SAM50_YEAST
ID SAM50_YEAST Reviewed; 484 AA.
AC P53969; D6W1F2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Sorting assembly machinery 50 kDa subunit;
DE AltName: Full=TOB complex 55 kDa subunit;
GN Name=SAM50; Synonyms=TOB55; OrderedLocusNames=YNL026W; ORFNames=N2802;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE SAM COMPLEX.
RX PubMed=14570913; DOI=10.1074/jbc.c300442200;
RA Kozjak V., Wiedemann N., Milenkovic D., Lohaus C., Meyer H.E., Guiard B.,
RA Meisinger C., Pfanner N.;
RT "An essential role of Sam50 in the protein sorting and assembly machinery
RT of the mitochondrial outer membrane.";
RL J. Biol. Chem. 278:48520-48523(2003).
RN [4]
RP IDENTIFICATION IN THE SAM COMPLEX.
RX PubMed=14685243; DOI=10.1038/nature02208;
RA Paschen S.A., Waizenegger T., Stan T., Preuss M., Cyrklaff M., Hell K.,
RA Rapaport D., Neupert W.;
RT "Evolutionary conservation of biogenesis of beta-barrel membrane
RT proteins.";
RL Nature 426:862-866(2003).
RN [5]
RP IDENTIFICATION IN THE SAM COMPLEX.
RX PubMed=15590639; DOI=10.1074/jbc.m411510200;
RA Habib S.J., Waizenegger T., Lech M., Neupert W., Rapaport D.;
RT "Assembly of the TOB complex of mitochondria.";
RL J. Biol. Chem. 280:6434-6440(2005).
CC -!- FUNCTION: Component of the mitochondrial outer membrane sorting
CC assembly machinery (SAM or TOB) complex, which is required for the
CC sorting of proteins with complicated topology, such as beta-barrel
CC proteins, to the mitochondrial outer membrane after import by the TOM
CC complex. {ECO:0000269|PubMed:14570913}.
CC -!- SUBUNIT: Component of the mitochondrial outer membrane sorting assembly
CC machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37
CC and SAM50 (PubMed:14570913, PubMed:14685243, PubMed:15590639).
CC Associates with the mitochondrial contact site and cristae organizing
CC system (MICOS) complex (also known as MINOS or MitOS complex) (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:14570913,
CC ECO:0000269|PubMed:14685243, ECO:0000269|PubMed:15590639}.
CC -!- INTERACTION:
CC P53969; P18409: MDM10; NbExp=4; IntAct=EBI-28646, EBI-10580;
CC P53969; P14693: SAM35; NbExp=8; IntAct=EBI-28646, EBI-24602;
CC P53969; P50110: SAM37; NbExp=5; IntAct=EBI-28646, EBI-2347180;
CC P53969; P49334: TOM22; NbExp=6; IntAct=EBI-28646, EBI-12527;
CC P53969; P23644: TOM40; NbExp=4; IntAct=EBI-28646, EBI-12539;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14570913}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:14685243}.
CC -!- DOMAIN: Its C-terminal part seems to contain many membrane-spanning
CC sided beta-sheets, that have the potential to adopt a transmembrane
CC beta-barrel type structure. {ECO:0000305|PubMed:14685243}.
CC -!- SIMILARITY: Belongs to the SAM50/omp85 family. {ECO:0000305}.
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DR EMBL; Z71302; CAA95888.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10518.1; -; Genomic_DNA.
DR PIR; S62938; S62938.
DR RefSeq; NP_014372.1; NM_001182865.1.
DR PDB; 7E4H; EM; 3.01 A; A=2-484.
DR PDB; 7E4I; EM; 3.05 A; A=2-484.
DR PDBsum; 7E4H; -.
DR PDBsum; 7E4I; -.
DR AlphaFoldDB; P53969; -.
DR SMR; P53969; -.
DR BioGRID; 35800; 387.
DR ComplexPortal; CPX-1744; Mitochondrial sorting and assembly machinery complex.
DR IntAct; P53969; 14.
DR MINT; P53969; -.
DR STRING; 4932.YNL026W; -.
DR TCDB; 1.B.33.3.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR MaxQB; P53969; -.
DR PaxDb; P53969; -.
DR PRIDE; P53969; -.
DR EnsemblFungi; YNL026W_mRNA; YNL026W; YNL026W.
DR GeneID; 855705; -.
DR KEGG; sce:YNL026W; -.
DR SGD; S000004971; SAM50.
DR VEuPathDB; FungiDB:YNL026W; -.
DR eggNOG; KOG2602; Eukaryota.
DR GeneTree; ENSGT00390000011355; -.
DR HOGENOM; CLU_014798_3_1_1; -.
DR InParanoid; P53969; -.
DR OMA; HHIALNA; -.
DR BioCyc; YEAST:G3O-33064-MON; -.
DR PRO; PR:P53969; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53969; protein.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0001401; C:SAM complex; IDA:SGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IDA:ComplexPortal.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport.
FT CHAIN 1..484
FT /note="Sorting assembly machinery 50 kDa subunit"
FT /id="PRO_0000215943"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 156..181
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 184..196
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 203..216
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 235..251
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 271..285
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 310..322
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 329..342
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 384..397
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 403..420
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 454..466
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:7E4H"
SQ SEQUENCE 484 AA; 54406 MW; 651A1FE08A1F1845 CRC64;
MTSSSGVDNE ISLDSPMPIF NESSTLKPIR VAGVVTTGTD HIDPSVLQAY LDDTIMKSIT
LGQLVKNADV LNKRLCQHHI ALNAKQSFHF QGNTYISDEK ETHDVVPLME VVSQLDILPP
KTFTAKTGTN FGNDNDAEAY LQFEKLIDKK YLKLPTRVNL EILRGTKIHS SFLFNSYSSL
SPQSILNLKV FSQFYNWNTN KGLDIGQRGA RLSLRYEPLF LHKLLHNPHS NESPTLFHEW
FLETCWRSTK ICSQGTSAPY MYSGTMLSQA GDQLRTILGH TFVLDKRDHI MCPTKGSMLK
WSNELSPGKH LKTQLELNSV KSWMNDDFIT FSTTIKTGYL KNLSSQQSLP VHICDKFQSG
GPSDIRGFQT FGLGPRDLYD AVGGDAFVSY GLSVFSRLPW KKVEKSNFRL HWFFNGGKLV
NHDNTSLGNC IGQLSKEHST STGIGLVLRH PMARFELNFT LPITAHENDL IRKGFQFGLG
LAFL
