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Database: UniProt
Entry: A0A133Q4Y9_STALU
LinkDB: A0A133Q4Y9_STALU
Original site: A0A133Q4Y9_STALU 
ID   A0A133Q4Y9_STALU        Unreviewed;       340 AA.
AC   A0A133Q4Y9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=HMPREF3225_01428 {ECO:0000313|EMBL:KXA37934.1};
OS   Staphylococcus lugdunensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA37934.1, ECO:0000313|Proteomes:UP000070063};
RN   [1] {ECO:0000313|EMBL:KXA37934.1, ECO:0000313|Proteomes:UP000070063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7738 {ECO:0000313|EMBL:KXA37934.1,
RC   ECO:0000313|Proteomes:UP000070063};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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:KXA37934.1}.
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DR   EMBL; LRQI01000063; KXA37934.1; -; Genomic_DNA.
DR   RefSeq; WP_002460713.1; NZ_KQ957382.1.
DR   EnsemblBacteria; KXA37934; KXA37934; HMPREF3225_01428.
DR   PATRIC; fig|28035.7.peg.1448; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000070063; 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:UP000070063};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:KXA37934.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Transferase {ECO:0000313|EMBL:KXA37934.1}.
FT   DOMAIN       31    222       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   340 AA;  38401 MW;  F3B030857AD16BF0 CRC64;
     MYLIEPIRNG KYIADGAVNL AMQVYVNQHI FLDEDILLPY YCDPKIEIGR FQNTAIEINQ
     EYVDTHGIQV VRRDTGGGAV YVDKGAVNVC CILEQDTSIY GDFQRFYRPA IKALHHLGAT
     DVIQSGRNDL TLHGKKISGA AMTVINNRIY GGYSLLLDVD YDAMVQSLNP NRKKIESKGI
     KSVRARVGNI RDSLAPEYQD ITIQAFKDLI IKQIMGIDDI SDAKRYTLTD EDWAGIDQLV
     ADKYANWEWN YGHSPRYEYN RNARFACGTI DISLSVTQNR ISGCSIFGDF FGQGDIHDVE
     THLVGTRMVK QDLIARLEDI DLNYYFGSLS AEELTQLILS
//
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