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Database: UniProt
Entry: F9QD84_9MOLU
LinkDB: F9QD84_9MOLU
Original site: F9QD84_9MOLU 
ID   F9QD84_9MOLU            Unreviewed;       326 AA.
AC   F9QD84;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 32.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=GIG_01950 {ECO:0000313|EMBL:EGS29342.1};
OS   Mycoplasma anatis 1340.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1034808 {ECO:0000313|EMBL:EGS29342.1, ECO:0000313|Proteomes:UP000005055};
RN   [1] {ECO:0000313|EMBL:EGS29342.1, ECO:0000313|Proteomes:UP000005055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1340 {ECO:0000313|EMBL:EGS29342.1,
RC   ECO:0000313|Proteomes:UP000005055};
RX   PubMed=21952548; DOI=10.1128/JB.05891-11;
RA   Guo Z., Chen P., Ren P., Kuang S., Zhou Z., Li Z., Liu M., Shi D.,
RA   Xiao Y., Wang X., Zhou R., Jin H., Bi D.;
RT   "Genome Sequence of Duck Pathogen Mycoplasma anatis Strain 1340.";
RL   J. Bacteriol. 193:5883-5884(2011).
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:EGS29342.1}.
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DR   EMBL; AFVJ01000015; EGS29342.1; -; Genomic_DNA.
DR   RefSeq; WP_006886453.1; NZ_AFVJ01000015.1.
DR   STRING; 1034808.GIG_01950; -.
DR   EnsemblBacteria; EGS29342; EGS29342; GIG_01950.
DR   eggNOG; ENOG4107UFM; Bacteria.
DR   eggNOG; COG0095; LUCA.
DR   OrthoDB; POG091H03KP; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000005055; 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:UP000005055};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:EGS29342.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005055}.
FT   DOMAIN       26    211       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   326 AA;  37393 MW;  364D8483C2EA119B CRC64;
     MKIFRIKSTS PYTTLSLEEL ITSDPEMTGD IFLIYQHNNA VIIGRNQNAY EEIKRDYIEE
     NKIELARRIS GGGAVYHDLG NINFSFITDY NKQAGYEKFL QPIISFLNSL GLNAEFHGRN
     DILCNGAKIS GNAQFIKGNR IVSHGTLLFD VDLTKLSNAL NPSKLKLESK GVQSIRQRVT
     NIAKELNYSM SVEEFIEKLI EHFVKNGDGE IIEIPYKKYE DKLNQMIEYK KSNEWLYNKN
     ADFQASNAKK FPGGILKIKY NVENNKFKEI VFEGDFLSKL DVNEIVGKFD NLEYSKQAVI
     DVLNSIRFEE YFGTIQIDEI LELIFG
//
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