RL11_MYCS2
ID RL11_MYCS2 Reviewed; 142 AA.
AC A0QS45; I7G3N3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
GN OrderedLocusNames=MSMEG_1346, MSMEI_1308;
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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4]
RP PUPYLATION AT LYS-101, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC Interacts with L10 and the large rRNA to form the base of the stalk.
CC L10 forms an elongated spine to which L12 dimers bind in a sequential
CC fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; CP000480; ABK76087.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37781.1; -; Genomic_DNA.
DR RefSeq; WP_003892734.1; NZ_SIJM01000030.1.
DR RefSeq; YP_885733.1; NC_008596.1.
DR PDB; 5O60; EM; 3.20 A; J=1-142.
DR PDB; 5O61; EM; 3.31 A; J=1-142.
DR PDB; 5ZEB; EM; 3.40 A; J=1-142.
DR PDB; 5ZEP; EM; 3.40 A; J=1-142.
DR PDB; 5ZET; EM; 3.20 A; J=1-142.
DR PDB; 6DZI; EM; 3.46 A; J=10-142.
DR PDB; 6DZP; EM; 3.42 A; J=1-142.
DR PDBsum; 5O60; -.
DR PDBsum; 5O61; -.
DR PDBsum; 5ZEB; -.
DR PDBsum; 5ZEP; -.
DR PDBsum; 5ZET; -.
DR PDBsum; 6DZI; -.
DR PDBsum; 6DZP; -.
DR AlphaFoldDB; A0QS45; -.
DR SMR; A0QS45; -.
DR IntAct; A0QS45; 3.
DR STRING; 246196.MSMEI_1308; -.
DR PRIDE; A0QS45; -.
DR EnsemblBacteria; ABK76087; ABK76087; MSMEG_1346.
DR EnsemblBacteria; AFP37781; AFP37781; MSMEI_1308.
DR GeneID; 66732806; -.
DR KEGG; msg:MSMEI_1308; -.
DR KEGG; msm:MSMEG_1346; -.
DR PATRIC; fig|246196.19.peg.1330; -.
DR eggNOG; COG0080; Bacteria.
DR OMA; CKQFNAK; -.
DR OrthoDB; 1702697at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit 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; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT CHAIN 1..142
FT /note="50S ribosomal protein L11"
FT /id="PRO_1000046220"
FT CROSSLNK 101
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5ZET"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5O60"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:5ZET"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:5ZET"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:5ZET"
SQ SEQUENCE 142 AA; 15002 MW; 7DE04CBF2F3C37E5 CRC64;
MAPKKKVAGL IKLQIQAGQA NPAPPVGPAL GQHGVNIMEF CKAYNAATES QRGNVIPVEI
TVYEDRSFTF ALKTPPAAKL LLKAAGVQKG SGEPHKTKVA KVTWDQVREI AETKKADLNA
NDIDAAAKII AGTARSMGIT VE
