RL22_MYCS2
ID RL22_MYCS2 Reviewed; 153 AA.
AC A0QSD6; I7FGB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331};
GN OrderedLocusNames=MSMEG_1441, MSMEI_1405;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(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: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; CP000480; ABK71298.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37878.1; -; Genomic_DNA.
DR RefSeq; WP_011727673.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885824.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; T=1-153.
DR PDB; 5O61; EM; 3.31 A; T=1-153.
DR PDB; 5XYM; EM; 3.08 A; S=1-153.
DR PDB; 5ZEB; EM; 3.40 A; T=1-153.
DR PDB; 5ZEP; EM; 3.40 A; T=1-153.
DR PDB; 5ZET; EM; 3.20 A; T=1-153.
DR PDB; 6DZI; EM; 3.46 A; T=6-119.
DR PDB; 6DZP; EM; 3.42 A; T=2-153.
DR PDBsum; 5O60; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5XYM; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZET; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZP; -.
DR AlphaFoldDB; A0QSD6; -.
DR SMR; A0QSD6; -.
DR IntAct; A0QSD6; 3.
DR STRING; 246196.MSMEI_1405; -.
DR PRIDE; A0QSD6; -.
DR EnsemblBacteria; ABK71298; ABK71298; MSMEG_1441.
DR EnsemblBacteria; AFP37878; AFP37878; MSMEI_1405.
DR GeneID; 66732900; -.
DR KEGG; msg:MSMEI_1405; -.
DR KEGG; msm:MSMEG_1441; -.
DR PATRIC; fig|246196.19.peg.1427; -.
DR eggNOG; COG0091; Bacteria.
DR OMA; KRIQPRA; -.
DR OrthoDB; 1666043at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..153
FT /note="50S ribosomal protein L22"
FT /id="PRO_1000052612"
FT REGION 110..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:5XYM"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5O60"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5XYM"
SQ SEQUENCE 153 AA; 16324 MW; 67F139A4E851F1C6 CRC64;
MSTVTEFPSA TAKARYVRVS ATKARRVIDL VRGKSVEEAL DILRWAPQAA SEPVAKVIAS
AAANAQNNEG LDPSTLVVAT VYADEGPTAK RIRPRAQGRA FRIRKRTSHI TVIVESRPPK
QKGASAASAR SRRAQGSKAA ATKKSAETKE GSE