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Protein

Octanoyl-[GcvH]:protein N-octanoyltransferase

Gene

lipL

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.UniRule annotation

Catalytic activityi

[Glycine cleavage system H]-N(6)-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N(6)-octanoyl-L-lysine.UniRule annotation

Pathwayi: protein lipoylation via endogenous pathway

This protein is involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481Acyl-thioester intermediateUniRule annotation
Sitei160 – 1601Lowers pKa of active site CysUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-3925-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Octanoyl-[GcvH]:protein N-octanoyltransferaseUniRule annotation (EC:2.3.1.204UniRule annotation)
Alternative name(s):
Octanoyl-[GcvH]:E2 amidotransferaseUniRule annotation
Gene namesi
Name:lipLUniRule annotation
Ordered Locus Names:BH3822
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Octanoyl-[GcvH]:protein N-octanoyltransferasePRO_0000410836Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272558.BH3822.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207Combined sources
Helixi27 – 4115Combined sources
Turni42 – 443Combined sources
Beta strandi49 – 535Combined sources
Beta strandi56 – 627Combined sources
Helixi63 – 664Combined sources
Helixi71 – 8010Combined sources
Beta strandi84 – 907Combined sources
Beta strandi95 – 973Combined sources
Beta strandi101 – 1099Combined sources
Helixi116 – 13015Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi159 – 16911Combined sources
Beta strandi172 – 1809Combined sources
Helixi185 – 20016Combined sources
Helixi214 – 2163Combined sources
Helixi220 – 2245Combined sources
Helixi230 – 24314Combined sources
Helixi255 – 27521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P5IX-ray2.21A2-278[»]
ProteinModelPortaliQ9K6A7.
SMRiQ9K6A7. Positions 12-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9K6A7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 249206BPL/LPL catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the octanoyltransferase LipL family.UniRule annotation
Contains 1 BPL/LPL catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105JGI. Bacteria.
COG0095. LUCA.
HOGENOMiHOG000078071.
KOiK16869.
OMAiCPGDYDL.
OrthoDBiEOG6QG8GV.

Family and domain databases

HAMAPiMF_02119. LipL.
InterProiIPR004143. BPL_LPL_catalytic.
IPR024897. LipL.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9K6A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLLQQHLS QPWRFLDHTS FGPTFQALQS FAYDDTLCTS IGKSQSPPTL
60 70 80 90 100
RAWVHHNTVV LGIQDSRLPQ IKAGIEALKG FQHDVIVRNS GGLAVVLDSG
110 120 130 140 150
ILNLSLVLKE EKGFSIDDGY ELMYELICSM FQDHREQIEA REIVGSYCPG
160 170 180 190 200
SYDLSIDGKK FAGISQRRIR GGVAVQIYLC VSGSGAERAK MIRTFYDKAV
210 220 230 240 250
AGQPTKFVYP RIKPETMASL SELLGQPHNV SDVLLKALMT LQQHGASLLT
260 270
ESLSADEWLL YEQHFARISE RNEKLLAE
Length:278
Mass (Da):31,000
Last modified:October 1, 2000 - v1
Checksum:i5858056515F4FFFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB07541.1.
PIRiF84127.
RefSeqiWP_010899947.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB07541; BAB07541; BAB07541.
KEGGibha:BH3822.
PATRICi18944962. VBIBacHal18977_3979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB07541.1.
PIRiF84127.
RefSeqiWP_010899947.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P5IX-ray2.21A2-278[»]
ProteinModelPortaliQ9K6A7.
SMRiQ9K6A7. Positions 12-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH3822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB07541; BAB07541; BAB07541.
KEGGibha:BH3822.
PATRICi18944962. VBIBacHal18977_3979.

Phylogenomic databases

eggNOGiENOG4105JGI. Bacteria.
COG0095. LUCA.
HOGENOMiHOG000078071.
KOiK16869.
OMAiCPGDYDL.
OrthoDBiEOG6QG8GV.

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-3925-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9K6A7.

Family and domain databases

HAMAPiMF_02119. LipL.
InterProiIPR004143. BPL_LPL_catalytic.
IPR024897. LipL.
[Graphical view]
PfamiPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PROSITEiPS51733. BPL_LPL_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
  2. "Crystal structure of a hypothetical protein from Bacillus halodurans: Pfam-PF03099."
    New York structural genomix research consortium (NYSGXRC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-278.

Entry informationi

Entry nameiLIPL_BACHD
AccessioniPrimary (citable) accession number: Q9K6A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: October 1, 2000
Last modified: January 20, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction proceeds via a thioester-linked acyl-enzyme intermediate.UniRule annotation

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.