LPLAC_THEAC
ID LPLAC_THEAC Reviewed; 94 AA.
AC Q9HKT2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Lipoate-protein ligase A subunit 2;
DE EC=6.3.1.20 {ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830};
DE AltName: Full=C-terminal domain of LplA;
DE Short=CTD;
DE AltName: Full=Lipoate--protein ligase subunit 2;
GN Name=lplB; OrderedLocusNames=Ta0513;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP POSSIBLE FUNCTION.
RX PubMed=16384580; DOI=10.1016/j.jmb.2005.11.057;
RA McManus E., Luisi B.F., Perham R.N.;
RT "Structure of a putative lipoate protein ligase from Thermoplasma
RT acidophilum and the mechanism of target selection for post-translational
RT modification.";
RL J. Mol. Biol. 356:625-637(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH TA0514, AND
RP PATHWAY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=19594830; DOI=10.1111/j.1742-4658.2009.07110.x;
RA Posner M.G., Upadhyay A., Bagby S., Hough D.W., Danson M.J.;
RT "A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma
RT acidophilum requires two proteins.";
RL FEBS J. 276:4012-4022(2009).
RN [4]
RP GENE NAME, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT,
RP INTERACTION WITH TA0514, AND PATHWAY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=19520844; DOI=10.1074/jbc.m109.015016;
RA Christensen Q.H., Cronan J.E.;
RT "The Thermoplasma acidophilum LplA-LplB complex defines a new class of
RT bipartite lipoate-protein ligases.";
RL J. Biol. Chem. 284:21317-21326(2009).
CC -!- FUNCTION: Part of a lipoate-protein ligase complex that catalyzes both
CC the ATP-dependent activation of exogenously supplied lipoate to lipoyl-
CC AMP and the transfer of the activated lipoyl onto the lipoyl domains of
CC lipoate-dependent enzymes. Can also use octanoate as substrate.
CC {ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC H(+); Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:456215; EC=6.3.1.20;
CC Evidence={ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC -!- SUBUNIT: Heterodimer composed of LplA and LplB.
CC {ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830}.
CC -!- MISCELLANEOUS: In contrast to E.coli, where the lipoate-protein ligase
CC is encoded by a single gene product (LplA) with a large N-terminal
CC domain and a small C-terminal domain, the same activity in
CC T.acidophilum is dependent on two separate proteins, corresponding to
CC the two domains of E.coli LplA, respectively.
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DR EMBL; AL445064; CAC11653.1; -; Genomic_DNA.
DR PDB; 3R07; X-ray; 2.70 A; C=7-94.
DR PDBsum; 3R07; -.
DR AlphaFoldDB; Q9HKT2; -.
DR SMR; Q9HKT2; -.
DR IntAct; Q9HKT2; 2.
DR MINT; Q9HKT2; -.
DR STRING; 273075.Ta0513m; -.
DR EnsemblBacteria; CAC11653; CAC11653; CAC11653.
DR KEGG; tac:Ta0513; -.
DR eggNOG; arCOG03837; Archaea.
DR HOGENOM; CLU_181210_0_0_2; -.
DR OMA; PYINVED; -.
DR OrthoDB; 129723at2157; -.
DR BioCyc; MetaCyc:MON-15674; -.
DR BRENDA; 6.3.1.20; 6324.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..94
FT /note="Lipoate-protein ligase A subunit 2"
FT /id="PRO_0000311127"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:3R07"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:3R07"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:3R07"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:3R07"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:3R07"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3R07"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3R07"
SQ SEQUENCE 94 AA; 10980 MW; ACA43ADFA3F7D634 CRC64;
MVLNYTMHMM YSKNWKAKKG LIRVTLDLDG NRIKDIHISG DFFMFPEDSI NRLEDMLRGS
SIEKINDIIR DFYNQGVITP GVEPEDFIQA LRVI
