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Database: UniProt
Entry: A0A095ZAY2_9FIRM
LinkDB: A0A095ZAY2_9FIRM
Original site: A0A095ZAY2_9FIRM 
ID   A0A095ZAY2_9FIRM        Unreviewed;       329 AA.
AC   A0A095ZAY2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   15-MAR-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=HMPREF2134_11830 {ECO:0000313|EMBL:KGF31935.1};
OS   Peptoniphilus lacrimalis DNF00528.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1401070 {ECO:0000313|EMBL:KGF31935.1, ECO:0000313|Proteomes:UP000029621};
RN   [1] {ECO:0000313|EMBL:KGF31935.1, ECO:0000313|Proteomes:UP000029621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00528 {ECO:0000313|EMBL:KGF31935.1,
RC   ECO:0000313|Proteomes:UP000029621};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KGF31935.1}.
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DR   EMBL; JRNL01000091; KGF31935.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGF31935; KGF31935; HMPREF2134_11830.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000029621; 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:UP000029621};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KGF31935.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029621}.
FT   DOMAIN       26    213       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   329 AA;  37794 MW;  4516E5582729F27B CRC64;
     MKYIINHSND TAFNIALEEY AFKHLLDEDQ IFLLWINKPS IIVGRHQNTI EEINRDYVRE
     NGIEVVRRIS GGGAVYHDLN NLNYTIISKE DENKAFDFKS FSTPVINTLA ELGVKAEFTG
     RNDLEIDGKK FCGNAQAYIN GRIMHHGCLL FDVDLSVLAN ALKVSKDKFE SKGVKSVRAR
     VTNIIDELPE KITVEEFRDL LLEYMKKEYP EMTEYVFSDE ELAEINRIKE TKFGTWDWNY
     GKSPEYNVRR GTKFPSGKVE IFANVIESKI QDIKIYGDFF GIEDVAAVED VLRDIKYERE
     DVLKALQTIN LGRYFAGITA EEIAEAVVE
//
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