ID   RLA2_RHOGU              Reviewed;         110 AA.
AC   Q96UQ7;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=60S acidic ribosomal protein P2;
DE   AltName: Full=Acyl carrier protein;
OS   Rhodotorula glutinis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5535 {ECO:0000312|EMBL:AAL30745.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PHOSPHOPANTETHEINYLATION AT SER-59, MUTAGENESIS
RP   OF SER-12; SER-17; SER-19; SER-40; SER-59; SER-64; SER-67 AND SER-100, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12869567; DOI=10.1074/jbc.m305052200;
RA   Raychaudhuri S., Rajasekharan R.;
RT   "Nonorganellar acyl carrier protein from oleaginous yeast is a homologue of
RT   ribosomal protein P2.";
RL   J. Biol. Chem. 278:37648-37657(2003).
RN   [2] {ECO:0000305}
RP   SUBUNIT.
RX   PubMed=11139581; DOI=10.1074/jbc.m009550200;
RA   Gangar A., Karande A.A., Rajasekharan R.;
RT   "Isolation and localization of a cytosolic 10 S triacylglycerol
RT   biosynthetic multienzyme complex from oleaginous yeast.";
RL   J. Biol. Chem. 276:10290-10298(2001).
CC   -!- FUNCTION: Probable bifunctional protein. The phosphorylated protein
CC       plays an important role in the elongation step of protein synthesis (By
CC       similarity). The phosphopantetheinylated protein acts as an acyl
CC       carrier protein. {ECO:0000250}.
CC   -!- SUBUNIT: The phosphorylated form is part of the ribosomal stalk
CC       involved in the interaction of the elongation factors with the ribosome
CC       during protein synthesis (By similarity). The phosphopantetheinylated
CC       form is part of the 10S triacylglycerol biosynthetic complex involved
CC       in de novo fatty acid biosynthesis. {ECO:0000250,
CC       ECO:0000269|PubMed:11139581}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       by acpS. This modification is essential for activity because fatty
CC       acids are bound in thioester linkage to the sulfhydryl of the
CC       prosthetic group. {ECO:0000269|PubMed:12869567}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF434667; AAL30745.1; -; mRNA.
DR   AlphaFoldDB; Q96UQ7; -.
DR   SMR; Q96UQ7; -.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR   GO; GO:0000036; F:acyl carrier activity; IDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR   GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; NAS:UniProtKB.
DR   CDD; cd05833; Ribosomal_P2; 1.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR   InterPro; IPR044076; Ribosomal_P2.
DR   PANTHER; PTHR21141; PTHR21141; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..110
FT                   /note="60S acidic ribosomal protein P2"
FT                   /id="PRO_0000157680"
FT   REGION          62..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="O-(pantetheine 4'-phosphoryl)serine; in acyl carrier
FT                   protein form"
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MOD_RES         100
FT                   /note="Phosphoserine; in ribosomal stalk form"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         12
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         17
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         19
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         40
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         59
FT                   /note="S->A: Abolishes acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         64
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         67
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
FT   MUTAGEN         100
FT                   /note="S->A: No change in acylation capacity."
FT                   /evidence="ECO:0000269|PubMed:12869567"
SQ   SEQUENCE   110 AA;  11098 MW;  14697B729910C781 CRC64;
     MKHVAAYLLL VSAGNTSPSA EDVKKVLAAA DIQADEERLS VLIKELEGKD VNEVIAEGSK
     KLASVPSGGA APAAAAGGAA AGGAAEEKAE DKPAEKDEES DDDMGFGLFD