RL6_GEOSE
ID RL6_GEOSE Reviewed; 178 AA.
AC P02391;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
DE AltName: Full=BL10;
GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1985969; DOI=10.1016/s0021-9258(17)35255-9;
RA Ramakrishnan V., Gerchman S.E.;
RT "Cloning, sequencing, and overexpression of genes for ribosomal proteins
RT from Bacillus stearothermophilus.";
RL J. Biol. Chem. 266:880-885(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-178.
RA Kimura M., Rawlings N., Appelt K.;
RT "The amino acid sequence of protein BL10 from the 50S subunit of the
RT Bacillus stearothermophilus ribosome.";
RL FEBS Lett. 136:58-64(1981).
RN [3]
RP PROTEIN SEQUENCE OF 150-164, AND CROSS-LINKING TO RRNA.
RC STRAIN=799;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8262035; DOI=10.1002/j.1460-2075.1993.tb06184.x;
RA Golden B.L., Ramakrishnan V., White S.W.;
RT "Ribosomal protein L6: structural evidence of gene duplication from a
RT primitive RNA binding protein.";
RL EMBO J. 12:4901-4908(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9642068; DOI=10.1006/jmbi.1998.1780;
RA Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V.,
RA White S.W.;
RT "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles
RT in protein synthesis and antibiotic resistance.";
RL J. Mol. Biol. 279:873-888(1998).
RN [6]
RP 3D-STRUCTURE MODELING 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: It is located near the subunit interface in the base of the
CC L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase
CC center (By similarity). This protein binds to the 23S rRNA, and is
CC important in its secondary structure. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR EMBL; M57622; AAA22700.1; ALT_SEQ; Genomic_DNA.
DR PIR; A02766; R5BS0F.
DR RefSeq; WP_011229634.1; NZ_RCTK01000011.1.
DR PDB; 1ML5; EM; 14.00 A; h=2-178.
DR PDB; 1RL6; X-ray; 2.00 A; A=2-178.
DR PDB; 4V4T; X-ray; 6.46 A; H=2-178.
DR PDBsum; 1ML5; -.
DR PDBsum; 1RL6; -.
DR PDBsum; 4V4T; -.
DR AlphaFoldDB; P02391; -.
DR SMR; P02391; -.
DR IntAct; P02391; 1.
DR GeneID; 58573177; -.
DR EvolutionaryTrace; P02391; -.
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 Gene3D; 3.90.930.12; -; 2.
DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR019906; Ribosomal_L6_bac-type.
DR InterPro; IPR002358; Ribosomal_L6_CS.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR PANTHER; PTHR11655:SF14; PTHR11655:SF14; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR PRINTS; PR00059; RIBOSOMALL6.
DR SUPFAM; SSF56053; SSF56053; 2.
DR TIGRFAMs; TIGR03654; L6_bact; 1.
DR PROSITE; PS00525; RIBOSOMAL_L6_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..178
FT /note="50S ribosomal protein L6"
FT /id="PRO_0000131037"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1RL6"
FT HELIX 59..80
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1RL6"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1RL6"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1RL6"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1RL6"
SQ SEQUENCE 178 AA; 19299 MW; C9D83BA8F35DB4FA CRC64;
MSRVGKKPIE IPAGVTVTVN GNTVTVKGPK GELTRTFHPD MTITVEGNVI TVTRPSDEKH
HRALHGTTRS LLANMVEGVS KGYEKALELV GVGYRASKQG KKLVLSVGYS HPVEIEPEEG
LEIEVPSQTK IIVKGADKQR VGELAANIRA VRPPEPYKGK GIRYEGELVR LKEGKTGK
