ID RL22_RICCN Reviewed; 119 AA. AC Q92GX1; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000255|HAMAP-Rule:MF_01331}; DE AltName: Full=50S ribosomal protein L22 {ECO:0000305}; GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=RC1001; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03539.1; -; Genomic_DNA. DR PIR; A97825; A97825. DR RefSeq; WP_010977585.1; NC_003103.1. DR AlphaFoldDB; Q92GX1; -. DR SMR; Q92GX1; -. DR GeneID; 928143; -. DR KEGG; rco:RC1001; -. DR PATRIC; fig|272944.4.peg.1141; -. DR HOGENOM; CLU_083987_3_0_5; -. DR Proteomes; UP000000816; 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; Ribosomal protein L22/L17; 1. DR HAMAP; MF_01331_B; Ribosomal_uL22_B; 1. DR InterPro; IPR001063; Ribosomal_uL22. DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type. DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type. DR InterPro; IPR018260; Ribosomal_uL22_CS. DR InterPro; IPR036394; Ribosomal_uL22_sf. DR NCBIfam; TIGR01044; rplV_bact; 1. DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1. DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1. DR Pfam; PF00237; Ribosomal_L22; 1. DR SUPFAM; SSF54843; Ribosomal protein L22; 1. DR PROSITE; PS00464; RIBOSOMAL_L22; 1. PE 3: Inferred from homology; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1..119 FT /note="Large ribosomal subunit protein uL22" FT /id="PRO_0000125213" SQ SEQUENCE 119 AA; 13253 MW; 5BE636CA907C7DA8 CRC64; MVQENKNFAT AQAKSIRVSS RKLNLVAAFI RNMKVSEALV QLTFSPKRIA KVVKDCLQSA VANAENNLGL DIDRLVVTKA TVGKALVMKR VMPRAKGRAT RINKFFSNLY ITVTEKEDN //