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Database: UniProt
Entry: S6HQE5_9GAMM
LinkDB: S6HQE5_9GAMM
Original site: S6HQE5_9GAMM 
ID   S6HQE5_9GAMM            Unreviewed;       273 AA.
AC   S6HQE5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 24.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00899171};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
DE   AltName: Full=Lipoate-protein ligase A {ECO:0000256|SAAS:SAAS00894004};
GN   ORFNames=OFPII_13800 {ECO:0000313|EMBL:EPJ47309.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   unclassified Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ47309.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ47309.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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. {ECO:0000256|SAAS:SAAS00894010}.
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier
CC       protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine
CC       + AMP + diphosphate. {ECO:0000256|SAAS:SAAS00603726}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|SAAS:SAAS00701662}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS00894007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00894009}.
CC   -!- SIMILARITY: Belongs to the LplA family.
CC       {ECO:0000256|SAAS:SAAS00894016}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPJ47309.1}.
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DR   EMBL; ASZJ01000070; EPJ47309.1; -; Genomic_DNA.
DR   PATRIC; fig|1330036.3.peg.1310; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR023741; Lipoate_ligase_A.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; PTHR12561; 1.
DR   PANTHER; PTHR12561:SF5; PTHR12561:SF5; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00428641};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014822};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00894000};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:EPJ47309.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT   DOMAIN        1    151       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   273 AA;  30857 MW;  FEE5D73723775885 CRC64;
     MYLARRQSGG GAVFQDLGNT NFTFMASKPE YSKDVSTAIV LNALQSLGIE GRVNGRNDMV
     VGEGEQLRKF SGSAYKEAKD RGFHHGTLLL NTDLSRLANY LNPDPKKLKA KGISSVRSRV
     VNLNSIKQEI DHQMVCDAIV SEFSKHYGES PELEFISPEN MPDLADFASR YATQKSWQWN
     FGKSLQFTHT LEERFSWGGV ELHLKLEKAH ISESKIFTDS LYPDPLEFFN EQLKGVVYHP
     QHLAACFDKV VQAYPNHKIE LLELRDWLAT AIA
//
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