ID   LPLA_BLOPB              Reviewed;         339 AA.
AC   Q492U9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Lipoate-protein ligase A;
DE            EC=2.7.7.63;
DE   AltName: Full=Lipoate--protein ligase;
GN   Name=lplA; OrderedLocusNames=BPEN_368;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000016; AAZ40993.1; -; Genomic_DNA.
DR   RefSeq; YP_277868.1; -.
DR   GeneID; 3563042; -.
DR   GenomeReviews; CP000016_GR; BPEN_368.
DR   KEGG; bpn:BPEN_368; -.
DR   HOGENOM; Q492U9; -.
DR   OMA; Q492U9; YEQSHLE.
DR   BioCyc; CBLO291272:BPEN_368-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_0000311125.
FT   NP_BIND      76     79       ATP (By similarity).
FT   BINDING      71     71       ATP (By similarity).
FT   BINDING     135    135       ATP (By similarity).
FT   BINDING     135    135       Lipoate (By similarity).
SQ   SEQUENCE   339 AA;  39198 MW;  A0790CCFE243EA82 CRC64;
     MCSLRLLLSD SYDPWFNLSL EEYIYKNIPK KQSILFLWRN QNTVVIGRAQ NAWKECNTRR
     MERDGIKLAR RNSGGGAVFH DLGNTCFTFI STQEHYDKSI SSNIVLNGLS YIGIKAIISG
     RNDIVIRTEN GEHRKISGSA YRETSGRKFH HGTLLLHVDI DKLDYYLNPD FKKLETKGIT
     SIRSRVANLN ELKPGINHQE VCLGLTEAFF QHYGMKVKPE ILSTDNFCKI PEFFKQFNKQ
     SDWNWNFGSA PAFTHQLDTR FDWGSVTLHC DIERGIIHRS HIFTDSLDPS PLEILAKKLV
     GIPYNNKSIL CCCKEWMQSW PQYKKELSEV SHWLIKTIS
//