RK22_SPIOL
ID RK22_SPIOL Reviewed; 199 AA.
AC P09594;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=50S ribosomal protein L22, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL22c {ECO:0000303|PubMed:28007896};
DE AltName: Full=Ribosomal protein CS-L13;
GN Name=rpl22;
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=2747623; DOI=10.1007/bf00334388;
RA Zhou D.X., Quigley F., Massenet O., Mache R.;
RT "Cotranscription of the S10- and spc-like operons in spinach chloroplasts
RT and identification of three of their gene products.";
RL Mol. Gen. Genet. 216:439-445(1989).
RN [2]
RP BINDING TO 5S RRNA.
RA Toukifimpa R., Romby P., Rozier C., Ehresmann C., Ehresmann B., Mache R.;
RT "Characterization and footprint analysis of two 5S rRNA binding proteins
RT from spinach chloroplast ribosomes.";
RL Biochemistry 28:5840-5846(1989).
RN [3]
RP ERYTHROMYCIN-BINDING, AND DELINEATION OF SEQUENCES REQUIRED FOR 5S
RP RRNA-BINDING.
RC STRAIN=cv. Geant d'hiver; TISSUE=Leaf;
RX PubMed=8441674; DOI=10.1093/nar/21.3.635;
RA Carol P., Rozier C., Lazaro E., Ballesta J.P.G., Mache R.;
RT "Erythromycin and 5S rRNA binding properties of the spinach chloroplast
RT ribosomal protein CL22.";
RL Nucleic Acids Res. 21:635-639(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [5]
RP PROTEIN SEQUENCE OF 2-7, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874046; DOI=10.1074/jbc.m005012200;
RA Yamaguchi K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 50S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28466-28482(2000).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS).
RX PubMed=18042701; DOI=10.1073/pnas.0709856104;
RA Sharma M.R., Wilson D.N., Datta P.P., Barat C., Schluenzen F., Fucini P.,
RA Agrawal R.K.;
RT "Cryo-EM study of the spinach chloroplast ribosome reveals the structural
RT and functional roles of plastid-specific ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19315-19320(2007).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=27762343; DOI=10.1038/srep35793;
RA Ahmed T., Yin Z., Bhushan S.;
RT "Cryo-EM structure of the large subunit of the spinach chloroplast
RT ribosome.";
RL Sci. Rep. 6:35793-35793(2016).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28007896; DOI=10.15252/embj.201695959;
RA Bieri P., Leibundgut M., Saurer M., Boehringer D., Ban N.;
RT "The complete structure of the chloroplast 70S ribosome in complex with
RT translation factor pY.";
RL EMBO J. 36:475-486(2017).
CC -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus. {ECO:0000305|PubMed:10874046,
CC ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast large ribosomal subunit (LSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins (PubMed:10874046, PubMed:28007896). uL22c binds 5S
CC rRNA in vitro; the central segment of the protein (approximately amino
CC acids 30 to 124) but not the last 28 amino acids are required for this
CC binding (PubMed:8441674). {ECO:0000269|PubMed:10874046,
CC ECO:0000269|PubMed:28007896, ECO:0000269|PubMed:8441674}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874046, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=23174.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; X13336; CAA31714.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88767.1; -; Genomic_DNA.
DR PIR; S01977; R5SP22.
DR RefSeq; NP_054974.1; NC_002202.1.
DR PDB; 4V61; EM; 9.40 A; BU=1-199.
DR PDB; 5H1S; EM; 3.50 A; U=1-199.
DR PDB; 5MLC; EM; 3.90 A; U=1-199.
DR PDB; 5MMI; EM; 3.25 A; T=1-199.
DR PDB; 5MMM; EM; 3.40 A; T=1-199.
DR PDB; 5X8P; EM; 3.40 A; T=1-199.
DR PDB; 5X8T; EM; 3.30 A; T=1-199.
DR PDB; 6ERI; EM; 3.00 A; AS=25-195.
DR PDBsum; 4V61; -.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MLC; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P09594; -.
DR SMR; P09594; -.
DR IntAct; P09594; 1.
DR STRING; 3562.P09594; -.
DR GeneID; 2715627; -.
DR KEGG; soe:2715627; -.
DR OrthoDB; 1389236at2759; -.
DR EvolutionaryTrace; P09594; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 2..199
FT /note="50S ribosomal protein L22, chloroplastic"
FT /id="PRO_0000125328"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 30..41
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 199 AA; 23246 MW; 58C444003AC28436 CRC64;
MGFFKKKEKK AEFDVFRLYG LHHPEPGKCD EITTRGYSIS MSVDKARRVI DQIRGRSYAE
TLMILELMPY RACYPIFKLI YSAAANASHN KQFNKANLII SKAEVNKGIT LKKVKPRARG
RSYMIKRPTC HITIVLRDIT HFDSYDKFLE SLTPKKLIAL LGLMSTGRRR ELLCGRFREN
HKIKSFLYKI ALFKRYEVM
