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Database: UniProt
Entry: A0A0A2UBW9_9BACL
LinkDB: A0A0A2UBW9_9BACL
Original site: A0A0A2UBW9_9BACL 
ID   A0A0A2UBW9_9BACL        Unreviewed;       333 AA.
AC   A0A0A2UBW9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   07-JUN-2017, entry version 18.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=P364_0106405 {ECO:0000313|EMBL:KGP83941.1};
OS   Paenibacillus sp. MAEPY2.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP83941.1, ECO:0000313|Proteomes:UP000030061};
RN   [1] {ECO:0000313|EMBL:KGP83941.1, ECO:0000313|Proteomes:UP000030061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP83941.1,
RC   ECO:0000313|Proteomes:UP000030061};
RX   PubMed=24526641;
RA   Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT   "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT   MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL   Genome Announc. 2:0-0(2014).
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:KGP83941.1}.
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DR   EMBL; AWUK01000008; KGP83941.1; -; Genomic_DNA.
DR   RefSeq; WP_024629363.1; NZ_AWUK01000008.1.
DR   EnsemblBacteria; KGP83941; KGP83941; P364_0106405.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000030061; 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:UP000030061};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KGP83941.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030061}.
FT   DOMAIN       27    214       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   333 AA;  38400 MW;  F80B267F9C1B54B6 CRC64;
     MLFVDNQGIT DPSVNLAIEE YILKHLPMDD SYLLFYINRP SIIIGKHQNT IEEINIEYVQ
     DNGVQVVRRL SGGGAVYHDL GNLNFSFITK DDGQSFHNFR KFTQPVVEAL QELGVNAELT
     GRNDLQVGEK KISGNAQFST RGRMFSHGTL MFNLNLDHVQ ASLNVNPEKF KSKSTKSVRS
     RVANIRDLID SNLTIEQFRD ELLRHIFRME PQDVPQYELT EKDWDKIKEI SAERYSNWDW
     NYGLSPESNV KHTRKFPVGI IDLRMNIKDG RIEDVKIFGD FFGVGDVADI EDMLRGKRYE
     ESEVRTALEG LDVKHYFGNL ELEDFIGLIF LEE
//
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