ID RT05_YEAST Reviewed; 307 AA. AC P33759; D6VQP7; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Small ribosomal subunit protein uS5m {ECO:0000303|PubMed:28154081}; DE AltName: Full=37S ribosomal protein S5, mitochondrial; DE Flags: Precursor; GN Name=MRPS5; OrderedLocusNames=YBR251W; ORFNames=YBR1704; 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=8256522; DOI=10.1002/yea.320091014; RA Doignon F., Biteau N., Aigle M., Crouzet M.; RT "The complete sequence of a 6794 bp segment located on the right arm of RT chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in RT a yeast."; RL Yeast 9:1131-1137(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). 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 IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND RP 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 [5] 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 [6] 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 [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(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 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 [10] 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 uS3m, uS4m and uS5m form the narrow entry site of the mRNA channel. CC {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:12392552, CC ECO:0000269|PubMed:28154081}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the CC mitochondrial inner membrane and spatially aligned with the membrane CC insertion machinery through two distinct membrane contact sites, formed CC by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein CC MBA1. {ECO:0000269|PubMed:25609543}. CC -!- MISCELLANEOUS: Present with 6680 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family. CC {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; L20296; AAA65610.1; -; Genomic_DNA. DR EMBL; Z36120; CAA85214.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07367.1; -; Genomic_DNA. DR PIR; S38374; S38374. DR RefSeq; NP_009810.3; NM_001178599.3. DR PDB; 5MRC; EM; 3.25 A; EE=14-306. DR PDB; 5MRE; EM; 3.75 A; EE=14-306. DR PDB; 5MRF; EM; 4.97 A; EE=14-306. DR PDB; 8D8J; EM; 3.80 A; E=1-307. DR PDB; 8D8K; EM; 3.13 A; E=1-307. DR PDB; 8D8L; EM; 2.60 A; E=1-307. DR PDBsum; 5MRC; -. DR PDBsum; 5MRE; -. DR PDBsum; 5MRF; -. DR PDBsum; 8D8J; -. DR PDBsum; 8D8K; -. DR PDBsum; 8D8L; -. DR AlphaFoldDB; P33759; -. DR EMDB; EMD-3551; -. DR EMDB; EMD-3552; -. DR EMDB; EMD-3553; -. DR SMR; P33759; -. DR BioGRID; 32946; 174. DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit. DR DIP; DIP-2869N; -. DR IntAct; P33759; 44. DR MINT; P33759; -. DR STRING; 4932.YBR251W; -. DR MaxQB; P33759; -. DR PaxDb; 4932-YBR251W; -. DR PeptideAtlas; P33759; -. DR EnsemblFungi; YBR251W_mRNA; YBR251W; YBR251W. DR GeneID; 852553; -. DR KEGG; sce:YBR251W; -. DR AGR; SGD:S000000455; -. DR SGD; S000000455; MRPS5. DR VEuPathDB; FungiDB:YBR251W; -. DR eggNOG; KOG2646; Eukaryota. DR GeneTree; ENSGT00390000001878; -. DR HOGENOM; CLU_037994_0_0_1; -. DR InParanoid; P33759; -. DR OMA; YWDYKPG; -. DR OrthoDB; 1407097at2759; -. DR BioCyc; YEAST:G3O-29177-MONOMER; -. DR BioGRID-ORCS; 852553; 5 hits in 10 CRISPR screens. DR PRO; PR:P33759; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P33759; 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:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR000851; Ribosomal_uS5. DR InterPro; IPR005324; Ribosomal_uS5_C. DR InterPro; IPR013810; Ribosomal_uS5_N. DR InterPro; IPR018192; Ribosomal_uS5_N_CS. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1. DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Transit peptide. FT TRANSIT 1..13 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 14..307 FT /note="Small ribosomal subunit protein uS5m" FT /id="PRO_0000131688" FT DOMAIN 144..208 FT /note="S5 DRBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268" FT HELIX 18..22 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 67..69 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 113..115 FT /evidence="ECO:0007829|PDB:8D8K" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 145..158 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 161..173 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 175..188 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 190..203 FT /evidence="ECO:0007829|PDB:8D8L" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 227..233 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 244..253 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 258..264 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 268..281 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 286..293 FT /evidence="ECO:0007829|PDB:8D8L" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:8D8L" FT HELIX 300..304 FT /evidence="ECO:0007829|PDB:8D8L" SQ SEQUENCE 307 AA; 34883 MW; 7A7BC49A4D414FC1 CRC64; MFKRQLSTSV RYLQHYDESL LSRYYPESLL KSIKLAQQTI PEDTKFRVSR NVEFAPPYLD DFTKIHPFWD YKPGMPHLHA QEENNNFSIF RWDQVQQPLP GEGNILPPGV SLPNDGGRKS KSADVAAGLH KQTGVDPDYI TRKLTMKPLV MKRVSNQTGK GKIASFYALV VVGDKNGMVG LGEGKSREEM SKAIFKAHWD AVRNLKEIPR YENRTIYGDI DFRYHGVKLH LRSAKPGFGL RVNHVIFEIC ECAGIKDLSG KVYKSRNDMN IAKGTIEAFT KAQKTLDEVA LGRGKKLVDV RKVYYSS //