ID A0A011RM11_9LACT Unreviewed; 339 AA.
AC A0A011RM11;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=ADIAL_1744 {ECO:0000313|EMBL:EXJ22893.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22893.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ22893.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:EXJ22893.1}.
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DR EMBL; JANL01000037; EXJ22893.1; -; Genomic_DNA.
DR RefSeq; WP_034302533.1; NZ_JANL01000037.1.
DR AlphaFoldDB; A0A011RM11; -.
DR STRING; 1229520.ADIAL_1744; -.
DR PATRIC; fig|1229520.3.peg.1708; -.
DR eggNOG; COG0095; Bacteria.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000020164; 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:EXJ22893.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 31..222
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 339 AA; 38825 MW; 90FF07AD05532CC8 CRC64;
MYYVKNERNG KEVHDPSLNL AIEYYLLNEV ELDEPILLFY INDHSIIVGR NQNTYEEVNT
NYVDDQDIKV VRRFSGGGAV YHDMGVLNFC FLTKDDGESF RDFKKFTLPV IDALHQMGVD
GAELKGRNDL VIDGKKFSGN AMYAKNNRLT AHGTLMFDSE IEAVVKALKP KKHKLESKGI
KSIRSRVTNI KPYLDDSYQY MNAKDFRDKL LLYIFDTDTK ETIKEYKLTE ADWEKIDAFA
DAYTGNWEWN YGKSPAFDTE RSERLSVGTV EVKMNVRQGT IEAIRVYGDF FGMGEIADVE
QALTGVAYTR EAITSALNGL DLNKYFGQVE VEELVNLLY
//
