Q0SHK6 (LIPB_RHOSR) 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:	RHA1_ro01153

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus › Rhodococcus jostii

Protein attributes

Sequence length	258 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 – 258	258	Octanoyltransferase HAMAP-Rule MF_00013		PRO_0000321664
Regions
	Region	80 – 87	8	Substrate binding By similarity
	Region	156 – 158	3	Substrate binding By similarity
	Region	169 – 171	3	Substrate binding By similarity
Sites
	Active site	187	1	Acyl-thioester intermediate By similarity
	Site	153	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0SHK6 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: A46022AB869156D5	FASTA	258	27,561
	10 20 30 40 50 60 MSSATQSARF SPSPISVEHL GTIGYVDAWD RQRELAAERA ENVGTDTLLL LEHPAVYTAG 70 80 90 100 110 120 RRTEPEDRPT DGTPVIDVDR GGKITWHGPG QLVGYPIVKL AEPVDVVRYV RRLEQALITV 130 140 150 160 170 180 CTDLGIVCGR VDGRSGVWLP ASFDNGQWLP ERKVAAIGVR VQRGVALHGF SLNCNSVLTG 190 200 210 220 230 240 FDAIIPCGIR DAGVTSLSRE LGRDVTVEEV TPAVTAAVVA ALDGELPVTE HDIERVTFDS 250 AAAGTTSSAP TFTTVQYG

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG92980.1.
RefSeq	YP_701138.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0SHK6.
SMR	Q0SHK6. Positions 7-227.
ModBase	Search...
Protein-protein interaction databases
STRING	101510.RHA1_ro01153.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG92980; ABG92980; RHA1_ro01153.
GeneID	4219760.
KEGG	rha:RHA1_ro01153.
PATRIC	23201121. VBIRhoJos26306_1180.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0321.
HOGENOM	HOG000194322.
KO	K03801.
OMA	KEYVYRI.
ProtClustDB	PRK14345.
Enzyme and pathway databases
BioCyc	RJOS101510:GJJ1-1152-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_RHOSR

Accession

Primary (citable) accession number: Q0SHK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program