LPLAN_THEAC
ID LPLAN_THEAC Reviewed; 262 AA.
AC Q9HKT1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lipoate-protein ligase A subunit 1;
DE EC=6.3.1.20 {ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830};
DE AltName: Full=Lipoate--protein ligase subunit 1;
GN Name=lplA; OrderedLocusNames=Ta0514;
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 PROTEIN SEQUENCE OF 1-7, X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF
RP APOENZYME AND IN COMPLEX WITH LIPOIC ACID AND MAGNESIUM, LACK OF FUNCTION
RP AS A LIPOYL TRANSFERASE, SUBUNIT, AND MASS SPECTROMETRY.
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 TA0513, 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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, INTERACTION
RP WITH TA0513, 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP SUBSTRATES, AND FUNCTION IN LIPOATE ACTIVATION.
RX PubMed=16141198; DOI=10.1074/jbc.m507284200;
RA Kim D.J., Kim K.H., Lee H.H., Lee S.J., Ha J.Y., Yoon H.J., Suh S.W.;
RT "Crystal structure of lipoate-protein ligase A bound with the activated
RT intermediate. Insights into interaction with lipoyl domains.";
RL J. Biol. Chem. 280:38081-38089(2005).
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:16141198, ECO:0000269|PubMed:19520844,
CC 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:16141198, ECO:0000269|PubMed:16384580,
CC ECO:0000269|PubMed:19520844, ECO:0000269|PubMed:19594830}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=29872; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16384580};
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.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR EMBL; AL445064; CAC11654.1; -; Genomic_DNA.
DR RefSeq; WP_010900939.1; NC_002578.1.
DR PDB; 2ARS; X-ray; 2.04 A; A=1-262.
DR PDB; 2ART; X-ray; 2.40 A; A=1-262.
DR PDB; 2ARU; X-ray; 2.50 A; A=1-262.
DR PDB; 2C7I; X-ray; 2.10 A; A/B/C/D=1-262.
DR PDB; 2C8M; X-ray; 1.89 A; A/B/C/D=1-262.
DR PDB; 3R07; X-ray; 2.70 A; A=1-262.
DR PDBsum; 2ARS; -.
DR PDBsum; 2ART; -.
DR PDBsum; 2ARU; -.
DR PDBsum; 2C7I; -.
DR PDBsum; 2C8M; -.
DR PDBsum; 3R07; -.
DR AlphaFoldDB; Q9HKT1; -.
DR SMR; Q9HKT1; -.
DR IntAct; Q9HKT1; 1.
DR MINT; Q9HKT1; -.
DR STRING; 273075.Ta0514; -.
DR PRIDE; Q9HKT1; -.
DR EnsemblBacteria; CAC11654; CAC11654; CAC11654.
DR GeneID; 1456113; -.
DR KEGG; tac:Ta0514; -.
DR eggNOG; arCOG01939; Archaea.
DR HOGENOM; CLU_022986_0_0_2; -.
DR OMA; YHCTLLY; -.
DR OrthoDB; 47035at2157; -.
DR BioCyc; MetaCyc:MON-15675; -.
DR BRENDA; 6.3.1.20; 6324.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR EvolutionaryTrace; Q9HKT1; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0031405; F:lipoic acid binding; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
DR DisProt; DP00096; -.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..262
FT /note="Lipoate-protein ligase A subunit 1"
FT /id="PRO_0000209571"
FT DOMAIN 30..226
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 77..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 132..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16384580"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16384580"
FT BINDING 145
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16384580"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3R07"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2ARS"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:2C8M"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:2C8M"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2C8M"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:2C8M"
SQ SEQUENCE 262 AA; 29872 MW; CDF95B791BAD93A2 CRC64;
MEGRLLLLET PGNTRMSLAY DEAIYRSFQY GDKPILRFYR HDRSVIIGYF QVAEEEVDLD
YMKKNGIMLA RRYTGGGAVY HDLGDLNFSV VRSSDDMDIT SMFRTMNEAV VNSLRILGLD
ARPGELNDVS IPVNKKTDIM AGEKKIMGAA GAMRKGAKLW HAAMLVHTDL DMLSAVLKVP
DEKFRDKIAK STRERVANVT DFVDVSIDEV RNALIRGFSE TLHIDFREDT ITEKEESLAR
ELFDKKYSTE EWNMGLLRKE VV
