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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)DescriptionActionsGraphical viewLength
Binding sitei72ATP1
Binding sitei85ATP1
Metal bindingi137Magnesium1 Publication1
Metal bindingi138Magnesium1 Publication1
Binding sitei145ATP1
Binding sitei145Lipoate1
Metal bindingi149Magnesium; via amide nitrogen1 Publication1
Binding sitei149ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei163ATP; via carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi77 – 80ATP4
Nucleotide bindingi132 – 135ATP4

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002095711 – 262Lipoate-protein ligase A subunit 1Add BLAST262

Proteomic databases

PRIDEiQ9HKT1.

Interactioni

Subunit structurei

Heterodimer composed of LplA and LplB.4 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi14 – 27Combined sources14
Beta strandi35 – 39Combined sources5
Beta strandi42 – 47Combined sources6
Helixi53 – 56Combined sources4
Helixi59 – 64Combined sources6
Beta strandi68 – 71Combined sources4
Beta strandi79 – 81Combined sources3
Beta strandi85 – 93Combined sources9
Helixi99 – 116Combined sources18
Beta strandi131 – 135Combined sources5
Beta strandi138 – 141Combined sources4
Beta strandi144 – 154Combined sources11
Beta strandi157 – 167Combined sources11
Helixi170 – 176Combined sources7
Helixi182 – 184Combined sources3
Helixi193 – 195Combined sources3
Helixi199 – 201Combined sources3
Helixi207 – 222Combined sources16
Beta strandi225 – 228Combined sources4
Helixi233 – 245Combined sources13
Turni246 – 248Combined sources3
Helixi250 – 254Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HKT1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 226BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST197

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.
OMAiGNEAWIF.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9HKT1. 1 interactor.
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.
OMAiGNEAWIF.

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...

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: November 2, 2016
This is version 97 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.