ID RT27_YEAST Reviewed; 110 AA. AC P53305; D6VUZ8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Small ribosomal subunit protein mS33 {ECO:0000303|PubMed:28154081}; DE AltName: Full=Mitochondrial 37S ribosomal protein S27; GN Name=RSM27; OrderedLocusNames=YGR215W; 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 [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9290212; RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y; RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.; RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae RT chromosome VII."; RL Yeast 13:1077-1090(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11278769; DOI=10.1074/jbc.m010864200; RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A., RA Jacquier A.; RT "Identification of 12 new yeast mitochondrial ribosomal proteins including RT 6 that have no prokaryotic homologues."; RL J. Biol. Chem. 276:15861-15867(2001). RN [6] RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x; RA Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.; RT "Tag-mediated isolation of yeast mitochondrial ribosome and mass RT spectrometric identification of its new components."; RL Eur. J. Biochem. 269:5203-5214(2002). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=25609543; DOI=10.1038/ncomms7019; RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.; RT "Organization of the mitochondrial translation machinery studied in situ by RT cryoelectron tomography."; RL Nat. Commun. 6:6019-6019(2015). RN [11] RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), AND SUBUNIT. RX PubMed=28154081; DOI=10.1126/science.aal2415; RA Desai N., Brown A., Amunts A., Ramakrishnan V.; RT "The structure of the yeast mitochondrial ribosome."; RL Science 355:528-531(2017). CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a CC dedicated translation machinery responsible for the synthesis of CC mitochondrial genome-encoded proteins, including at least some of the CC essential transmembrane subunits of the mitochondrial respiratory CC chain. The mitoribosomes are attached to the mitochondrial inner CC membrane and translation products are cotranslationally integrated into CC the membrane. {ECO:0000305|PubMed:25609543, CC ECO:0000305|PubMed:28154081}. CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt- CC SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) CC and a large (54S) subunit. The 37S small subunit contains a 15S CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. CC {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:12392552, CC ECO:0000269|PubMed:28154081}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278769, CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and CC spatially aligned with the membrane insertion machinery through two CC distinct membrane contact sites, formed by the 21S rRNA expansion CC segment 96-ES1 and the inner membrane protein MBA1. CC {ECO:0000269|PubMed:25609543}. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mS33 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z73000; CAA97242.1; -; Genomic_DNA. DR EMBL; AY558379; AAS56705.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08309.1; -; Genomic_DNA. DR PIR; S64538; S64538. DR RefSeq; NP_011731.3; NM_001181344.3. DR PDB; 5MRC; EM; 3.25 A; XX=1-96. DR PDB; 5MRE; EM; 3.75 A; XX=1-96. DR PDB; 5MRF; EM; 4.97 A; XX=1-96. DR PDB; 8D8K; EM; 3.13 A; X=1-110. DR PDB; 8D8L; EM; 2.60 A; X=1-110. DR PDBsum; 5MRC; -. DR PDBsum; 5MRE; -. DR PDBsum; 5MRF; -. DR PDBsum; 8D8K; -. DR PDBsum; 8D8L; -. DR AlphaFoldDB; P53305; -. DR EMDB; EMD-3551; -. DR EMDB; EMD-3552; -. DR EMDB; EMD-3553; -. DR SMR; P53305; -. DR BioGRID; 33468; 131. DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit. DR DIP; DIP-5606N; -. DR IntAct; P53305; 5. DR MINT; P53305; -. DR STRING; 4932.YGR215W; -. DR MaxQB; P53305; -. DR PaxDb; 4932-YGR215W; -. DR PeptideAtlas; P53305; -. DR EnsemblFungi; YGR215W_mRNA; YGR215W; YGR215W. DR GeneID; 853129; -. DR KEGG; sce:YGR215W; -. DR AGR; SGD:S000003447; -. DR SGD; S000003447; RSM27. DR VEuPathDB; FungiDB:YGR215W; -. DR eggNOG; KOG4844; Eukaryota. DR HOGENOM; CLU_150777_0_0_1; -. DR InParanoid; P53305; -. DR OMA; MKAQCQV; -. DR OrthoDB; 1408578at2759; -. DR BioCyc; YEAST:G3O-30897-MONOMER; -. DR BioGRID-ORCS; 853129; 0 hits in 10 CRISPR screens. DR PRO; PR:P53305; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P53305; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR InterPro; IPR013219; Ribosomal_mS33. DR PANTHER; PTHR13362:SF2; 28S RIBOSOMAL PROTEIN S33, MITOCHONDRIAL; 1. DR PANTHER; PTHR13362; MITOCHONDRIAL RIBOSOMAL PROTEIN S33; 1. DR Pfam; PF08293; MRP-S33; 1. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..110 FT /note="Small ribosomal subunit protein mS33" FT /id="PRO_0000202847" FT REGION 84..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 5..19 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 32..36 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 41..45 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 56..62 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:8D8K" FT HELIX 71..85 FT /evidence="ECO:0007829|PDB:8D8L" SQ SEQUENCE 110 AA; 12393 MW; 05008CA4F5D09004 CRC64; MNVPKARLLK VAELSAKIFD QNFNPSGIRT GSKILNERLK GPSVASYYGN PDILKFRHLK TLYPDIEFVD LEEQYRLSMV EAKKRRGKGA PKKMKKDAAA TAKGKGKKKK //