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Database: UniProt
Entry: J9WA32_LACBU
LinkDB: J9WA32_LACBU
Original site: J9WA32_LACBU 
ID   J9WA32_LACBU            Unreviewed;       340 AA.
AC   J9WA32;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-NOV-2017, entry version 31.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   Name=lpla3 {ECO:0000313|EMBL:AFS00936.1};
GN   ORFNames=LBUCD034_1947 {ECO:0000313|EMBL:AFS00936.1};
OS   Lactobacillus buchneri CD034.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1071400 {ECO:0000313|EMBL:AFS00936.1, ECO:0000313|Proteomes:UP000007332};
RN   [1] {ECO:0000313|EMBL:AFS00936.1, ECO:0000313|Proteomes:UP000007332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD034 {ECO:0000313|EMBL:AFS00936.1};
RX   PubMed=22465289; DOI=10.1016/j.jbiotec.2012.03.007;
RA   Heinl S., Wibberg D., Eikmeyer F., Szczepanowski R., Blom J.,
RA   Linke B., Goesmann A., Grabherr R., Schwab H., Puhler A., Schluter A.;
RT   "Insights into the completely annotated genome of Lactobacillus
RT   buchneri CD034, a strain isolated from stable grass silage.";
RL   J. Biotechnol. 161:153-166(2012).
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}.
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DR   EMBL; CP003043; AFS00936.1; -; Genomic_DNA.
DR   RefSeq; WP_014940446.1; NC_018610.1.
DR   EnsemblBacteria; AFS00936; AFS00936; LBUCD034_1947.
DR   GeneID; 34322834; -.
DR   KEGG; lbn:LBUCD034_1947; -.
DR   PATRIC; fig|1071400.3.peg.1864; -.
DR   KO; K03800; -.
DR   OrthoDB; POG091H03KP; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000007332; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase 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:UP000007332};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:AFS00936.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:AFS00936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007332};
KW   Transferase {ECO:0000313|EMBL:AFS00936.1}.
FT   DOMAIN       21    213       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   340 AA;  37870 MW;  842350525BCDBD68 CRC64;
     MKYLKDPTVE QAFPEYLQTT AKFSDALVYF YHPQTPIVIC GVHQNVFAEV NMAYLQAHGI
     DLVRRGSGGG AVYVDPGNLT YVFIDTEPTV QHPHFRKYAQ PVVKALQSLG VNAESDSRND
     LTVDGRKFSG MSASKIGHRV SYGGTLMIDV DIEAASSVLK PSRAKLRAKG VQSVHSRVTN
     LREHFDDAHR TVSIDQVQQT ILTQVFQTTD LAQVPTYRLT EKDWQAIVSL AHTKYGSKTW
     IFGAGNQHQY YRDGYFNGIG TVGIGFSIQD NHVVDSKIYG DFLQPNSNLH AITERLDGTE
     FNLSALTEAF ARADLTTSIG PIPSKRLAEI MLDRLHDEQF
//
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