RK22_CHLRE
ID RK22_CHLRE Reviewed; 175 AA.
AC Q84U21;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=50S ribosomal protein L22, chloroplastic;
DE Flags: Precursor;
GN Name=ERY2; Synonyms=RPL22;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=CC-1952;
RX PubMed=12930744; DOI=10.1093/genetics/164.4.1345;
RA Bowers A.K., Keller J.A., Dutcher S.K.;
RT "Molecular markers for rapidly identifying candidate genes in Chlamydomonas
RT reinhardtii: ERY1 and ERY2 encode chloroplast ribosomal proteins.";
RL Genetics 164:1345-1353(2003).
RN [2]
RP DISRUPTION PHENOTYPE.
RA Hanson M.R., Bogorad L.;
RT "The ery-M2 group of Chlamydomonas reinhardtii: cold-sensitive,
RT erythromycin-resistant mutants deficient in chloroplast ribosomes.";
RL J. Gen. Microbiol. 105:253-262(1978).
CC -!- FUNCTION: This protein binds specifically to 23S rRNA. {ECO:0000250}.
CC -!- FUNCTION: The globular domain of the protein is located near the
CC polypeptide exit tunnel on the outside of the subunit, while an
CC extended beta-hairpin is found that lines the wall of the exit tunnel
CC in the center of the 70S ribosome. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- DISRUPTION PHENOTYPE: Cells are erythromycin and tylosin resistant.
CC Ery2 mutants (formerly called ery-M2) are cold-sensitive for growth at
CC 15 degrees Celsius. Resistance and cold sensitivity are recessive to
CC the wild-type allele. At least one mutant (ery2-4 formerly ery-M2d) has
CC fewer chloroplast ribosomes than the wild-type.
CC {ECO:0000269|PubMed:12930744, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; AY226166; AAO53243.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84U21; -.
DR SMR; Q84U21; -.
DR EnsemblPlants; PNW73989; PNW73989; CHLRE_13g580850v5.
DR EnsemblPlants; PNW73990; PNW73990; CHLRE_13g580850v5.
DR Gramene; PNW73989; PNW73989; CHLRE_13g580850v5.
DR Gramene; PNW73990; PNW73990; CHLRE_13g580850v5.
DR OMA; YRACEKI; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR PANTHER; PTHR13501; PTHR13501; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01044; rplV_bact; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Chloroplast; Plastid; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..175
FT /note="50S ribosomal protein L22, chloroplastic"
FT /id="PRO_0000030484"
SQ SEQUENCE 175 AA; 18925 MW; BF4AE8B281D585DE CRC64;
MALRACSSSL VARSAARSVQ PFRPAAVRPA RIAPVARKTA TVVCSAATDA PAAPVAEAVV
GEVKSGVAHL KFQRGSADKI RRVLDVIRGR SYEEALVLCE YMPYRACEKI IKCLMSAAAN
AKHNKGALKT KLVVSECFAD EGPVLKRARP RAQGRANLIM KPTFHMTIRV EERAQ
