Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATPBy similarity
Binding sitei134 – 1341ATPBy similarity
Binding sitei134 – 1341LipoateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 794ATPBy similarity

GO - Molecular functioni

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731S → A: 20-fold decrease in affinity for ATP. 1 Publication
Mutagenesisi141 – 1411R → A: More than 10-fold reduction in Vmax. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 338337Lipoate-protein ligase APRO_0000209564Add
BLAST

Proteomic databases

PaxDbiP32099.
PRIDEiP32099.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
yncEP761161EBI-553559,EBI-562173

Protein-protein interaction databases

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

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi14 – 2714Combined sources
Beta strandi33 – 386Combined sources
Beta strandi41 – 466Combined sources
Helixi52 – 554Combined sources
Helixi58 – 636Combined sources
Beta strandi67 – 704Combined sources
Beta strandi78 – 803Combined sources
Beta strandi84 – 929Combined sources
Turni93 – 953Combined sources
Helixi98 – 11114Combined sources
Beta strandi117 – 1193Combined sources
Turni120 – 1223Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi144 – 15613Combined sources
Helixi159 – 1657Combined sources
Beta strandi172 – 1754Combined sources
Helixi188 – 1903Combined sources
Helixi197 – 21216Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi223 – 2253Combined sources
Helixi232 – 2409Combined sources
Helixi242 – 2454Combined sources
Turni246 – 2483Combined sources
Beta strandi252 – 2609Combined sources
Beta strandi263 – 27210Combined sources
Beta strandi275 – 2839Combined sources
Helixi289 – 2979Combined sources
Turni298 – 3003Combined sources
Beta strandi302 – 3043Combined sources
Helixi305 – 31410Combined sources
Turni315 – 3184Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 33715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32099.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 216188BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

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.
OrthoDBiEOG6038ZS.
PhylomeDBiP32099.

Family and domain databases

HAMAPiMF_01602. LplA.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741G → S in lplA1 or slr1; selenolipoate resistance mutation. 1 Publication

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
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. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262787. 9 interactions.
DIPiDIP-10119N.
IntActiP32099. 3 interactions.
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.
OrthoDBiEOG6038ZS.
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.
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...

Publicationsi

  1. "Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product."
    Morris T.W., Reed K.E., Cronan J.E. Jr.
    J. Biol. Chem. 269:16091-16100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, CHARACTERIZATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "An Escherichia coli membrane protein with a unique signal sequence."
    Neuwald A.F., Stauffer G.V.
    Gene 82:219-228(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
    Strain: K12.
  6. "Purification and properties of the lipoate protein ligase of Escherichia coli."
    Green D.E., Morris T.W., Green J., Cronan J.E. Jr., Guest J.R.
    Biochem. J. 309:853-862(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein."
    Morris T.W., Reed K.E., Cronan J.E. Jr.
    J. Bacteriol. 177:1-10(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-74.
  8. "The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase."
    Jordan S.W., Cronan J.E. Jr.
    J. Bacteriol. 185:1582-1589(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12 / JK1.
  9. "Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site."
    Fujiwara K., Toma S., Okamura-Ikeda K., Motokawa Y., Nakagawa A., Taniguchi H.
    J. Biol. Chem. 280:33645-33651(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), MUTAGENESIS OF SER-73 AND ARG-141.

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: June 8, 2016
This is version 141 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.