ID   RL22_PELTS              Reviewed;         113 AA.
AC   A5D5J5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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}; OrderedLocusNames=PTH_0325;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009389; BAF58506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D5J5; -.
DR   SMR; A5D5J5; -.
DR   STRING; 370438.PTH_0325; -.
DR   EnsemblBacteria; BAF58506; BAF58506; PTH_0325.
DR   KEGG; pth:PTH_0325; -.
DR   eggNOG; COG0091; Bacteria.
DR   HOGENOM; CLU_083987_3_3_9; -.
DR   OMA; KRIQPRA; -.
DR   Proteomes; UP000006556; 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   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..113
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_1000086560"
SQ   SEQUENCE   113 AA;  12836 MW;  B992F77264C3026B CRC64;
     MEAKAVARYI RISPRKVRQV VDLIRGKKLN EALAILRYTP KRASAVVAKV VRSAAANAEN
     NLQMDRDELF IKACYVDQGP TYKRYMPRAF GRADVMRKRT SHITVVVSDK KEG