RL22_ALTMD
ID RL22_ALTMD Reviewed; 110 AA.
AC B4S096; F2G5N9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
GN OrderedLocusNames=MADE_1002285;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(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}.
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DR EMBL; CP001103; AEA96606.1; -; Genomic_DNA.
DR RefSeq; WP_012516962.1; NC_011138.3.
DR AlphaFoldDB; B4S096; -.
DR SMR; B4S096; -.
DR EnsemblBacteria; AEA96606; AEA96606; MADE_1002285.
DR GeneID; 56340946; -.
DR KEGG; amc:MADE_1002285; -.
DR HOGENOM; CLU_083987_3_3_6; -.
DR OMA; KRIQPRA; -.
DR Proteomes; UP000001870; 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..110
FT /note="50S ribosomal protein L22"
FT /id="PRO_1000142222"
SQ SEQUENCE 110 AA; 12098 MW; F7CBFBA3BA315746 CRC64;
MEALAKHRFA RTSAQKARLV ADQIRGLHVE KALEVLAYSP KKSAALVKKV LESAIANAEH
NEGADIDELV VAKVFVDEGP TMKRIKPRAK GRADRIFKRS SHITVVVADN