UniProtKB - P32099 (LPLA_ECOLI)
Protein
Lipoate-protein ligase A
Gene
lplA
Organism
Escherichia coli (strain K12)
Status
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
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.
Catalytic activityi
- (R)-lipoate + [lipoyl-carrier protein]-L-lysine + ATP = [lipoyl-carrier protein]-(R)-N6-lipoyl-L-lysine + AMP + diphosphate + H+EC:6.3.1.20
Activity regulationi
6-seleno-octanoate, 8-thio-octanoate and 8-seleno-octanoate caused 100%, 50% and 63% inhibition respectively. Inhibited by Cu2+.
Kineticsi
- KM=1.9 µM for ATP1 Publication
- KM=1.7 µM for D,L-lipoic acid1 Publication
- KM=152 µM for magnesium ion1 Publication
- Vmax=40 nmol/min/mg enzyme toward ATP1 Publication
- 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
: protein lipoylation via exogenous pathway Pathwayi
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:
- Lipoate-protein ligase A (lplA)
- Lipoate-protein ligase A (lplA), Lipoate-protein ligase A (lplA), Lipoate-protein ligase A (lplA), Lipoate-protein ligase A (lplA), Lipoate-protein ligase A (lplA)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 71 | ATPBy similarity | 1 | |
Binding sitei | 134 | ATPBy similarity | 1 | |
Binding sitei | 134 | LipoateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 76 – 79 | ATPBy similarity | 4 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- lipoate-protein ligase activity Source: CAFA
- lipoyltransferase activity Source: CAFA
GO - Biological processi
- protein lipoylation Source: CAFA
Keywordsi
Molecular function | Ligase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11796-MONOMER ECOL316407:JW4349-MONOMER MetaCyc:EG11796-MONOMER |
BRENDAi | 2.7.7.63 2026 |
UniPathwayi | UPA00537;UER00594 UPA00537;UER00595 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:lplA Synonyms:yjjF Ordered Locus Names:b4386, JW4349 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
- mitochondrion Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 73 | S → A: 20-fold decrease in affinity for ATP. 1 Publication | 1 | |
Mutagenesisi | 141 | R → A: More than 10-fold reduction in Vmax. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000209564 | 2 – 338 | Lipoate-protein ligase AAdd BLAST | 337 |
Proteomic databases
jPOSTi | P32099 |
PaxDbi | P32099 |
PRIDEi | P32099 |
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
BioGridi | 4262787, 24 interactors |
DIPi | DIP-10119N |
IntActi | P32099, 3 interactors |
STRINGi | 511145.b4386 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P32099 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32099 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 29 – 216 | BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST | 188 |
Sequence similaritiesi
Belongs to the LplA family.Curated
Phylogenomic databases
eggNOGi | ENOG4107RMF Bacteria COG0095 LUCA |
HOGENOMi | HOG000260594 |
InParanoidi | P32099 |
KOi | K03800 |
PhylomeDBi | P32099 |
Family and domain databases
HAMAPi | MF_01602 LplA, 1 hit |
InterProi | View protein in InterPro IPR004143 BPL_LPL_catalytic IPR023741 Lipoate_ligase_A IPR019491 Lipoate_protein_ligase_C IPR004562 LipoylTrfase_LipoateP_Ligase |
PANTHERi | PTHR12561 PTHR12561, 1 hit PTHR12561:SF5 PTHR12561:SF5, 1 hit |
Pfami | View protein in Pfam PF03099 BPL_LplA_LipB, 1 hit PF10437 Lip_prot_lig_C, 1 hit |
TIGRFAMsi | TIGR00545 lipoyltrans, 1 hit |
PROSITEi | View protein in PROSITE PS51733 BPL_LPL_CATALYTIC, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P32099-1 [UniParc]FASTAAdd to basket
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
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 74 | G → S in lplA1 or slr1; selenolipoate resistance mutation. 1 Publication | 1 |
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 |
PIRi | A54035 |
RefSeqi | NP_418803.1, NC_000913.3 WP_000105884.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC77339; AAC77339; b4386 BAE78375; BAE78375; BAE78375 |
GeneIDi | 944865 |
KEGGi | ecj:JW4349 eco:b4386 |
PATRICi | fig|1411691.4.peg.2299 |
Similar proteinsi
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 |
PIRi | A54035 |
RefSeqi | NP_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 entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1X2G | X-ray | 2.40 | A/B/C | 2-338 | [»] | |
1X2H | X-ray | 2.91 | A/B/C | 2-338 | [»] | |
3A7A | X-ray | 3.10 | A/C | 2-338 | [»] | |
3A7R | X-ray | 2.05 | A | 2-338 | [»] | |
4TVW | X-ray | 3.50 | A/B/C/D | 1-338 | [»] | |
4TVY | X-ray | 2.15 | A/B | 1-338 | [»] | |
SMRi | P32099 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 4262787, 24 interactors |
DIPi | DIP-10119N |
IntActi | P32099, 3 interactors |
STRINGi | 511145.b4386 |
Proteomic databases
jPOSTi | P32099 |
PaxDbi | P32099 |
PRIDEi | P32099 |
Genome annotation databases
EnsemblBacteriai | AAC77339; AAC77339; b4386 BAE78375; BAE78375; BAE78375 |
GeneIDi | 944865 |
KEGGi | ecj:JW4349 eco:b4386 |
PATRICi | fig|1411691.4.peg.2299 |
Organism-specific databases
EchoBASEi | EB1744 |
Phylogenomic databases
eggNOGi | ENOG4107RMF Bacteria COG0095 LUCA |
HOGENOMi | HOG000260594 |
InParanoidi | P32099 |
KOi | K03800 |
PhylomeDBi | P32099 |
Enzyme and pathway databases
UniPathwayi | UPA00537;UER00594 UPA00537;UER00595 |
BioCyci | EcoCyc:EG11796-MONOMER ECOL316407:JW4349-MONOMER MetaCyc:EG11796-MONOMER |
BRENDAi | 2.7.7.63 2026 |
Miscellaneous databases
EvolutionaryTracei | P32099 |
PROi | PR:P32099 |
Family and domain databases
HAMAPi | MF_01602 LplA, 1 hit |
InterProi | View protein in InterPro IPR004143 BPL_LPL_catalytic IPR023741 Lipoate_ligase_A IPR019491 Lipoate_protein_ligase_C IPR004562 LipoylTrfase_LipoateP_Ligase |
PANTHERi | PTHR12561 PTHR12561, 1 hit PTHR12561:SF5 PTHR12561:SF5, 1 hit |
Pfami | View protein in Pfam PF03099 BPL_LplA_LipB, 1 hit PF10437 Lip_prot_lig_C, 1 hit |
TIGRFAMsi | TIGR00545 lipoyltrans, 1 hit |
PROSITEi | View protein in PROSITE PS51733 BPL_LPL_CATALYTIC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LPLA_ECOLI | |
Accessioni | P32099Primary (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 13, 2019 | |
This is version 164 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references