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
//
