ID   RL22_SPIKU              Reviewed;         112 AA.
AC   Q6XYY1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
OS   Spiroplasma kunkelii.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=47834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CR2-3x;
RX   PubMed=12845528; DOI=10.1007/s00438-003-0878-3;
RA   Zhao Y., Hammond R.W., Jomantiene R., Dally E.L., Lee I.-M., Jia H., Wu H.,
RA   Lin S., Zhang P., Kenton S., Najar F.Z., Hua A., Roe B.A., Fletcher J.,
RA   Davis R.E.;
RT   "Gene content and organization of an 85-kb DNA segment from the genome of
RT   the phytopathogenic mollicute Spiroplasma kunkelii.";
RL   Mol. Genet. Genomics 269:592-602(2003).
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; AY198133; AAP58897.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6XYY1; -.
DR   SMR; Q6XYY1; -.
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   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..112
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000125220"
SQ   SEQUENCE   112 AA;  12572 MW;  3398140A8E793CAC CRC64;
     MDVRANLRSI RISPRKVRLV TDLIRNKKVG DAIVILNNTN KKSSVPVQKL VKSAVANAVN
     NNGLDADRLF IKEIFVNEGP TLKRFRPRAH GRAYEILKRT SHITVTVSDG QQ