RL21_MYCS2
ID RL21_MYCS2 Reviewed; 103 AA.
AC A0R151; I7G5N4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363};
GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363};
GN OrderedLocusNames=MSMEG_4625, MSMEI_4508;
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 to 23S rRNA in the presence of protein
CC L20. {ECO:0000255|HAMAP-Rule:MF_01363}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L20.
CC {ECO:0000255|HAMAP-Rule:MF_01363}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.
CC {ECO:0000255|HAMAP-Rule:MF_01363}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK75887.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40962.1; -; Genomic_DNA.
DR RefSeq; WP_003896002.1; NZ_SIJM01000004.1.
DR RefSeq; YP_888889.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; S=1-103.
DR PDB; 5O61; EM; 3.31 A; S=1-103.
DR PDB; 5XYM; EM; 3.08 A; R=1-103.
DR PDB; 5ZEB; EM; 3.40 A; S=1-103.
DR PDB; 5ZEP; EM; 3.40 A; S=1-103.
DR PDB; 5ZET; EM; 3.20 A; S=1-103.
DR PDB; 6DZI; EM; 3.46 A; S=3-102.
DR PDB; 6DZP; EM; 3.42 A; S=2-103.
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; A0R151; -.
DR SMR; A0R151; -.
DR IntAct; A0R151; 3.
DR STRING; 246196.MSMEI_4508; -.
DR PRIDE; A0R151; -.
DR EnsemblBacteria; ABK75887; ABK75887; MSMEG_4625.
DR EnsemblBacteria; AFP40962; AFP40962; MSMEI_4508.
DR GeneID; 66735945; -.
DR KEGG; msg:MSMEI_4508; -.
DR KEGG; msm:MSMEG_4625; -.
DR PATRIC; fig|246196.19.peg.4520; -.
DR eggNOG; COG0261; Bacteria.
DR OMA; HRQEITR; -.
DR OrthoDB; 1949059at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 HAMAP; MF_01363; Ribosomal_L21; 1.
DR InterPro; IPR036164; L21-like_sf.
DR InterPro; IPR028909; L21p-like.
DR InterPro; IPR001787; Ribosomal_L21.
DR InterPro; IPR018258; Ribosomal_L21_CS.
DR PANTHER; PTHR21349; PTHR21349; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR SUPFAM; SSF141091; SSF141091; 1.
DR TIGRFAMs; TIGR00061; L21; 1.
DR PROSITE; PS01169; RIBOSOMAL_L21; 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..103
FT /note="50S ribosomal protein L21"
FT /id="PRO_1000067857"
FT STRAND 4..19
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5XYM"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5XYM"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5XYM"
SQ SEQUENCE 103 AA; 11034 MW; 79524E8A2DF81DDC CRC64;
MATYAIVKTG GKQYKVAAGD VVKVEKLDSE PGASVSLPVA LVVDGANVTS KADDLAKVAV
TAEVLEHTKG PKIRIHKFKN KTGYHKRQGH RQQLTVLKVT GIK