RL22_THET2
ID RL22_THET2 Reviewed; 113 AA.
AC Q72I09;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=TT_C1323;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
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:0000255|HAMAP-Rule:MF_01331}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR EMBL; AE017221; AAS81665.1; -; Genomic_DNA.
DR RefSeq; WP_011173710.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; Q=1-113.
DR PDB; 4V4J; X-ray; 3.83 A; Q=1-113.
DR PDB; 4V63; X-ray; 3.21 A; BW/DW=1-113.
DR PDB; 4V67; X-ray; 3.00 A; BW/DW=1-113.
DR PDB; 4V7P; X-ray; 3.62 A; BS/CS=1-112.
DR PDB; 4V83; X-ray; 3.50 A; BS/DS=1-112.
DR PDB; 4V84; X-ray; 3.40 A; BS/DS=1-112.
DR PDB; 4V9J; X-ray; 3.86 A; BW/DW=1-113.
DR PDB; 4V9K; X-ray; 3.50 A; BW/DW=1-113.
DR PDB; 4V9L; X-ray; 3.50 A; BW/DW=1-113.
DR PDB; 4V9M; X-ray; 4.00 A; BW/DW=1-113.
DR PDB; 4V9N; X-ray; 3.40 A; BW/DW=1-112.
DR PDB; 4V9Q; X-ray; 3.40 A; AS/CS=1-112.
DR PDB; 4W29; X-ray; 3.80 A; BW/DW=1-113.
DR PDB; 4XEJ; X-ray; 3.80 A; AL22/BL22=1-112.
DR PDB; 5J4D; X-ray; 3.10 A; T/YB=1-113.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; Q72I09; -.
DR SMR; Q72I09; -.
DR IntAct; Q72I09; 4.
DR STRING; 262724.TT_C1323; -.
DR EnsemblBacteria; AAS81665; AAS81665; TT_C1323.
DR GeneID; 3169835; -.
DR KEGG; tth:TT_C1323; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_083987_3_1_0; -.
DR OMA; KRIQPRA; -.
DR OrthoDB; 1666043at2; -.
DR EvolutionaryTrace; Q72I09; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..113
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125248"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 22..26
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 76..87
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 113 AA; 12780 MW; 11814D2DE644AF1F CRC64;
MEAKAIARYV RISPRKVRLV VDLIRGKSLE EARNILRYTN KRGAYFVAKV LESAAANAVN
NHDMLEDRLY VKAAYVDEGP ALKRVLPRAR GRADIIKKRT SHITVILGEK HGK
