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P10507 (MPPB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial-processing peptidase subunit beta

EC=3.4.24.64
Alternative name(s):
Beta-MPP
PEP
Gene names
Name:MAS1
Synonyms:MIF1
Ordered Locus Names:YLR163C
ORF Names:L9632.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves presequences (transit peptides) from mitochondrial protein precursors.

Catalytic activity

Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Heterodimer of alpha and beta subunits.

Subcellular location

Mitochondrion matrix.

Miscellaneous

Present with 1360 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase M16 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAS2P119145EBI-11212,EBI-11205

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Ref.5
Chain21 – 462442Mitochondrial-processing peptidase subunit beta
PRO_0000026784

Sites

Active site731Proton acceptor
Metal binding701Zinc
Metal binding741Zinc
Metal binding1501Zinc

Amino acid modifications

Modified residue2431Phosphoserine Ref.7

Experimental info

Mutagenesis731E → Q: Loss of activity. Ref.8

Secondary structure

......................................................................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10507 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 084CE63C495EDFC4

FASTA46251,084
        10         20         30         40         50         60 
MFSRTASKFR NTRRLLSTIS SQIPGTRTSK LPNGLTIATE YIPNTSSATV GIFVDAGSRA 

        70         80         90        100        110        120 
ENVKNNGTAH FLEHLAFKGT QNRSQQGIEL EIENIGSHLN AYTSRENTVY YAKSLQEDIP 

       130        140        150        160        170        180 
KAVDILSDIL TKSVLDNSAI ERERDVIIRE SEEVDKMYDE VVFDHLHEIT YKDQPLGRTI 

       190        200        210        220        230        240 
LGPIKNIKSI TRTDLKDYIT KNYKGDRMVL AGAGAVDHEK LVQYAQKYFG HVPKSESPVP 

       250        260        270        280        290        300 
LGSPRGPLPV FCRGERFIKE NTLPTTHIAI ALEGVSWSAP DYFVALATQA IVGNWDRAIG 

       310        320        330        340        350        360 
TGTNSPSPLA VAASQNGSLA NSYMSFSTSY ADSGLWGMYI VTDSNEHNVQ LIVNEILKEW 

       370        380        390        400        410        420 
KRIKSGKISD AEVNRAKAQL KAALLLSLDG STAIVEDIGR QVVTTGKRLS PEEVFEQVDK 

       430        440        450        460 
ITKDDIIMWA NYRLQNKPVS MVALGNTSTV PNVSYIEEKL NQ 

« Hide

References

« Hide 'large scale' references
[1]"MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease."
Witte C., Jensen R.E., Yaffe M.P., Schatz G.
EMBO J. 7:1439-1447(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein."
Yang M., Geli V., Oppliger W., Suda K., James P., Schatz G.
J. Biol. Chem. 266:6416-6423(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences."
Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z., Ito A., Deisenhofer J.
Structure 9:615-625(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 21-462 IN COMPLEX WITH ZINC AND SUBSTRATES, MUTAGENESIS OF GLU-73.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07649 Genomic DNA. Translation: CAA30489.1.
U51921 Genomic DNA. Translation: AAB67487.1.
AY693198 Genomic DNA. Translation: AAT93217.1.
BK006945 Genomic DNA. Translation: DAA09485.1.
PIRS00552.
RefSeqNP_013264.1. NM_001182050.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HR6X-ray2.50B/D/F/H21-462[»]
1HR7X-ray2.55B/D/F/H21-462[»]
1HR8X-ray2.70B/D/F/H21-462[»]
1HR9X-ray3.01B/D/F/H21-462[»]
ProteinModelPortalP10507.
SMRP10507. Positions 23-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31436. 20 interactions.
DIPDIP-2402N.
IntActP10507. 14 interactions.
MINTMINT-614379.
STRING4932.YLR163C.

Protein family/group databases

MEROPSM16.003.

Proteomic databases

PaxDbP10507.
PeptideAtlasP10507.
PRIDEP10507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR163C; YLR163C; YLR163C.
GeneID850860.
KEGGsce:YLR163C.

Organism-specific databases

CYGDYLR163c.
SGDS000004153. MAS1.

Phylogenomic databases

eggNOGCOG0612.
GeneTreeENSGT00550000074701.
HOGENOMHOG000242450.
KOK17732.
OMATETTSYY.
OrthoDBEOG7BW0TR.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16673.
YEAST:G3O-32293-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.
SABIO-RKP10507.

Gene expression databases

GenevestigatorP10507.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 2 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10507.
NextBio967179.
PROP10507.

Entry information

Entry nameMPPB_YEAST
AccessionPrimary (citable) accession number: P10507
Secondary accession number(s): D6VYG9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references