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Protein

Sorting assembly machinery 50 kDa subunit

Gene

SAM50

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.1 Publication

GO - Molecular functioni

  1. protein channel activity Source: SGD

GO - Biological processi

  1. protein complex assembly Source: SGD
  2. protein import into mitochondrial outer membrane Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33064-MONOMER.
ReactomeiREACT_189012. Mitochondrial protein import.

Protein family/group databases

TCDBi1.B.33.3.1. the outer membrane protein insertion porin (bam complex) (ompip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting assembly machinery 50 kDa subunit
Alternative name(s):
TOB complex 55 kDa subunit
Gene namesi
Name:SAM50
Synonyms:TOB55
Ordered Locus Names:YNL026W
ORF Names:N2802
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL026w.
SGDiS000004971. SAM50.

Subcellular locationi

GO - Cellular componenti

  1. integral component of mitochondrial outer membrane Source: SGD
  2. mitochondrial outer membrane Source: Reactome
  3. mitochondrial sorting and assembly machinery complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Sorting assembly machinery 50 kDa subunitPRO_0000215943Add
BLAST

Proteomic databases

MaxQBiP53969.
PaxDbiP53969.
PeptideAtlasiP53969.

Expressioni

Gene expression databases

GenevestigatoriP53969.

Interactioni

Subunit structurei

Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37 and SAM50. Associates with the mitochondrial inner membrane MINOS/MitOS complex (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM10P184094EBI-28646,EBI-10580
SAM35P146938EBI-28646,EBI-24602
SAM37P501105EBI-28646,EBI-2347180
TOM22P493346EBI-28646,EBI-12527
TOM40P236444EBI-28646,EBI-12539

Protein-protein interaction databases

BioGridi35800. 14 interactions.
IntActiP53969. 14 interactions.
MINTiMINT-4791160.
STRINGi4932.YNL026W.

Structurei

3D structure databases

ProteinModelPortaliP53969.
SMRiP53969. Positions 225-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure.

Sequence similaritiesi

Belongs to the SAM50/omp85 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiCOG4775.
GeneTreeiENSGT00390000011355.
HOGENOMiHOG000170308.
InParanoidiP53969.
KOiK07277.
OrthoDBiEOG7W9S4R.

Family and domain databases

InterProiIPR000184. Bac_surfAg_D15.
[Graphical view]
PfamiPF01103. Bac_surface_Ag. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53969-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSSSGVDNE ISLDSPMPIF NESSTLKPIR VAGVVTTGTD HIDPSVLQAY
60 70 80 90 100
LDDTIMKSIT LGQLVKNADV LNKRLCQHHI ALNAKQSFHF QGNTYISDEK
110 120 130 140 150
ETHDVVPLME VVSQLDILPP KTFTAKTGTN FGNDNDAEAY LQFEKLIDKK
160 170 180 190 200
YLKLPTRVNL EILRGTKIHS SFLFNSYSSL SPQSILNLKV FSQFYNWNTN
210 220 230 240 250
KGLDIGQRGA RLSLRYEPLF LHKLLHNPHS NESPTLFHEW FLETCWRSTK
260 270 280 290 300
ICSQGTSAPY MYSGTMLSQA GDQLRTILGH TFVLDKRDHI MCPTKGSMLK
310 320 330 340 350
WSNELSPGKH LKTQLELNSV KSWMNDDFIT FSTTIKTGYL KNLSSQQSLP
360 370 380 390 400
VHICDKFQSG GPSDIRGFQT FGLGPRDLYD AVGGDAFVSY GLSVFSRLPW
410 420 430 440 450
KKVEKSNFRL HWFFNGGKLV NHDNTSLGNC IGQLSKEHST STGIGLVLRH
460 470 480
PMARFELNFT LPITAHENDL IRKGFQFGLG LAFL
Length:484
Mass (Da):54,406
Last modified:October 1, 1996 - v1
Checksum:i651A1FE08A1F1845
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71302 Genomic DNA. Translation: CAA95888.1.
BK006947 Genomic DNA. Translation: DAA10518.1.
PIRiS62938.
RefSeqiNP_014372.1. NM_001182865.1.

Genome annotation databases

EnsemblFungiiYNL026W; YNL026W; YNL026W.
GeneIDi855705.
KEGGisce:YNL026W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71302 Genomic DNA. Translation: CAA95888.1.
BK006947 Genomic DNA. Translation: DAA10518.1.
PIRiS62938.
RefSeqiNP_014372.1. NM_001182865.1.

3D structure databases

ProteinModelPortaliP53969.
SMRiP53969. Positions 225-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35800. 14 interactions.
IntActiP53969. 14 interactions.
MINTiMINT-4791160.
STRINGi4932.YNL026W.

Protein family/group databases

TCDBi1.B.33.3.1. the outer membrane protein insertion porin (bam complex) (ompip) family.

Proteomic databases

MaxQBiP53969.
PaxDbiP53969.
PeptideAtlasiP53969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL026W; YNL026W; YNL026W.
GeneIDi855705.
KEGGisce:YNL026W.

Organism-specific databases

CYGDiYNL026w.
SGDiS000004971. SAM50.

Phylogenomic databases

eggNOGiCOG4775.
GeneTreeiENSGT00390000011355.
HOGENOMiHOG000170308.
InParanoidiP53969.
KOiK07277.
OrthoDBiEOG7W9S4R.

Enzyme and pathway databases

BioCyciYEAST:G3O-33064-MONOMER.
ReactomeiREACT_189012. Mitochondrial protein import.

Miscellaneous databases

NextBioi980043.
PROiP53969.

Gene expression databases

GenevestigatoriP53969.

Family and domain databases

InterProiIPR000184. Bac_surfAg_D15.
[Graphical view]
PfamiPF01103. Bac_surface_Ag. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane."
    Kozjak V., Wiedemann N., Milenkovic D., Lohaus C., Meyer H.E., Guiard B., Meisinger C., Pfanner N.
    J. Biol. Chem. 278:48520-48523(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SAM COMPLEX.
  4. "Evolutionary conservation of biogenesis of beta-barrel membrane proteins."
    Paschen S.A., Waizenegger T., Stan T., Preuss M., Cyrklaff M., Hell K., Rapaport D., Neupert W.
    Nature 426:862-866(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SAM COMPLEX.
  5. Cited for: IDENTIFICATION IN THE SAM COMPLEX.

Entry informationi

Entry nameiSAM50_YEAST
AccessioniPrimary (citable) accession number: P53969
Secondary accession number(s): D6W1F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

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 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.