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Database: UniProt
Entry: R1CUF8_9CLOT
LinkDB: R1CUF8_9CLOT
Original site: R1CUF8_9CLOT 
ID   R1CUF8_9CLOT            Unreviewed;       326 AA.
AC   R1CUF8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   07-JUN-2017, entry version 28.
DE   RecName: Full=Lipoate--protein ligase {ECO:0000256|SAAS:SAAS00603724};
DE            EC=6.3.1.20 {ECO:0000256|SAAS:SAAS00603724};
GN   ORFNames=L21TH_1608 {ECO:0000313|EMBL:EOD00309.1};
OS   Caldisalinibacter kiritimatiensis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Caldisalinibacter.
OX   NCBI_TaxID=1304284 {ECO:0000313|EMBL:EOD00309.1, ECO:0000313|Proteomes:UP000013378};
RN   [1] {ECO:0000313|EMBL:EOD00309.1, ECO:0000313|Proteomes:UP000013378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-TH-D2 {ECO:0000313|EMBL:EOD00309.1,
RC   ECO:0000313|Proteomes:UP000013378};
RA   Ben Hania W., Joseph M., Fiebig A., Bunk B., Klenk H.-P.,
RA   Fardeau M.-L., Spring S.;
RT   "Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately
RT   thermohalophilic thiosulfate-reducing bacterium from a hypersaline
RT   microbial mat.";
RL   Geomicrobiol. J. 32:347-354(2015).
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:EOD00309.1}.
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DR   EMBL; ARZA01000186; EOD00309.1; -; Genomic_DNA.
DR   EnsemblBacteria; EOD00309; EOD00309; L21TH_1608.
DR   PATRIC; fig|1304284.3.peg.1576; -.
DR   OrthoDB; POG091H03KP; -.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000013378; 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:UP000013378};
KW   Ligase {ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:EOD00309.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00026749};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013378}.
FT   DOMAIN       27    210       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
SQ   SEQUENCE   326 AA;  37931 MW;  2FBEABA93EF2B4C0 CRC64;
     MTRIVETSSV NPWYNLAMEE YLFNNISDKE IILYLWQNKD TVVIGRNQNP WKECRCEELK
     RDGGKLARRL SGGGAVYHDL GNLNFTFIMK EYLYDFEKQI QVILNGIKQL GIQAEFTGRN
     DIVVQGKKIS GNAFYFSNNR AYHHGTILVD TDFSKLSTYL QPSKAKIMSK GIDSVKSRVI
     NLKELKSDIT IDTVKKSIKQ SFINIYNGTN EDMGINESNE EIKRLYKKYS SWEWRYGDSP
     DFDIKFSDKF TWGEIDIRLR LQEGYIKRVT IYSDAMNSTL IQKLAHELKG IQLKLDNIIK
     KIDDVAYDCE DNNIIKDIKE LFIKMI
//
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