ID   LPLA_SHISS              Reviewed;         338 AA.
AC   Q3YU08;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Lipoate-protein ligase A;
DE            EC=2.7.7.63;
DE   AltName: Full=Lipoate--protein ligase;
GN   Name=lplA; OrderedLocusNames=SSON_4536;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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.
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DR   EMBL; CP000038; AAZ91004.1; -; Genomic_DNA.
DR   RefSeq; YP_313239.1; -.
DR   SMR; Q3YU08; 2-338.
DR   GeneID; 3668069; -.
DR   GenomeReviews; CP000038_GR; SSON_4536.
DR   KEGG; ssn:SSON_4536; -.
DR   HOGENOM; Q3YU08; -.
DR   OMA; Q3YU08; YEQSHLE.
DR   BioCyc; SSON300269:SSO_4536-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    338       Lipoate-protein ligase A.
FT                                /FTId=PRO_1000069390.
FT   NP_BIND      76     79       ATP (By similarity).
FT   BINDING      71     71       ATP (By similarity).
FT   BINDING     134    134       ATP (By similarity).
FT   BINDING     134    134       Lipoate (By similarity).
SQ   SEQUENCE   338 AA;  37910 MW;  FE230928FD55523E CRC64;
     MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVSAEASG
     RNDLVVKTVE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS
     VRSRVTNLTE LLPGITHEQV CEAITKAFFA HYGERVEAEI ISPDKTPDLP NFAETFARQS
     SWEWNFGQAP AFSHLLDERF SWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG
     CLYRADMLQQ ECEALLVDFP DQEKELRELS TWIAGAVR
//