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3.A.28.1.1
The mitochondrial chaperone (Wagener et al., 2011). Some proteins require completion of folding before translocation across a membrane into another cellular compartment, but the permeability barrier of the membrane should not be compromised. Kater et al. 2020 presented the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex (TC# 3.D.3). Bcs1 assembles into an exclusively heptameric homo-oligomer, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, Kater et al. 2020 proposed an airlock-like translocation mechanism for folded Rip1.

Accession Number:P32839
Protein Name:Mitochondrial chaperone BCS1
Length:456
Molecular Weight:51107.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Mitochondrion inner membrane1 / Single-pass membrane protein2
Substrate

Cross database links:

Genevestigator: P32839
eggNOG: fuNOG06383
HEGENOM: HBG521794
Entrez Gene ID: 851981   
Pfam: PF00004    PF08740   
KEGG: sce:YDR375C   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005743 C:mitochondrial inner membrane
GO:0005524 F:ATP binding
GO:0017111 F:nucleoside-triphosphatase activity
GO:0009060 P:aerobic respiration
GO:0051131 P:chaperone-mediated protein complex assembly
GO:0007005 P:mitochondrion organization

References (5)

[1] “BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae.”  Nobrega F.G.et.al.   1327750
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.”  Jacq C.et.al.   9169867
[3] “Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria.”  Foelsch H.et.al.   8599931
[4] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[5] “Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.”  Chi A.et.al.   17287358
Structure:
6SH3   6SH4   6SH5     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSDKPIDIQY DKQATPNLSG VITPPTNETG NDSVREKLSK LVGDAMSNNP YFAAGGGLMI 
61:	LGTGLAVARS GIIKASRVLY RQMIVDLEIQ SKDKSYAWFL TWMAKHPQRV SRHLSVRTNY 
121:	IQHDNGSVST KFSLVPGPGN HWIRYKGAFI LIKRERSAKM IDIANGSPFE TVTLTTLYRD 
181:	KHLFDDILNE AKDIALKTTE GKTVIYTSFG PEWRKFGQPK AKRMLPSVIL DSGIKEGILD 
241:	DVYDFMKNGK WYSDRGIPYR RGYLLYGPPG SGKTSFIQAL AGELDYNICI LNLSENNLTD 
301:	DRLNHLMNNM PERSILLLED IDAAFNKRSQ TGEQGFHSSV TFSGLLNALD GVTSSEETIT 
361:	FMTTNHPEKL DAAIMRPGRI DYKVFVGNAT PYQVEKMFMK FYPGETDICK KFVNSVKELD 
421:	ITVSTAQLQG LFVMNKDAPH DALKMVSSLR NANHIF