ID   RL22_THETH              Reviewed;         113 AA.
AC   P48286;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=50S ribosomal protein L22;
GN   Name=rplV; Synonyms=rpl22;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RX   PubMed=7649262; DOI=10.1016/0014-5793(95)00755-x;
RA   Davydova N., Gryaznova O.I., Mashchenko O.V., Vysotskaya V.S.,
RA   Jonsson B.-H., Al-Karadaghi S., Liljas A., Garber M.B.;
RT   "Ribosomal protein L22 from Thermus thermophilus: sequencing,
RT   overexpression and crystallisation.";
RL   FEBS Lett. 369:229-232(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC   STRAIN=VK1;
RX   PubMed=9862810; DOI=10.1016/s0969-2126(98)00155-5;
RA   Unge J., Aaberg A., Al-Karadaghi S., Nikulin A., Nikonov S., Davydova N.,
RA   Nevskaya N., Garber M.B., Liljas A.;
RT   "The crystal structure of ribosomal protein L22 from Thermus thermophilus:
RT   insights into the mechanism of erythromycin resistance.";
RL   Structure 6:1577-1586(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT 82-LEU-ARG-84 DEL.
RC   STRAIN=VK1;
RX   PubMed=12225755; DOI=10.1016/s0022-2836(02)00772-6;
RA   Davydova N., Streltsov V., Wilce M., Liljas A., Garber M.B.;
RT   "L22 ribosomal protein and effect of its mutation on ribosome resistance to
RT   erythromycin.";
RL   J. Mol. Biol. 322:635-644(2002).
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:0000250}.
CC   -!- FUNCTION: The globular domain of the protein is one of the proteins
CC       that surrounds the polypeptide exit tunnel on the outside of the
CC       subunit, while an extended beta-hairpin is found that penetrates into
CC       the center of the 70S ribosome. This extension seems to form part of
CC       the wall of the exit tunnel (By similarity). Deleting residues 82 to 84
CC       (the equivalent deletion in E.coli renders cells resistant to
CC       erythromycin) would probably cause the tip of the hairpin to penetrate
CC       into the tunnel. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
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DR   EMBL; X84708; CAA59196.1; -; Genomic_DNA.
DR   RefSeq; WP_011173710.1; NZ_LR027517.1.
DR   PDB; 1BXE; X-ray; 1.90 A; A=1-113.
DR   PDB; 1I4J; X-ray; 1.80 A; A/B=1-113.
DR   PDBsum; 1BXE; -.
DR   PDBsum; 1I4J; -.
DR   AlphaFoldDB; P48286; -.
DR   SMR; P48286; -.
DR   GeneID; 3169835; -.
DR   EvolutionaryTrace; P48286; -.
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_0000125250"
FT   MUTAGEN         82..84
FT                   /note="Missing: Alters the orientation of the tip of the
FT                   beta-hairpin, bending it into the polypeptide exit tunnel."
FT   STRAND          3..12
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   HELIX           14..24
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   HELIX           29..38
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   HELIX           44..60
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   STRAND          69..81
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:1I4J"
FT   STRAND          98..111
FT                   /evidence="ECO:0007829|PDB:1I4J"
SQ   SEQUENCE   113 AA;  12780 MW;  11814D2DE644AF1F CRC64;
     MEAKAIARYV RISPRKVRLV VDLIRGKSLE EARNILRYTN KRGAYFVAKV LESAAANAVN
     NHDMLEDRLY VKAAYVDEGP ALKRVLPRAR GRADIIKKRT SHITVILGEK HGK