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Database: UniProt
Entry: A0A150WDK3_BDEBC
LinkDB: A0A150WDK3_BDEBC
Original site: A0A150WDK3_BDEBC 
ID   A0A150WDK3_BDEBC        Unreviewed;       339 AA.
AC   A0A150WDK3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
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   Name=lplA {ECO:0000313|EMBL:KYG60952.1};
GN   ORFNames=AZI86_18720 {ECO:0000313|EMBL:KYG60952.1};
OS   Bdellovibrio bacteriovorus.
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=959 {ECO:0000313|EMBL:KYG60952.1, ECO:0000313|Proteomes:UP000075320};
RN   [1] {ECO:0000313|EMBL:KYG60952.1, ECO:0000313|Proteomes:UP000075320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R0 {ECO:0000313|EMBL:KYG60952.1,
RC   ECO:0000313|Proteomes:UP000075320};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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:KYG60952.1}.
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DR   EMBL; LUKE01000008; KYG60952.1; -; Genomic_DNA.
DR   RefSeq; WP_061836830.1; NZ_LUKE01000008.1.
DR   EnsemblBacteria; KYG60952; KYG60952; AZI86_18720.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000075320; 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; PF03099; BPL_LplA_LipB; 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:UP000075320};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00894000};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KYG60952.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075320}.
FT   DOMAIN       29    216       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   339 AA;  38767 MW;  3DDF572AA308EE5E CRC64;
     MKKLKVFLSE SKNPHLNIAT EEWIFDNLDP SQQVLFLWQN EETVVIGRNQ NPWNECNLAK
     MKEDKVHLAR RKTGGGAVFH DLGNICFTFL SPREEYKREN NVQIIFNALK ELGITGEASG
     RNDLLIPFPD GPRKFSGSAY REKKDRAFHH GTLLLHADLT RLGNYLTPNP KKLQAKGKES
     VRARVANLNE VRPGIEAKHI VEYMVPAFER FYDGKADIEM LSLATVNKNA ELKGHYDQLS
     SWEWLYGNTL EFTHKMDEYL SLGFFDFQFK VEDGVIKDVH IYTDCLYPSL VDELTTRLKG
     QPYRGDSVKA AIEAAKTKHP DLIAGVSELG QWLLKNIEI
//
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