ID RL22_MYCA1 Reviewed; 180 AA.
AC A0QL13;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=MAV_4466;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000479; ABK69438.1; -; Genomic_DNA.
DR RefSeq; WP_009979094.1; NC_008595.1.
DR AlphaFoldDB; A0QL13; -.
DR SMR; A0QL13; -.
DR GeneID; 75271980; -.
DR KEGG; mav:MAV_4466; -.
DR HOGENOM; CLU_083987_1_0_11; -.
DR Proteomes; UP000001574; 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..180
FT /note="Large ribosomal subunit protein uL22"
FT /id="PRO_1000052611"
FT REGION 111..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 180 AA; 19073 MW; CC4DF2C458B13225 CRC64;
MTTTEFPSAV AKARFVRVSP RKARRVIDLV RGRSVTDALD ILRWAPQAAS EPVAKVIASA
AANAQNNNGL DPATLVVATV YADEGPTAKR IRPRAQGRAF RIRKRTSHIT VVVESRPAKD
QRSAKSSRTR RAEASKAAAK APAKKAPAKK APAKKAPAKT AAKKTPAKTS ETSDAKGGSD
//
