ID G7SHQ9_STRSU Unreviewed; 329 AA.
AC G7SHQ9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SSUD12_1801 {ECO:0000313|EMBL:AER20069.1};
OS Streptococcus suis D12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER20069.1, ECO:0000313|Proteomes:UP000008845};
RN [1] {ECO:0000313|EMBL:AER20069.1, ECO:0000313|Proteomes:UP000008845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D12 {ECO:0000313|EMBL:AER20069.1};
RX PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J.,
RA Jin M.;
RT "Comparative Genomic Analysis of Streptococcus suis reveals significant
RT genomic diversity among different serotypes.";
RL BMC Genomics 12:523-523(2011).
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; CP002644; AER20069.1; -; Genomic_DNA.
DR RefSeq; WP_014638588.1; NC_017621.1.
DR AlphaFoldDB; G7SHQ9; -.
DR KEGG; ssk:SSUD12_1801; -.
DR PATRIC; fig|1004952.3.peg.1755; -.
DR HOGENOM; CLU_022986_0_2_9; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000008845; 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:AER20069.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 26..213
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 329 AA; 37229 MW; DF8646A97CD037A0 CRC64;
MKYIVNNSND PAYNIALEAY AFKELTDIDE IFILWINEPA IIIGKHQNAI EEINKEFTDE
KGIHVVRRLS GGGAVYHDLN NLNYTIISNK ADEGAFDFKT FSKPVIDTLA TLGVEANFTG
RNDLEIDGKK ICGNAQAYAK GRMMHHGCLL FDVDMSVLAS ALKVSKDKIE SKGVKSVRAR
VTNINNELPE KMTVLEFKDA ILNQMKQEYP DIDEYVLVED DLARIQEIRD TQFATWDWTY
GQTPEYTVER SVRYPAGKIT TYIKAEKSVI ESIKIYGDFF GIGDVSDIED LLVGTRYEYA
DVLAKLQEID TTHYFSRMTT EEVAKAIVA
//
