; fig|1423743.5.peg.1123; -.
DR   eggNOG; COG0095; Bacteria.
DR   OrthoDB; 9788148at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000019488; Unassembled WGS sequence.
DR   Proteomes; UP000051966; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16443; LplA; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 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   NCBIfam; TIGR00545; lipoyltrans; 1.
DR   PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF82649; SufE/NifU; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:GAF37990.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          26..211
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   327 AA;  36558 MW;  9A67D5CA39F62AE6 CRC64;
     MIYIPVTSTD VYHNFALEYY LMSEKRFREP VFLLWSTTPT VMLGKYQDAT TELNLANVKR
     YGVHVARRYS GGGTIYTDQG GCQFTLIYPD EHTEIDFSVG LRLIKTALNQ IGIQAANDSR
     NDLVVAGRKV SGSAQYVTPG YKLHHGSLLF DSNLATMAAV LKVDPVKLKA KRIASVHQRT
     INLKEQQPNW SAQEFKDYLR QAVVSLQQAE TYQLTPADEA RILGISSQRF ANPDFIYGKR
     SRLAHTGKRY FQGGGLARIS YSLDNQRLTA VHLSGDFFSN LDTGRFEQAL VGTKYDRSAV
     LKIIDAQLAI TPIMGISANQ LTGLIFD
//

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