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Database: UniProt
Entry: C2ESH5_9LACO
LinkDB: C2ESH5_9LACO
Original site: C2ESH5_9LACO 
ID   C2ESH5_9LACO            Unreviewed;       342 AA.
AC   C2ESH5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=HMPREF0549_0411 {ECO:0000313|EMBL:EEJ41140.1};
OS   Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ41140.1, ECO:0000313|Proteomes:UP000004483};
RN   [1] {ECO:0000313|EMBL:EEJ41140.1, ECO:0000313|Proteomes:UP000004483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ41140.1,
RC   ECO:0000313|Proteomes:UP000004483};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:EEJ41140.1}.
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DR   EMBL; ACGV01000026; EEJ41140.1; -; Genomic_DNA.
DR   RefSeq; WP_003717058.1; NZ_GG693413.1.
DR   AlphaFoldDB; C2ESH5; -.
DR   STRING; 1423814.HMPREF0549_0411; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_0_2_9; -.
DR   OrthoDB; 9788148at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000004483; 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:EEJ41140.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EEJ41140.1};
KW   Transferase {ECO:0000313|EMBL:EEJ41140.1}.
FT   DOMAIN          31..214
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   342 AA;  38121 MW;  F4C0928EEEEE46F1 CRC64;
     MFFIDTSRNG KPVHDALVNQ SLDNYLINDL RLKGHGLICY INQPSVIIGV NQNAYAEIDL
     PYLKEHQIEL VRRSSGGGAV YHDFGNLVFE NIVVGDTSKF GDFHAIGDPI VDALHDLGIS
     SAEVSGRNDM TIDGKKFSGM AIVKGDNSYA AGGTVMFDLN MQNANEVLTP EQDKLASKGV
     KSVNARVTNI KPYLPEKYQH WTTEDFKEYL LCHMFGVDSM DQVETYHLTD HDWSIIDSRL
     DKQYRTDLWN YGHNPGFDNY VSKHFPIGTV SFNFNESNGV ITSIKIYGDF FTTGDPAIIE
     HNLNGTKLDS SSLISSLKQS NLEANLGQIS PEELADLILS RK
//
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