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Protein

Lipoate-protein ligase A subunit 1

Gene

lplA

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.3 Publications

Catalytic activityi

ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate.2 Publications

Pathwayi: protein lipoylation via exogenous pathway

This protein is involved in step 1 and 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lipoate-protein ligase A subunit 2 (lplB), Lipoate-protein ligase A subunit 1 (lplA)
  2. Lipoate-protein ligase A subunit 2 (lplB), Lipoate-protein ligase A subunit 1 (lplA)
This subpathway is part of the pathway protein lipoylation via exogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from lipoate, the pathway protein lipoylation via exogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATP
Binding sitei85 – 851ATP
Metal bindingi137 – 1371Magnesium1 Publication
Metal bindingi138 – 1381Magnesium1 Publication
Binding sitei145 – 1451ATP
Binding sitei145 – 1451Lipoate
Metal bindingi149 – 1491Magnesium; via amide nitrogen1 Publication
Binding sitei149 – 1491ATP; via amide nitrogen and carbonyl oxygen
Binding sitei163 – 1631ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 804ATP
Nucleotide bindingi132 – 1354ATP

GO - Molecular functioni

GO - Biological processi

  • protein lipoylation Source: UniProtKB

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15675.
BRENDAi2.7.7.63. 6324.
UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoate-protein ligase A subunit 1 (EC:6.3.1.202 Publications)
Alternative name(s):
Lipoate--protein ligase subunit 1
Gene namesi
Name:lplA
Ordered Locus Names:Ta0514
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Lipoate-protein ligase A subunit 1PRO_0000209571Add
BLAST

Proteomic databases

PRIDEiQ9HKT1.

Interactioni

Subunit structurei

Heterodimer composed of LplA and LplB.4 Publications

Protein-protein interaction databases

IntActiQ9HKT1. 1 interaction.
MINTiMINT-7103708.
STRINGi273075.Ta0514.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi14 – 2714Combined sources
Beta strandi35 – 395Combined sources
Beta strandi42 – 476Combined sources
Helixi53 – 564Combined sources
Helixi59 – 646Combined sources
Beta strandi68 – 714Combined sources
Beta strandi79 – 813Combined sources
Beta strandi85 – 939Combined sources
Helixi99 – 11618Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi144 – 15411Combined sources
Beta strandi157 – 16711Combined sources
Helixi170 – 1767Combined sources
Helixi182 – 1843Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 2013Combined sources
Helixi207 – 22216Combined sources
Beta strandi225 – 2284Combined sources
Helixi233 – 24513Combined sources
Turni246 – 2483Combined sources
Helixi250 – 2545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ARSX-ray2.04A1-262[»]
2ARTX-ray2.40A1-262[»]
2ARUX-ray2.50A1-262[»]
2C7IX-ray2.10A/B/C/D1-262[»]
2C8MX-ray1.89A/B/C/D1-262[»]
3R07X-ray2.70A1-262[»]
DisProtiDP00096.
ProteinModelPortaliQ9HKT1.
SMRiQ9HKT1. Positions 1-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HKT1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 226197BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the LplA family.Curated
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG01939. Archaea.
COG0095. LUCA.
HOGENOMiHOG000245032.
KOiK03800.
OMAiRTMNEAV.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HKT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGRLLLLET PGNTRMSLAY DEAIYRSFQY GDKPILRFYR HDRSVIIGYF
60 70 80 90 100
QVAEEEVDLD YMKKNGIMLA RRYTGGGAVY HDLGDLNFSV VRSSDDMDIT
110 120 130 140 150
SMFRTMNEAV VNSLRILGLD ARPGELNDVS IPVNKKTDIM AGEKKIMGAA
160 170 180 190 200
GAMRKGAKLW HAAMLVHTDL DMLSAVLKVP DEKFRDKIAK STRERVANVT
210 220 230 240 250
DFVDVSIDEV RNALIRGFSE TLHIDFREDT ITEKEESLAR ELFDKKYSTE
260
EWNMGLLRKE VV
Length:262
Mass (Da):29,872
Last modified:March 1, 2001 - v1
Checksum:iCDF95B791BAD93A2
GO

Mass spectrometryi

Molecular mass is 29872±3 Da from positions 1 - 262. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11654.1.
RefSeqiWP_010900939.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11654; CAC11654; CAC11654.
GeneIDi1456113.
KEGGitac:Ta0514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11654.1.
RefSeqiWP_010900939.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ARSX-ray2.04A1-262[»]
2ARTX-ray2.40A1-262[»]
2ARUX-ray2.50A1-262[»]
2C7IX-ray2.10A/B/C/D1-262[»]
2C8MX-ray1.89A/B/C/D1-262[»]
3R07X-ray2.70A1-262[»]
DisProtiDP00096.
ProteinModelPortaliQ9HKT1.
SMRiQ9HKT1. Positions 1-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9HKT1. 1 interaction.
MINTiMINT-7103708.
STRINGi273075.Ta0514.

Proteomic databases

PRIDEiQ9HKT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11654; CAC11654; CAC11654.
GeneIDi1456113.
KEGGitac:Ta0514.

Phylogenomic databases

eggNOGiarCOG01939. Archaea.
COG0095. LUCA.
HOGENOMiHOG000245032.
KOiK03800.
OMAiRTMNEAV.

Enzyme and pathway databases

UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.
BioCyciMetaCyc:MONOMER-15675.
BRENDAi2.7.7.63. 6324.

Miscellaneous databases

EvolutionaryTraceiQ9HKT1.

Family and domain databases

InterProiIPR004143. BPL_LPL_catalytic.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  2. "Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification."
    McManus E., Luisi B.F., Perham R.N.
    J. Mol. Biol. 356:625-637(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7, X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH LIPOIC ACID AND MAGNESIUM, LACK OF FUNCTION AS A LIPOYL TRANSFERASE, SUBUNIT, MASS SPECTROMETRY.
  3. "A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins."
    Posner M.G., Upadhyay A., Bagby S., Hough D.W., Danson M.J.
    FEBS J. 276:4012-4022(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH TA0513, PATHWAY.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  4. "The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases."
    Christensen Q.H., Cronan J.E.
    J. Biol. Chem. 284:21317-21326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, INTERACTION WITH TA0513, PATHWAY.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  5. "Crystal structure of lipoate-protein ligase A bound with the activated intermediate. Insights into interaction with lipoyl domains."
    Kim D.J., Kim K.H., Lee H.H., Lee S.J., Ha J.Y., Yoon H.J., Suh S.W.
    J. Biol. Chem. 280:38081-38089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATES, FUNCTION IN LIPOATE ACTIVATION.

Entry informationi

Entry nameiLPLAN_THEAC
AccessioniPrimary (citable) accession number: Q9HKT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to E.coli, where the lipoate-protein ligase is encoded by a single gene product (LplA) with a large N-terminal domain and a small C-terminal domain, the same activity in T.acidophilum is dependent on two separate proteins, corresponding to the two domains of E.coli LplA, respectively.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.