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Database: UniProt
Entry: A0A147KAG9_9BACI
LinkDB: A0A147KAG9_9BACI
Original site: A0A147KAG9_9BACI 
ID   A0A147KAG9_9BACI        Unreviewed;       330 AA.
AC   A0A147KAG9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=Q75_04230 {ECO:0000313|EMBL:KUP07718.1};
OS   Bacillus coahuilensis p1.1.43.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP07718.1, ECO:0000313|Proteomes:UP000074108};
RN   [1] {ECO:0000313|EMBL:KUP07718.1, ECO:0000313|Proteomes:UP000074108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX   PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA   Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D.,
RA   Souza V., Olmedo-Alvarez G.;
RT   "Microevolution Analysis of Bacillus coahuilensis Unveils Differences
RT   in Phosphorus Acquisition Strategies and Their Regulation.";
RL   Front. Microbiol. 7:58-58(2016).
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   -!- 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:KUP07718.1}.
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DR   EMBL; LDYG01000020; KUP07718.1; -; Genomic_DNA.
DR   RefSeq; WP_059350505.1; NZ_LDYG01000020.1.
DR   EnsemblBacteria; KUP07718; KUP07718; Q75_04230.
DR   PATRIC; fig|1150625.3.peg.884; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000074108; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; PTHR12561; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00428641};
KW   Complete proteome {ECO:0000313|Proteomes:UP000074108};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KUP07718.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT   DOMAIN       28    215       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   330 AA;  38058 MW;  E28E6B591E4AD532 CRC64;
     MLFIDNNGIT DPHINLAMEE FVLKHLDVEK ETYFLFYINE PSIIIGKNQN TIEEINTEYV
     EAQKLHVVRR LSGGGAVYHD LGNLNFSFIT KDDGNSFHNF KKFTEPVIEA LQELGVKAEL
     SGRNDILAEG RKISGNAQFS TKGRMFSHGT LLFHSEMDHV VSALKVKKDK IESKGIKSVR
     SRVANITEFL TDTITIEEFR QLLLEHIFGG KDSIQEYKLT DEDWDTIEEI SKKRYRNWDW
     NYGKSPKFNI QHSHRFPVGQ IDIRMEVSKG TIQDCVIFGD FFGVGDVAEI QEKLKGIRYD
     RESIERALLD VNVKHYFGNV EKEDLLNLIY
//
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