P60722 (LIPB_ECOL6) 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:	c0720

Organism

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

199310 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	213 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 – 213	213	Octanoyltransferase HAMAP-Rule MF_00013		PRO_0000062836
Regions
	Region	71 – 78	8	Substrate binding By similarity
	Region	138 – 140	3	Substrate binding By similarity
	Region	151 – 153	3	Substrate binding By similarity
Sites
	Active site	169	1	Acyl-thioester intermediate By similarity
	Site	135	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60722 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: 56EE2BB105F99EAD	FASTA	213	23,883
	10 20 30 40 50 60 MYQDKILVRQ LGLQPYEPIS QAMHEFTDTR DDSTLDEIWL VEHYPVFTQG QAGKAEHILM 70 80 90 100 110 120 PGDIPVIQSD RGGQVTYHGP GQQVMYVLLN LKRRKLGVRE LVTLLEQTVV NTLAELGIEA 130 140 150 160 170 180 HPRADAPGVY VGEKKICSLG LRIRRGCSFH GLALNVNMDL SPFLRINPCG YAGMEMAKIS 190 200 210 QWKPEATTNN IAPRLLENIL ALLNNPDFEY ITA

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN79193.1.
RefSeq	NP_752650.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P60722.
SMR	P60722. Positions 5-173.
ModBase	Search...
Protein-protein interaction databases
STRING	199310.c0720.
Proteomic databases
PRIDE	P60722.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN79193; AAN79193; c0720.
GeneID	1036853.
KEGG	ecc:c0720.
PATRIC	18279479. VBIEscCol75197_0683.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000194321.
KO	K03801.
OMA	DAHPRAD.
ProtClustDB	PRK14342.
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_ECOL6

Accession

Primary (citable) accession number: P60722
Secondary accession number(s): P30976, P77684, Q8XBQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program