RL11_GEOSE
ID RL11_GEOSE Reviewed; 133 AA.
AC P56210;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
DE Flags: Fragment;
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7783196; DOI=10.1006/jmbi.1995.0299;
RA Xing Y., Draper D.E.;
RT "Stabilization of a ribosomal RNA tertiary structure by ribosomal protein
RT L11.";
RL J. Mol. Biol. 249:319-331(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 63-129.
RX PubMed=10325228; DOI=10.1126/science.284.5417.1171;
RA Conn G.L., Draper D.E., Lattman E.E., Gittis A.G.;
RT "Crystal structure of a conserved ribosomal protein-RNA complex.";
RL Science 284:1171-1174(1999).
RN [3]
RP STRUCTURE BY NMR OF 59-133.
RX PubMed=8989327; DOI=10.1038/nsb0197-70;
RA Markus M.A., Hinck A.P., Huang S., Draper D.E., Torchia D.A.;
RT "High resolution solution structure of ribosomal protein L11-C76, a helical
RT protein with a flexible loop that becomes structured upon binding to RNA.";
RL Nat. Struct. Biol. 4:70-77(1997).
RN [4]
RP 3D-STRUCTURE MODELING OF 63-129 ONTO THE H.MARISMORTUI 50S RIBOSOME.
RX PubMed=10476961; DOI=10.1038/23641;
RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.;
RT "Placement of protein and RNA structures into a 5 A-resolution map of the
RT 50S ribosomal subunit.";
RL Nature 400:841-847(1999).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors.
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 2 L12 dimers bind in a sequential
CC fashion forming a pentameric L10(L12)2(L12)2 complex.
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 PIR; S55555; S55555.
DR PDB; 1ACI; NMR; -; A=59-133.
DR PDB; 1FOW; NMR; -; A=59-133.
DR PDB; 1FOX; NMR; -; A=59-133.
DR PDB; 1FOY; NMR; -; A=59-133.
DR PDB; 1HC8; X-ray; 2.80 A; A/B=58-132.
DR PDB; 1QA6; X-ray; 2.80 A; A/B=63-129.
DR PDB; 1Y39; X-ray; 2.80 A; A/B=58-133.
DR PDB; 2FOW; NMR; -; A=59-133.
DR PDBsum; 1ACI; -.
DR PDBsum; 1FOW; -.
DR PDBsum; 1FOX; -.
DR PDBsum; 1FOY; -.
DR PDBsum; 1HC8; -.
DR PDBsum; 1QA6; -.
DR PDBsum; 1Y39; -.
DR PDBsum; 2FOW; -.
DR AlphaFoldDB; P56210; -.
DR SMR; P56210; -.
DR EvolutionaryTrace; P56210; -.
DR GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IMP:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00349; Ribosomal_L11; 1.
DR DisProt; DP00512; -.
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; Direct protein sequencing; Methylation; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN <1..133
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104244"
FT NON_TER 1
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1ACI"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:1HC8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1ACI"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1HC8"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1HC8"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1HC8"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1HC8"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:1HC8"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1HC8"
SQ SEQUENCE 133 AA; 14103 MW; 2F0DAC76EFD4AAE1 CRC64;
MKLQIPAGKA NPAPPVGPAL GQAGVNIMAF CKEFNARTAD QAGLIIPVEI TVFEDRSFTF
ITKTPPAAVL LKKAAGIESG SGEPNRNKVA TIKRDKVREI AELKMPDLNA ASIEAAMRMI
EGTARSMGIV VED
