Q8YC54 (LIPB_BRUME) 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:	BMEII0678

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	264 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 By similarity 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 – 264	264	Octanoyltransferase HAMAP-Rule MF_00013		PRO_0000062818
Regions
	Region	113 – 120	8	Substrate binding By similarity
	Region	193 – 195	3	Substrate binding By similarity
	Region	206 – 208	3	Substrate binding By similarity
Sites
	Active site	224	1	Acyl-thioester intermediate By similarity
	Site	190	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YC54 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 058A451FA3271D0D	FASTA	264	29,301
	10 20 30 40 50 60 MPTGKLRQKP PYAAIMTNSP VTPSTETQQP KRYARFLPQE ADAPPVEWLI AEGLTDYEEA 70 80 90 100 110 120 LAFMEARVQA IREGTASELV WLVEHPPLYT AGTSANAEDL LTPDRFPVFN TGRGGEYTYH 130 140 150 160 170 180 GPGQRVAYVM LDLKRRREDV RAFVASLEQW IIETLAAFNI KGERREDRVG VWVVRPEKPR 190 200 210 220 230 240 LADGSMCEDK IAAIGIRLRR WVSFHGIAIN VEPDLSHYGG IVPCGISEHG VTSLVDLGLP 250 260 VTMGDVDVAL GKAFESVFGP RQTK

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008918 Genomic DNA. Translation: AAL53920.1.
PIR	AE3594.
RefSeq	NP_541656.1. NC_003318.1.
3D structure databases
ProteinModelPortal	Q8YC54.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEII0678.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL53920; AAL53920; BMEII0678.
GeneID	1198450.
KEGG	bme:BMEII0678.
PATRIC	17799718. VBIBruMel146950_2195.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000194320.
KO	K03801.
OMA	KEYVYRI.
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_BRUME

Accession

Primary (citable) accession number: Q8YC54

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program