Q5GT50 (LIPB_WOLTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Octanoyltransferase
EC=2.3.1.181

Alternative name(s):
Lipoate-protein ligase B
Lipoyl/octanoyl transferase
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase

Gene names

Name:	lipB
Ordered Locus Names:	Wbm0235

Organism

Wolbachia sp. subsp. Brugia malayi (strain TRS) [Complete proteome] [HAMAP]

Taxonomic identifier

292805 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Wolbachieae › Wolbachia › Wolbachia endosymbiont of Brugia malayi

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate By similarity. HAMAP-Rule MF_00013
Catalytic activity	Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. HAMAP-Rule MF_00013
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. HAMAP-Rule MF_00013
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00013.
Miscellaneous	In the reaction, the free carboxyl group of octanoic 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_00013
Sequence similarities	Belongs to the LipB family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from electronic annotation. Source: InterPro lipoate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipoyl(octanoyl) transferase activity Inferred from electronic annotation. Source: EC octanoyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 205	205	Octanoyltransferase HAMAP-Rule MF_00013		PRO_0000242780
Regions
	Region	68 – 75	8	Substrate binding By similarity
	Region	140 – 142	3	Substrate binding By similarity
	Region	153 – 155	3	Substrate binding By similarity
Sites
	Active site	171	1	Acyl-thioester intermediate By similarity
	Site	137	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5GT50 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: D10747AED75A8722	FASTA	205	23,781
	10 20 30 40 50 60 MVEWLISDQL INYNYAVKFM EKKIQQIHNN SSDELVWLLQ HPPLYTAGIS ATDDDVVEKL 70 80 90 100 110 120 LPIYKTGRGG KYTYHGPGQR IIYLMLNLKK RNKCDIKLYI RELGSWIINV LKHFNIFGEF 130 140 150 160 170 180 KEDRIGVWVN NNGVEEKIAA FGIRLRKWIT YHGIALNFSP DLSHYKGIIP CGLKGYGVTS 190 200 IKELGVKAPL FKLDNILKKE FYKIF

References

[1]

"The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode." Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S. , Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B. PLoS Biol. 3:599-614(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TRS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017321 Genomic DNA. Translation: AAW70824.1.
RefSeq	YP_198066.1. NC_006833.1.
3D structure databases
ProteinModelPortal	Q5GT50.
ModBase	Search...
Protein-protein interaction databases
STRING	292805.Wbm0235.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW70824; AAW70824; Wbm0235.
GeneID	3266637.
KEGG	wbm:Wbm0235.
PATRIC	24032011. VBIWolEnd7741_0386.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0321.
HOGENOM	HOG000194320.
KO	K03801.
OMA	DAHPRAD.
ProtClustDB	PRK14341.
Enzyme and pathway databases
UniPathway	UPA00538; UER00592.
Family and domain databases
HAMAP	MF_00013. LipB.
InterPro	IPR004143. BPL_LipA_LipB. IPR000544. Octanoyltransferase. IPR020605. Octanoyltransferase_CS. [Graphical view]
PANTHER	PTHR10993:SF0. PTHR10993:SF0. 1 hit.
Pfam	PF03099. BPL_LplA_LipB. 1 hit. [Graphical view]
PIRSF	PIRSF016262. LPLase. 1 hit.
TIGRFAMs	TIGR00214. lipB. 1 hit.
PROSITE	PS01313. LIPB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIPB_WOLTR

Accession

Primary (citable) accession number: Q5GT50

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 1, 2005
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program