A9IH67 (LIPB_BORPD) 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:	Bpet4804

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella petrii

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_1000089439
Regions
	Region	66 – 73	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)
	A9IH67 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: AEFC8E73E7742AB1	FASTA	213	22,757
	10 20 30 40 50 60 MIKWLTRPAD YAPVWQDMRA FTAGRGAATP DEVWLCEHAP VYTLGQAGKP EHLLNPGAIP 70 80 90 100 110 120 VVMCDRGGQV TYHGPGQVVA YTLFDLRRAG LFVREYVRLL EDAAIGTLDD FGVPGACRKP 130 140 150 160 170 180 GAPGVYVPLG PAGELAKIAA LGIKIRNGYA YHGVALNVDM DLSPFLGINP CGYEGLVTVD 190 200 210 MAACGVRRDL VDVGQRLAER LLAAMPEPAG ATR

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP45156.1.
RefSeq	YP_001633423.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IH67.
ModBase	Search...
Protein-protein interaction databases
STRING	340100.Bpet4804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAP45156; CAP45156; Bpet4804.
GeneID	5820333.
KEGG	bpt:Bpet4804.
PATRIC	21171214. VBIBorPet31633_4833.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0321.
HOGENOM	HOG000194321.
KO	K03801.
OMA	DAHPRAD.
ProtClustDB	PRK14349.
Enzyme and pathway databases
BioCyc	BPET340100:GJBO-4875-MONOMER.
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_BORPD

Accession

Primary (citable) accession number: A9IH67

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program