RL22_MYCMM
ID RL22_MYCMM Reviewed; 176 AA.
AC B2HSN6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=MMAR_1036;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(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; CP000854; ACC39494.1; -; Genomic_DNA.
DR RefSeq; WP_012392942.1; NC_010612.1.
DR AlphaFoldDB; B2HSN6; -.
DR SMR; B2HSN6; -.
DR STRING; 216594.MMAR_1036; -.
DR EnsemblBacteria; ACC39494; ACC39494; MMAR_1036.
DR GeneID; 64259778; -.
DR KEGG; mmi:MMAR_1036; -.
DR eggNOG; COG0091; Bacteria.
DR HOGENOM; CLU_083987_1_0_11; -.
DR OMA; KRIQPRA; -.
DR OrthoDB; 1666043at2; -.
DR Proteomes; UP000001190; 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..176
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000354488"
FT REGION 113..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 18638 MW; D4783A4B70CEBCF4 CRC64;
MTTTTEFPSA TAKARFVRVS PRKARRVIDL VRGRSVSDAL DILRWAPQAA SEPVAKVIAS
AAANAQNNNG LDPATLIVAT VYADEGPTAK RIRPRAQGRA FRIRKRTSHI TVVVESRPSK
DQRSSKSSRA RRAEGSKAAA TAPAKKSSAS KAPAKKAATK AESKTSETSE AKGGSD