Lipoate-protein ligase A - Escherichia coli (strain K12)

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P32099 (LPLA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Lipoate-protein ligase A
EC=2.7.7.63

Alternative name(s):
Lipoate--protein ligase

Gene names

Name:	lplA
Synonyms:	yjjF
Ordered Locus Names:	b4386, JW4349

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6
Catalytic activity	ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP-Rule MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP-Rule MF_01602
Enzyme regulation	6-seleno-octanoate, 8-thio-octanoate and 8-seleno-octanoate caused 100%, 50% and 63% inhibition respectively. Inhibited by Cu²⁺. HAMAP-Rule MF_01602
Pathway	Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. HAMAP-Rule MF_01602 Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
Subunit structure	Monomer. Ref.6
Subcellular location	Cytoplasm HAMAP-Rule MF_01602.
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. HAMAP-Rule MF_01602
Sequence similarities	Belongs to the LplA family.
Biophysicochemical properties	Kinetic parameters: K_M=1.9 µM for ATP Ref.6 K_M=1.7 µM for D,L-lipoic acid K_M=152 µM for magnesium ion V_max=40 nmol/min/mg enzyme toward ATP V_max=24 nmol/min/mg enzyme toward D,L-lipoic acid pH dependence: Most active from pH 5.5 to 8.0. Inactive below pH 4.3.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-lysine lipoylation Inferred from electronic annotation. Source: HAMAP protein lipoylation Inferred from mutant phenotype Ref.1. Source: EcoCyc
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate-protein ligase activity Inferred from mutant phenotype Ref.1. Source: EcoliWiki transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
yncE	P76116	1	EBI-553559,EBI-562173

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 338

337

Lipoate-protein ligase A HAMAP-Rule MF_01602

PRO_0000209564

Regions

Nucleotide binding

76 – 79

ATP By similarity

Sites

Binding site

ATP By similarity

Binding site

134

ATP By similarity

Binding site

134

Lipoate By similarity

Natural variations

Natural variant

G → S in lplA1 or slr1; selenolipoate resistance mutation. Ref.7

Experimental info

Mutagenesis

S → A: 20-fold decrease in affinity for ATP. Ref.9

Mutagenesis

141

R → A: More than 10-fold reduction in Vmax. Ref.9

Secondary structure

338

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32099 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 102788082E182A6F
Show »

FASTA

338

37,926

        10         20         30         40         50         60 
MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR 

        70         80         90        100        110        120 
MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVSAEASG 

       130        140        150        160        170        180 
RNDLVVKTVE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS 

       190        200        210        220        230        240 
VRSRVTNLTE LLPGITHEQV CEAITEAFFA HYGERVEAEI ISPNKTPDLP NFAETFARQS 

       250        260        270        280        290        300 
SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG 

       310        320        330 
CLYRADMLQQ ECEALLVDFP EQEKELRELS AWMAGAVR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A54035.

RefSeq

NP_418803.1. NC_000913.2.
YP_492516.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P32099.

SMR

P32099. Positions 2-338.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10119N.

IntAct

P32099. 3 interactions.

MINT

MINT-1288545.

STRING

511145.b4386.

Proteomic databases

PaxDb

P32099.

PRIDE

P32099.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77339; AAC77339; b4386.
BAE78375; BAE78375; BAE78375.

GeneID

12933793.
944865.

KEGG

ecj:Y75_p4270.
eco:b4386.

PATRIC

32124388. VBIEscCol129921_4534.

Organism-specific databases

EchoBASE

EB1744.

EcoGene

EG11796. lplA.

Phylogenomic databases

eggNOG

COG0095.

HOGENOM

HOG000260594.

K03800.

OMA

SEERYQN.

ProtClustDB

PRK03822.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11796-MONOMER.
ECOL316407:JW4349-MONOMER.
MetaCyc:EG11796-MONOMER.

UniPathway

UPA00537; UER00594.
UPA00537; UER00595.

Gene expression databases

Genevestigator

P32099.

Family and domain databases

HAMAP

MF_01602. LplA.

InterPro

IPR004143. BPL_LipA_LipB.
IPR023741. Lipoate_ligase_A.
IPR019491. Lipoate_protein_ligase_C.
IPR004562. LipoylTrfase_LipoateP_Ligase.
[Graphical view]

Pfam

PF03099. BPL_LplA_LipB. 1 hit.
PF10437. Lip_prot_lig_C. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00545. lipoyltrans. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P32099.

Entry information

Entry name

LPLA_ECOLI

Accession

Primary (citable) accession number: P32099
Secondary accession number(s): Q2M5T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents