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P60722 (LIPB_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence similarities

Belongs to the LipB family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Inferred from electronic annotation. Source: InterPro

lipoate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipoyl(octanoyl) transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

octanoyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Octanoyltransferase HAMAP-Rule MF_00013
PRO_0000062836

Regions

Region71 – 788Substrate binding By similarity
Region138 – 1403Substrate binding By similarity
Region151 – 1533Substrate binding By similarity

Sites

Active site1691Acyl-thioester intermediate By similarity
Site1351Lowers pKa of active site Cys By similarity

Sequences

Sequence LengthMass (Da)Tools
P60722 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 56EE2BB105F99EAD

FASTA21323,883
        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 

« Hide

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.
RefSeqNP_752650.1. NC_004431.1.

3D structure databases

ProteinModelPortalP60722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0720.

Proteomic databases

PRIDEP60722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN79193; AAN79193; c0720.
GeneID1036853.
KEGGecc:c0720.
PATRIC18279479. VBIEscCol75197_0683.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000194321.
KOK03801.
OMAIWLVEHD.
OrthoDBEOG6XM7G6.

Enzyme and pathway databases

BioCycECOL199310:C0720-MONOMER.
UniPathwayUPA00538; UER00592.

Family and domain databases

HAMAPMF_00013. LipB.
InterProIPR004143. BPL_LipA_LipB.
IPR000544. Octanoyltransferase.
IPR020605. Octanoyltransferase_CS.
[Graphical view]
PfamPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PIRSFPIRSF016262. LPLase. 1 hit.
TIGRFAMsTIGR00214. lipB. 1 hit.
PROSITEPS01313. LIPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPB_ECOL6
AccessionPrimary (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: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways