ID RL22_AQUPY Reviewed; 133 AA.
AC Q9ZI45;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 76.
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};
GN Synonyms=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331};
OS Aquifex pyrophilus.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=2714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX PubMed=10795828; DOI=10.1007/s002399910040;
RA Bocchetta M., Gribaldo S., Sanangelantoni A.M., Cammarano P.;
RT "Phylogenetic depth of the bacterial genera Aquifex and Thermotoga inferred
RT from analysis of ribosomal protein, elongation factor, and RNA polymerase
RT subunit sequences.";
RL J. Mol. Evol. 50:366-380(2000).
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; AF040100; AAD08790.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZI45; -.
DR SMR; Q9ZI45; -.
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..133
FT /note="Large ribosomal subunit protein uL22"
FT /id="PRO_0000125111"
SQ SEQUENCE 133 AA; 15118 MW; 894D0ED96A604247 CRC64;
MGQLKIKDKS QREGYKPNQA IAILRYAHIS PLKARLVLRE IHGKDVGEAL YLLKVIPKRA
ARIAEKLLKS AIANAEQKGL DLDRLYIKKA VADRGPILKK WIPRAHGRAT MVRKRLSHIT
IVLEEKPEGK EEE
//
