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Database: UniProt
Entry: F9PWJ3_9STRE
LinkDB: F9PWJ3_9STRE
Original site: F9PWJ3_9STRE 
ID   F9PWJ3_9STRE            Unreviewed;       329 AA.
AC   F9PWJ3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-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   ORFNames=HMPREF9954_1222 {ECO:0000313|EMBL:EGV04017.1};
OS   Streptococcus infantis SK970.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1035189 {ECO:0000313|EMBL:EGV04017.1, ECO:0000313|Proteomes:UP000005460};
RN   [1] {ECO:0000313|EMBL:EGV04017.1, ECO:0000313|Proteomes:UP000005460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK970 {ECO:0000313|EMBL:EGV04017.1,
RC   ECO:0000313|Proteomes:UP000005460};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Nelson K.E.;
RL   Submitted (JUL-2011) 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:EGV04017.1}.
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DR   EMBL; AFUT01000003; EGV04017.1; -; Genomic_DNA.
DR   RefSeq; WP_006154380.1; NZ_AFUT01000003.1.
DR   STRING; 1035189.HMPREF9954_1222; -.
DR   EnsemblBacteria; EGV04017; EGV04017; HMPREF9954_1222.
DR   PATRIC; fig|1035189.4.peg.693; -.
DR   eggNOG; ENOG4105DF9; Bacteria.
DR   eggNOG; COG0095; LUCA.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000005460; 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:0016740; F:transferase 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:UP000005460};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:EGV04017.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005460};
KW   Transferase {ECO:0000313|EMBL:EGV04017.1}.
FT   DOMAIN       26    213       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   329 AA;  37731 MW;  B3FDA5E34C6F5F61 CRC64;
     MKYIINHSND TAFNIALEEY AFKHLLDEDQ IFLLWINKPS IIVGRHQNTI EEINRDYVRE
     HGIEVVRRIS GGGAVYHDLN NLNYTIISKE DENKAFDFKS FSTPVINTLA ELGVKAEFTG
     RNDLEIDGKK FCGNAQAYIN GRIMHHGCLL FDVDLSVLAN ALKVSKDKFE SKGVKSVRAR
     VTNIIDELPE KITVEEFRDL LLEYMKKEYP EMTEYVFSDE ELAEINRIKD TKFGTWDWNY
     GKSPEYNVRR GTKFPSGKVE IFANVIESKI QDIKIYGDFF GIEDVAAVED VLRGVKYERE
     DVLKALQTLN LGRYFAGITA EEIAEAVVE
//
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