ID   X0QLF7_9GAMM            Unreviewed;       339 AA.
AC   X0QLF7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=JCM18902_267 {ECO:0000313|EMBL:GAF57558.1};
OS   Psychrobacter sp. JCM 18902.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1298607 {ECO:0000313|EMBL:GAF57558.1, ECO:0000313|Proteomes:UP000019502};
RN   [1] {ECO:0000313|EMBL:GAF57558.1, ECO:0000313|Proteomes:UP000019502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18902 {ECO:0000313|EMBL:GAF57558.1,
RC   ECO:0000313|Proteomes:UP000019502};
RA   Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA   Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA   Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K., Yuki M.,
RA   Iida T., Moriya S., Inoue T., Hongo Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM
RT   18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT   Organisms.";
RL   Genome Announc. 2:e00280-14(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}.
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:GAF57558.1}.
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DR   EMBL; BAWI01000001; GAF57558.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0QLF7; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000019502; 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:GAF57558.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          28..211
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   339 AA;  38438 MW;  61987A8729885B32 CRC64;
     MKLRILKSSV TNPWFNLATE DWIFNTLNPD SHTLFLWRNS ETVVIGRSQN PWVECKIDKM
     EADNVFLARR QSGGGAVFHD LGNTNFTFLS PKADYDQAAN FTIIINALKK LGIDADLSGR
     NDMQVGDKKI SGSAFKHAAD RSFHHGTLLV NANMQKLGDY LNPHPLKLKA KGIKSVRARV
     ANLVEFNEDI NHETLSEAII EAFCEYYRDK DYGDTTPIEA LDEASLAQQP SLNKYYEQMA
     DWDWRFGKTP EFSHHIETRF DWGIIDLHLD VKQAVIRDVV IFSDALNVEL IDQLKAALTG
     VKYNKEAIKA KLDELGKTHP DLAAQIDDVS VWLLREMEG
//