RL22_ACIC1
ID RL22_ACIC1 Reviewed; 281 AA.
AC A0LRM5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=50S ribosomal protein L22;
GN Name=rplV; OrderedLocusNames=Acel_0311;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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:0000250}.
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:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; CP000481; ABK52085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LRM5; -.
DR SMR; A0LRM5; -.
DR STRING; 351607.Acel_0311; -.
DR EnsemblBacteria; ABK52085; ABK52085; Acel_0311.
DR KEGG; ace:Acel_0311; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_989112_0_0_11; -.
DR OMA; RTSHFKV; -.
DR Proteomes; UP000008221; 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..281
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000354536"
FT REGION 1..138
FT /note="50S ribosomal protein L22"
FT REGION 137..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..281
FT /note="Unknown"
FT REGION 199..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 29253 MW; CE26C01FBACCFC21 CRC64;
MASPMGSTAS LTGPVVRARA RLRYSTITPM KARRVVDLVR GLPADEALTT LQFLPQAASA
TVYKVLASAI ANAQQEAAKQ GERLDAEDLV VSAAYVDEGP TLKRFRPRAQ GRAYRIRKRT
SHITIHVESW PAEAETRATK KAVPKGARHR RRLTGAGKPA ASAATETPAA QPVAATTETV
EVEAAATAGA PPTVETPVAV ASAATETPAA TAAETKAGGA AEAEVATTDE QTTETAPAAE
AEKPAVRRPA ARKSTTSARR RAAETEGHDS DAESTDEGGT R
