Lipoate-protein ligase A subunit 1 - Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

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Q9HKT1 (LPLAN_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lipoate-protein ligase A subunit 1
EC=2.7.7.63

Alternative name(s):
Lipoate--protein ligase subunit 1

Gene names

Name:	lplA
Ordered Locus Names:	Ta0514

Organism

Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

Taxonomic identifier

273075 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.3 Ref.4 Ref.5
Catalytic activity	ATP + lipoate = diphosphate + lipoyl-AMP. Ref.3 Ref.4 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. Ref.3 Ref.4
Pathway	Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. Ref.3 Ref.4 Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
Subunit structure	Heterodimer composed of LplA and LplB. Ref.2 Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity.
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.
Sequence similarities	Belongs to the lplA family.
Mass spectrometry	Molecular mass is 29872±3 Da from positions 1 - 262. Determined by ESI. Ref.2

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein lipoylation Inferred from direct assay Ref.3. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.3. Source: UniProtKB transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 262

262

Lipoate-protein ligase A subunit 1

PRO_0000209571

Regions

Nucleotide binding

77 – 80

ATP

Nucleotide binding

132 – 135

ATP

Sites

Metal binding

137

Magnesium

Metal binding

138

Magnesium

Metal binding

149

Magnesium; via amide nitrogen

Binding site

ATP

Binding site

ATP

Binding site

145

ATP

Binding site

145

Lipoate

Binding site

149

ATP; via amide nitrogen and carbonyl oxygen

Binding site

163

ATP; via carbonyl oxygen

Secondary structure

262

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HKT1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: CDF95B791BAD93A2
Show »

FASTA

262

29,872

        10         20         30         40         50         60 
MEGRLLLLET PGNTRMSLAY DEAIYRSFQY GDKPILRFYR HDRSVIIGYF QVAEEEVDLD 

        70         80         90        100        110        120 
YMKKNGIMLA RRYTGGGAVY HDLGDLNFSV VRSSDDMDIT SMFRTMNEAV VNSLRILGLD 

       130        140        150        160        170        180 
ARPGELNDVS IPVNKKTDIM AGEKKIMGAA GAMRKGAKLW HAAMLVHTDL DMLSAVLKVP 

       190        200        210        220        230        240 
DEKFRDKIAK STRERVANVT DFVDVSIDEV RNALIRGFSE TLHIDFREDT ITEKEESLAR 

       250        260 
ELFDKKYSTE EWNMGLLRKE VV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11029001] [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: 16384580] [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: 19594830] [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: 19520844] [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: 16141198] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATES, FUNCTION IN LIPOATE ACTIVATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL445064 Genomic DNA. Translation: CAC11654.1.

RefSeq

NP_393990.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ARS	X-ray	2.04	A	1-262	[»]
2ART	X-ray	2.40	A	1-262	[»]
2ARU	X-ray	2.50	A	1-262	[»]
2C7I	X-ray	2.10	A/B/C/D	1-262	[»]
2C8M	X-ray	1.89	A/B/C/D	1-262	[»]

ProteinModelPortal

Q9HKT1.

SMR

Q9HKT1. Positions 1-257.

DisProt

DP00096.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7103708.

Proteomic databases

PRIDE

Q9HKT1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1456113.

GenomeReviews

Gene locus Ta0514 in contig AL139299_GR.

KEGG

tac:Ta0514.

NMPDR

fig|273075.1.peg.512.

Phylogenomic databases

HOGENOM

HBG650514.

OMA

VRSEVTN.

PhylomeDB

Q9HKT1.

ProtClustDB

CLSK337563.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15675.
TACI273075:TA0514-MONOMER.

BRENDA

2.7.7.63. 6324.

Family and domain databases

InterPro

IPR004143. BPL_LipA_LipB.
[Graphical view]

K03800.

Pfam

PF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LPLAN_THEAC

Accession

Primary (citable) accession number: Q9HKT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	March 1, 2001
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents