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Protein

Lipoate-protein ligase A

Gene

lplA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.1 Publication

Catalytic activityi

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

Enzyme regulationi

6-seleno-octanoate, 8-thio-octanoate and 8-seleno-octanoate caused 100%, 50% and 63% inhibition respectively. Inhibited by Cu2+.

Kineticsi

  1. KM=1.9 µM for ATP1 Publication
  2. KM=1.7 µM for D,L-lipoic acid1 Publication
  3. KM=152 µM for magnesium ion1 Publication
  1. Vmax=40 nmol/min/mg enzyme toward ATP1 Publication
  2. Vmax=24 nmol/min/mg enzyme toward D,L-lipoic acid1 Publication

pH dependencei

Most active from pH 5.5 to 8.0. Inactive below pH 4.3.1 Publication

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 (lplA)
  2. Lipoate-protein ligase A (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 sitei71ATPBy similarity1
Binding sitei134ATPBy similarity1
Binding sitei134LipoateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi76 – 79ATPBy similarity4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • lipoate-protein ligase activity Source: EcoCyc
  • lipoyltransferase activity Source: GO_Central

GO - Biological processi

  • peptidyl-lysine lipoylation Source: UniProtKB-HAMAP
  • protein lipoylation Source: EcoCyc

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11796-MONOMER.
ECOL316407:JW4349-MONOMER.
MetaCyc:EG11796-MONOMER.
BRENDAi2.7.7.63. 2026.
UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoate-protein ligase A (EC:6.3.1.20)
Alternative name(s):
Lipoate--protein ligase
Gene namesi
Name:lplA
Synonyms:yjjF
Ordered Locus Names:b4386, JW4349
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11796. lplA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73S → A: 20-fold decrease in affinity for ATP. 1 Publication1
Mutagenesisi141R → A: More than 10-fold reduction in Vmax. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002095642 – 338Lipoate-protein ligase AAdd BLAST337

Proteomic databases

PaxDbiP32099.
PRIDEiP32099.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4262787. 9 interactors.
DIPiDIP-10119N.
IntActiP32099. 3 interactors.
MINTiMINT-1288545.
STRINGi511145.b4386.

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi14 – 27Combined sources14
Beta strandi33 – 38Combined sources6
Beta strandi41 – 46Combined sources6
Helixi52 – 55Combined sources4
Helixi58 – 63Combined sources6
Beta strandi67 – 70Combined sources4
Beta strandi78 – 80Combined sources3
Beta strandi84 – 92Combined sources9
Turni93 – 95Combined sources3
Helixi98 – 111Combined sources14
Beta strandi117 – 119Combined sources3
Turni120 – 122Combined sources3
Beta strandi123 – 126Combined sources4
Beta strandi133 – 142Combined sources10
Beta strandi144 – 156Combined sources13
Helixi159 – 165Combined sources7
Beta strandi172 – 175Combined sources4
Helixi188 – 190Combined sources3
Helixi197 – 212Combined sources16
Beta strandi219 – 221Combined sources3
Beta strandi223 – 225Combined sources3
Helixi232 – 240Combined sources9
Helixi242 – 245Combined sources4
Turni246 – 248Combined sources3
Beta strandi252 – 260Combined sources9
Beta strandi263 – 272Combined sources10
Beta strandi275 – 283Combined sources9
Helixi289 – 297Combined sources9
Turni298 – 300Combined sources3
Beta strandi302 – 304Combined sources3
Helixi305 – 314Combined sources10
Turni315 – 318Combined sources4
Helixi320 – 322Combined sources3
Helixi323 – 337Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X2GX-ray2.40A/B/C2-338[»]
1X2HX-ray2.91A/B/C2-338[»]
3A7AX-ray3.10A/C2-338[»]
3A7RX-ray2.05A2-338[»]
4TVWX-ray3.50A/B/C/D1-338[»]
4TVYX-ray2.15A/B1-338[»]
ProteinModelPortaliP32099.
SMRiP32099.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32099.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 216BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST188

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107RMF. Bacteria.
COG0095. LUCA.
HOGENOMiHOG000260594.
InParanoidiP32099.
KOiK03800.
OMAiWRNAETV.
PhylomeDBiP32099.

Family and domain databases

HAMAPiMF_01602. LplA. 1 hit.
InterProiIPR004143. BPL_LPL_catalytic.
IPR023741. Lipoate_ligase_A.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ
60 70 80 90 100
NPWKECNTRR MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI
110 120 130 140 150
STSIVLNALN ALGVSAEASG RNDLVVKTVE GDRKVSGSAY RETKDRGFHH
160 170 180 190 200
GTLLLNADLS RLANYLNPDK KKLAAKGITS VRSRVTNLTE LLPGITHEQV
210 220 230 240 250
CEAITEAFFA HYGERVEAEI ISPNKTPDLP NFAETFARQS SWEWNFGQAP
260 270 280 290 300
AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG
310 320 330
CLYRADMLQQ ECEALLVDFP EQEKELRELS AWMAGAVR
Length:338
Mass (Da):37,926
Last modified:January 23, 2007 - v3
Checksum:i102788082E182A6F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti74G → S in lplA1 or slr1; selenolipoate resistance mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27665 Genomic DNA. Translation: AAA21740.1.
U14003 Genomic DNA. Translation: AAA97282.1.
U00096 Genomic DNA. Translation: AAC77339.1.
AP009048 Genomic DNA. Translation: BAE78375.1.
X03046 Genomic DNA. Translation: CAA26854.1.
PIRiA54035.
RefSeqiNP_418803.1. NC_000913.3.
WP_000105884.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77339; AAC77339; b4386.
BAE78375; BAE78375; BAE78375.
GeneIDi944865.
KEGGiecj:JW4349.
eco:b4386.
PATRICi32124388. VBIEscCol129921_4534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27665 Genomic DNA. Translation: AAA21740.1.
U14003 Genomic DNA. Translation: AAA97282.1.
U00096 Genomic DNA. Translation: AAC77339.1.
AP009048 Genomic DNA. Translation: BAE78375.1.
X03046 Genomic DNA. Translation: CAA26854.1.
PIRiA54035.
RefSeqiNP_418803.1. NC_000913.3.
WP_000105884.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X2GX-ray2.40A/B/C2-338[»]
1X2HX-ray2.91A/B/C2-338[»]
3A7AX-ray3.10A/C2-338[»]
3A7RX-ray2.05A2-338[»]
4TVWX-ray3.50A/B/C/D1-338[»]
4TVYX-ray2.15A/B1-338[»]
ProteinModelPortaliP32099.
SMRiP32099.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262787. 9 interactors.
DIPiDIP-10119N.
IntActiP32099. 3 interactors.
MINTiMINT-1288545.
STRINGi511145.b4386.

Proteomic databases

PaxDbiP32099.
PRIDEiP32099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77339; AAC77339; b4386.
BAE78375; BAE78375; BAE78375.
GeneIDi944865.
KEGGiecj:JW4349.
eco:b4386.
PATRICi32124388. VBIEscCol129921_4534.

Organism-specific databases

EchoBASEiEB1744.
EcoGeneiEG11796. lplA.

Phylogenomic databases

eggNOGiENOG4107RMF. Bacteria.
COG0095. LUCA.
HOGENOMiHOG000260594.
InParanoidiP32099.
KOiK03800.
OMAiWRNAETV.
PhylomeDBiP32099.

Enzyme and pathway databases

UniPathwayiUPA00537; UER00594.
UPA00537; UER00595.
BioCyciEcoCyc:EG11796-MONOMER.
ECOL316407:JW4349-MONOMER.
MetaCyc:EG11796-MONOMER.
BRENDAi2.7.7.63. 2026.

Miscellaneous databases

EvolutionaryTraceiP32099.
PROiP32099.

Family and domain databases

HAMAPiMF_01602. LplA. 1 hit.
InterProiIPR004143. BPL_LPL_catalytic.
IPR023741. Lipoate_ligase_A.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00545. lipoyltrans. 1 hit.
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLPLA_ECOLI
AccessioniPrimary (citable) accession number: P32099
Secondary accession number(s): Q2M5T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.