ID   RL22_MYCSM              Reviewed;         153 AA.
AC   O06115;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9402018; DOI=10.1046/j.1365-2958.1997.5811946.x;
RA   Sander P., Prammananan T., Meier A., Frischkorn K., Boettger E.C.;
RT   "The role of ribosomal RNAs in macrolide resistance.";
RL   Mol. Microbiol. 26:469-480(1997).
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; Y13227; CAA73670.1; -; Genomic_DNA.
DR   RefSeq; WP_011727673.1; NZ_UGQO01000001.1.
DR   PDB; 7S0S; EM; 3.05 A; U=6-119.
DR   PDBsum; 7S0S; -.
DR   AlphaFoldDB; O06115; -.
DR   SMR; O06115; -.
DR   GeneID; 66732900; -.
DR   OMA; KRIQPRA; -.
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..153
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000125186"
FT   REGION          110..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   153 AA;  16324 MW;  67F139A4E851F1C6 CRC64;
     MSTVTEFPSA TAKARYVRVS ATKARRVIDL VRGKSVEEAL DILRWAPQAA SEPVAKVIAS
     AAANAQNNEG LDPSTLVVAT VYADEGPTAK RIRPRAQGRA FRIRKRTSHI TVIVESRPPK
     QKGASAASAR SRRAQGSKAA ATKKSAETKE GSE