C0Q7M8 (LPLA_SALPC) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	SPC_4708

Organism

Salmonella paratyphi C (strain RKS4594) [Complete proteome] [HAMAP]

Taxonomic identifier

476213 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella enterica subsp. enterica serovar Paratyphi C

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP-Rule MF_01602
Catalytic activity	ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP-Rule MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. 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 By similarity.
Subcellular location	Cytoplasm By similarity.
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 By similarity. HAMAP-Rule MF_01602
Sequence similarities	Belongs to the LplA family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptidyl-lysine lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate-protein ligase activity Inferred from electronic annotation. Source: HAMAP 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 – 338	338	Lipoate-protein ligase A HAMAP-Rule MF_01602		PRO_1000185797
Regions
	Nucleotide binding	76 – 79	4	ATP By similarity
Sites
	Binding site	71	1	ATP By similarity
	Binding site	134	1	ATP By similarity
	Binding site	134	1	Lipoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	C0Q7M8 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: B2E07A75E495FCB9	FASTA	338	37,700
	10 20 30 40 50 60 MTTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR 70 80 90 100 110 120 MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STHIVLAALN SLGVMADASG 130 140 150 160 170 180 RNDLVVKTPD GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS 190 200 210 220 230 240 VRSRVANLTE LLPGITHEQV CQAVTEAFFA HYGERVDAEV ISPNKTPDLP NFAETFARQS 250 260 270 280 290 300 SWEWNFGQAP AFSHLLDEHF TWGGVELHFD VEKGVITRAQ VFTDSLNPAP LEALAGRLQG 310 320 330 CQYRADVLEQ ACESLIAEFP AQKGELRELA AWMAQAVR

References

[1]

"Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis and pathogenic convergence with Salmonella typhi." Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L. PLoS ONE 4:E4510-E4510(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RKS4594.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000857 Genomic DNA. Translation: ACN48751.1.
RefSeq	YP_002640192.1. NC_012125.1.
3D structure databases
ProteinModelPortal	C0Q7M8.
ModBase	Search...
Protein-protein interaction databases
STRING	476213.SPC_4708.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACN48751; ACN48751; SPC_4708.
GeneID	7557287.
KEGG	sei:SPC_4708.
PATRIC	32368389. VBISalEnt12305_4739.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0095.
HOGENOM	HOG000260594.
KO	K03800.
OMA	INLINPT.
ProtClustDB	PRK03822.
Enzyme and pathway databases
BioCyc	SENT476213:GH8J-4803-MONOMER.
UniPathway	UPA00537; UER00594. UPA00537; UER00595.
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...

Entry information

Entry name

LPLA_SALPC

Accession

Primary (citable) accession number: C0Q7M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program