ID W6A862_9MOLU Unreviewed; 331 AA.
AC W6A862;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=lplA {ECO:0000313|EMBL:AHI53333.1};
GN ORFNames=SCULI_v1c09930 {ECO:0000313|EMBL:AHI53333.1};
OS Spiroplasma culicicola AES-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276246 {ECO:0000313|EMBL:AHI53333.1, ECO:0000313|Proteomes:UP000019267};
RN [1] {ECO:0000313|EMBL:AHI53333.1, ECO:0000313|Proteomes:UP000019267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AES-1 {ECO:0000313|EMBL:AHI53333.1};
RX PubMed=24534435;
RA Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT "Molecular evolution of the substrate utilization strategies and putative
RT virulence factors in mosquito-associated Spiroplasma species.";
RL Genome Biol. Evol. 6:500-509(2014).
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}.
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DR EMBL; CP006681; AHI53333.1; -; Genomic_DNA.
DR RefSeq; WP_025363555.1; NZ_CP006681.1.
DR AlphaFoldDB; W6A862; -.
DR STRING; 1276246.SCULI_v1c09930; -.
DR KEGG; scq:SCULI_v1c09930; -.
DR PATRIC; fig|1276246.3.peg.989; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_0_2_14; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000019267; Chromosome.
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:AHI53333.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019267}.
FT DOMAIN 26..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 331 AA; 37964 MW; E28B3972F68409BF CRC64;
MYIYRTDCVD PKYNLATEEY LTRSLKFDEP ILFLWQNDNT IVVGRNQNAA WEINLQQAEA
DNVNVIRRNT GGGTIFHDLG NMNFSIIYTD KENTAVSMFS TMLEPVIETL NRMGVAAQFS
GRNDIVLNEK KISGNAMWKE GQRFLQHGTI LFNANLDKLT KYLTVDRAKI LSKNIKSIAA
RVTNINSEVE HKIEIKDFMD ELIKTYETKN EVKELVLEQQ DIKAIEDLCE SKYRDPNWTY
AKNATFTYQN KVRIEGKGGV DVLAQIVDGK ILDVKFYGDF LGFAGTEKLE QSLINVEYKT
KDIKIVLEQN NIQAIFGDNF VIQDILDLLI Q
//
