ID F0RJM5_DEIPM Unreviewed; 333 AA.
AC F0RJM5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN OrderedLocusNames=Deipr_1453 {ECO:0000313|EMBL:ADY26595.1};
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY26595.1, ECO:0000313|Proteomes:UP000007718};
RN [1] {ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT 20540.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY26595.1, ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RX PubMed=22768367; DOI=10.4056/sigs.2756060;
RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the orange-red pigmented, radioresistant
RT Deinococcus proteolyticus type strain (MRP(T)).";
RL Stand. Genomic Sci. 6:240-250(2012).
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; CP002536; ADY26595.1; -; Genomic_DNA.
DR RefSeq; WP_013615203.1; NC_015161.1.
DR AlphaFoldDB; F0RJM5; -.
DR STRING; 693977.Deipr_1453; -.
DR KEGG; dpt:Deipr_1453; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_0_2_0; -.
DR OrthoDB; 9787898at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000007718; 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:ADY26595.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007718};
KW Transferase {ECO:0000313|EMBL:ADY26595.1}.
FT DOMAIN 27..217
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 333 AA; 37932 MW; 53082EDEB1173CD8 CRC64;
MHYIRNAENH DVTVNLALET YLVRNRLVDG PLLLFYINDP CVIVGRNQNT IEEINREYVE
ENGVQVVRRL SGGGAVYQDG GNLCYCFIKD DDGSFRDFAS FTEPVVSALQ RMGAAEAALR
GRNDLVIGDQ KISGNAMYVA GGRMTAHGTL LYDVNLDHVA AALKPPKEKI ESKGIKSVRA
RVTNIRPHLA PEFQGMTTGE FRDEILRQLA QQSGEEPTEY QLTGHDWQEI ERIRQEYFLN
WDWNFGRSPD FSLERRHKFA SGLIDVRMNV EKKHIQDIRI YGDFFALDDV ADLERALTGV
PYRPEDIAAA LEPFDLSRYF GAVEREEFVR LII
//
