ID   LPLA_PSYCK              Reviewed;         339 AA.
AC   Q1QEC2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Lipoate-protein ligase A;
DE            EC=2.7.7.63;
DE   AltName: Full=Lipoate--protein ligase;
GN   Name=lplA; OrderedLocusNames=Pcryo_0197;
OS   Psychrobacter cryohalolentis (strain K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of
CC       exogenously supplied lipoate to lipoyl-AMP and the transfer of the
CC       activated lipoyl onto the lipoyl domains of lipoate-dependent
CC       enzymes (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + lipoate = diphosphate + lipoyl-AMP.
CC   -!- CATALYTIC ACTIVITY: Lipoyl-AMP + protein = protein N(6)-
CC       (lipoyl)lysine + AMP.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 1/2.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 2/2.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group
CC       of lipoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes (By similarity).
CC   -!- SIMILARITY: Belongs to the lplA family.
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DR   EMBL; CP000323; ABE73981.1; -; Genomic_DNA.
DR   RefSeq; YP_579465.1; -.
DR   GeneID; 4035677; -.
DR   GenomeReviews; CP000323_GR; Pcryo_0197.
DR   KEGG; pcr:Pcryo_0197; -.
DR   NMPDR; fig|335284.3.peg.806; -.
DR   HOGENOM; Q1QEC2; -.
DR   OMA; Q1QEC2; RKFSGNA.
DR   BioCyc; PCRY335284:PCRYO_0197-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018055; P:peptidyl-lysine lipoylation; IEA:HAMAP.
DR   HAMAP; MF_01602; -; 1.
DR   InterPro; IPR004143; BPL_LipA_LipB.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   Gene3D; G3DSA:3.30.390.50; CO_DH_flav_C; 1.
DR   Pfam; PF03099; BPL_LipA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    339       Lipoate-protein ligase A.
FT                                /FTId=PRO_0000311126.
FT   NP_BIND      75     78       ATP (By similarity).
FT   BINDING      70     70       ATP (By similarity).
FT   BINDING     129    129       ATP (By similarity).
FT   BINDING     129    129       Lipoate (By similarity).
SQ   SEQUENCE   339 AA;  38722 MW;  FEE9767D1831EB73 CRC64;
     MKLRILKSAV TNPWFNLATE DWIFNTLNPD SHTLFLWRNS ETVVIGRSQN PWVECKIDKM
     EADDVFLARR QSGGGAVFHD LGNTNFTFLS PKDDYDQAAN FTIIINALKK LGIDADLSGR
     NDMQVGDKKI SGSAFKHTAD RSFHHGTLLV NANMQKLGDY LNPHPLKLKA KGIKSVRARV
     ANLVEFNEDI NHETLSDAII EAFREYYRDT DYGDTAPVEE LDEASLAKQP NLNKYYQQMA
     DWDWRFGKTP EFTHHIETRF NWGIIDLHLD VKQAAIREVV IFSDALNVEL IDLLKESLAD
     VKYDKHDIKA KFDELNRAHP ELAAQIDDVS EWLIGEMEG
//