ID A0A133Q4Y9_STALU Unreviewed; 340 AA.
AC A0A133Q4Y9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=EQ812_06670 {ECO:0000313|EMBL:TBW72651.1}, HMPREF3225_01428
GN {ECO:0000313|EMBL:KXA37934.1};
OS Staphylococcus lugdunensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA37934.1, ECO:0000313|Proteomes:UP000070063};
RN [1] {ECO:0000313|EMBL:KXA37934.1, ECO:0000313|Proteomes:UP000070063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7738 {ECO:0000313|EMBL:KXA37934.1,
RC ECO:0000313|Proteomes:UP000070063};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TBW72651.1, ECO:0000313|Proteomes:UP000293637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E7 {ECO:0000313|EMBL:TBW72651.1,
RC ECO:0000313|Proteomes:UP000293637};
RA Williams M.R.;
RT "Quorum sensing between bacterial species on the skin protects against
RT epidermal injury in atopic dermatitis.";
RL Sci. Transl. Med. 0:0-0(2019).
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:KXA37934.1}.
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DR EMBL; LRQI01000063; KXA37934.1; -; Genomic_DNA.
DR EMBL; SCHB01000003; TBW72651.1; -; Genomic_DNA.
DR RefSeq; WP_002460713.1; NZ_SCHB01000003.1.
DR AlphaFoldDB; A0A133Q4Y9; -.
DR STRING; 28035.B6N84_01065; -.
DR GeneID; 58090982; -.
DR PATRIC; fig|28035.7.peg.1448; -.
DR eggNOG; COG0095; Bacteria.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000070063; Unassembled WGS sequence.
DR Proteomes; UP000293637; 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:KXA37934.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:KXA37934.1}.
FT DOMAIN 31..222
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 340 AA; 38401 MW; F3B030857AD16BF0 CRC64;
MYLIEPIRNG KYIADGAVNL AMQVYVNQHI FLDEDILLPY YCDPKIEIGR FQNTAIEINQ
EYVDTHGIQV VRRDTGGGAV YVDKGAVNVC CILEQDTSIY GDFQRFYRPA IKALHHLGAT
DVIQSGRNDL TLHGKKISGA AMTVINNRIY GGYSLLLDVD YDAMVQSLNP NRKKIESKGI
KSVRARVGNI RDSLAPEYQD ITIQAFKDLI IKQIMGIDDI SDAKRYTLTD EDWAGIDQLV
ADKYANWEWN YGHSPRYEYN RNARFACGTI DISLSVTQNR ISGCSIFGDF FGQGDIHDVE
THLVGTRMVK QDLIARLEDI DLNYYFGSLS AEELTQLILS
//
