Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q4L4T8

- LIPA_STAHJ

UniProt

Q4L4T8 - LIPA_STAHJ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lipoyl synthase

Gene

lipA

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi46 – 461Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi52 – 521Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi68 – 681Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-2085-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
Ordered Locus Names:SH2028
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Lipoyl synthasePRO_0000325313Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi279808.SH2028.

Structurei

3D structure databases

ProteinModelPortaliQ4L4T8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OrthoDBiEOG6038ZS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4L4T8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATKNEEILR KPDWLKIKLN TNENYIGLKK MMREKNLHTV CEEAKCPNIH
60 70 80 90 100
ECWGARRTAT FMILGAVCTR ACRFCAVKTG LPNELDLNEP ERVAESVELM
110 120 130 140 150
NLKHVVITAV ARDDLRDAGS NVYAETVRKV RERNPFTTIE ILPSDMGGDY
160 170 180 190 200
EALETLMASK PDILNHNIET VRRLTPRVRA RATYERTLEF LRRSKELQPD
210 220 230 240 250
IPTKSSLMVG LGETIEEIYE TMDDLRANDV DILTIGQYLQ PSRKHLKVEK
260 270 280 290 300
YYTPLEFGKL RKVAMDKGFK HCEAGPMVRS SYHADEQVNE AAKEKHRLGE

EKLQQN
Length:306
Mass (Da):35,161
Last modified:March 18, 2008 - v2
Checksum:i1F3B0F228EE955F1
GO

Sequence cautioni

The sequence BAE05337.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05337.1. Different initiation.
RefSeqiYP_253943.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05337; BAE05337; SH2028.
GeneIDi3482120.
KEGGisha:SH2028.
PATRICi19620157. VBIStaHae67511_1999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05337.1 . Different initiation.
RefSeqi YP_253943.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L4T8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH2028.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE05337 ; BAE05337 ; SH2028 .
GeneIDi 3482120.
KEGGi sha:SH2028.
PATRICi 19620157. VBIStaHae67511_1999.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

BioCyci SHAE279808:GJX7-2085-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiLIPA_STAHJ
AccessioniPrimary (citable) accession number: Q4L4T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 26, 2014
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3