Reviewed, UniProtKB/Swiss-Prot Q1QEC2 (LPLA_PSYCK)

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:	Pcryo_0197

Organism

Psychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]

Taxonomic identifier

335284 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP MF_01602
Pathway	Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoic acid: step 1/2. HAMAP MF_01602 Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoic acid: 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.
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 – 339	339	Lipoate-protein ligase A HAMAP MF_01602		PRO_0000311126
Regions
	Nucleotide binding	75 – 78	4	ATP By similarity
Sites
	Binding site	70	1	ATP By similarity
	Binding site	129	1	ATP By similarity
	Binding site	129	1	Lipoate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1QEC2-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: FEE9767D1831EB73	FASTA	339	38,722
	10 20 30 40 50 60 MKLRILKSAV TNPWFNLATE DWIFNTLNPD SHTLFLWRNS ETVVIGRSQN PWVECKIDKM 70 80 90 100 110 120 EADDVFLARR QSGGGAVFHD LGNTNFTFLS PKDDYDQAAN FTIIINALKK LGIDADLSGR 130 140 150 160 170 180 NDMQVGDKKI SGSAFKHTAD RSFHHGTLLV NANMQKLGDY LNPHPLKLKA KGIKSVRARV 190 200 210 220 230 240 ANLVEFNEDI NHETLSDAII EAFREYYRDT DYGDTAPVEE LDEASLAKQP NLNKYYQQMA 250 260 270 280 290 300 DWDWRFGKTP EFTHHIETRF NWGIIDLHLD VKQAAIREVV IFSDALNVEL IDLLKESLAD 310 320 330 VKYDKHDIKA KFDELNRAHP ELAAQIDDVS EWLIGEMEG

References

[1]

"Complete sequence of chromosome of Psychrobacter cryohalolentis K5." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000323 Genomic DNA. Translation: ABE73981.1.
RefSeq	YP_579465.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4035677.
GenomeReviews	Gene locus Pcryo_0197 in contig CP000323_GR.
KEGG	pcr:Pcryo_0197.
NMPDR	fig|335284.3.peg.806.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1QEC2.
OMA	Q1QEC2. RKFSGNA.
Enzyme and pathway databases
BioCyc	PCRY335284:PCRYO_0197-MON.
Family and domain databases
HAMAP	MF_01602. [Tree]
InterPro	IPR004143. BPL_LipA_LipB. IPR005107. CO_DH_flav_C. IPR019491. Lipoate_protein_ligase_C. IPR004562. LipoylTrfase_LipoateP_Ligase. [Graphical view]
Gene3D	G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
Pfam	PF03099. BPL_LipA_LipB. 1 hit. PF10437. Lip_prot_lig_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00545. lipoyltrans. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LPLA_PSYCK

Accession

Primary (citable) accession number: Q1QEC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)