RL1_THETH
ID RL1_THETH Reviewed; 229 AA.
AC P27150;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318};
GN Synonyms=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VK1;
RA Ossina N., Eliseikina I.A., Garber M.B., Jonsson B.-H.;
RT "Cloning and overexpression of the ribosomal protein L1 gene from Thermus
RT thermophilus VK1. Crystallization of the recombinant protein L1.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-229.
RX PubMed=8136022; DOI=10.1007/bf01024930;
RA Amons R., Muranova T.A., Rykunova A.I., Eliseikina I.A., Sedelnikova S.E.;
RT "The complete primary structure of ribosomal protein L1 from Thermus
RT thermophilus.";
RL J. Protein Chem. 12:725-734(1993).
RN [3]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=VK1;
RX PubMed=1637860; DOI=10.1016/0300-9084(92)90110-z;
RA Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V.,
RA Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A.,
RA Svensson L.A.;
RT "Ribosomal proteins from Thermus thermophilus for structural
RT investigations.";
RL Biochimie 74:327-336(1992).
RN [4]
RP BINDING TO METHANOCOCCUS VANNIELII 23S RRNA AND TO M.VANNIELII L1 MRNA.
RC STRAIN=VK1;
RX PubMed=9746351; DOI=10.1046/j.1432-1327.1998.2560097.x;
RA Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.;
RT "Interaction of ribosomal L1 proteins from mesophilic and thermophilic
RT Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA.";
RL Eur. J. Biochem. 256:97-105(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RC STRAIN=VK1;
RX PubMed=8635468; DOI=10.1002/j.1460-2075.1996.tb00477.x;
RA Nikonov S.V., Nevskaya N., Eliseikina I.A., Fomenkova N.P., Nikulin A.,
RA Ossina N., Garber M.B., Jonsson B.-H., Briand C., Al-Karadaghi S.,
RA Svensson L.A., Aevarsson A., Liljas A.;
RT "Crystal structure of the RNA binding ribosomal protein L1 from Thermus
RT thermophilus.";
RL EMBO J. 15:1350-1359(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT CYS-180.
RX PubMed=9247141; DOI=10.1016/s0014-5793(97)00611-x;
RA Unge J., Al-Karadaghi S., Liljas A., Jonsson B.H., Eliseikina I.,
RA Ossina N., Nevskaya N., Fomenkova N., Garber M., Nikonov S.;
RT "A mutant form of the ribosomal protein L1 reveals conformational
RT flexibility.";
RL FEBS Lett. 411:53-59(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH A M.VANNIELII L1 MRNA
RP FRAGMENT.
RC STRAIN=VK1;
RX PubMed=16330048; DOI=10.1016/j.jmb.2005.10.084;
RA Nevskaya N., Tishchenko S., Volchkov S., Kljashtorny V., Nikonova E.,
RA Nikonov O., Nikulin A., Kohrer C., Piendl W., Zimmermann R., Stockley P.,
RA Garber M.B., Nikonov S.;
RT "New insights into the interaction of ribosomal protein L1 with RNA.";
RL J. Mol. Biol. 355:747-759(2006).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.5 ANGSTROMS).
RX PubMed=10721991; DOI=10.1016/s0092-8674(00)80690-x;
RA Gabashvili I.S., Agrawal R.K., Spahn C.M., Grassucci R.A., Svergun D.I.,
RA Frank J., Penczek P.;
RT "Solution structure of the E. coli 70S ribosome at 11.5 A resolution.";
RL Cell 100:537-549(2000).
CC -!- FUNCTION: The L1 stalk is quite mobile in the ribosome, and is involved
CC in E site tRNA release (By similarity). Binds directly to 23S rRNA.
CC {ECO:0000250}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of the L11 operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01318, ECO:0000269|PubMed:16330048}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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; X81375; CAA57139.1; -; Genomic_DNA.
DR PIR; S66577; S66577.
DR RefSeq; WP_011174098.1; NZ_CP053287.1.
DR PDB; 1AD2; X-ray; 1.90 A; A=2-229.
DR PDB; 1ZHO; X-ray; 2.60 A; A/C/E/G=2-229.
DR PDB; 2HW8; X-ray; 2.10 A; A=2-229.
DR PDB; 2OUM; X-ray; 2.55 A; A=2-229.
DR PDB; 2OV7; X-ray; 2.30 A; A/B/C=2-229.
DR PDB; 2VPL; X-ray; 2.30 A; A/C=2-229.
DR PDB; 3U4M; X-ray; 2.00 A; A=1-229.
DR PDB; 3U56; X-ray; 2.10 A; A=1-229.
DR PDB; 3UMY; X-ray; 1.90 A; A=2-229.
DR PDB; 4F9T; X-ray; 1.46 A; A=1-229.
DR PDB; 4QG3; X-ray; 2.00 A; A=2-229.
DR PDB; 4QGB; X-ray; 2.60 A; A/B=14-229.
DR PDB; 4QVI; X-ray; 1.90 A; A=1-229.
DR PDB; 4REO; X-ray; 1.35 A; A=1-229.
DR PDB; 5IB7; X-ray; 2.99 A; 71=1-229.
DR PDB; 5IB8; X-ray; 3.13 A; 71=1-229.
DR PDB; 5IBB; X-ray; 2.96 A; 71/79=1-229.
DR PDB; 5IMQ; EM; 3.80 A; Z=1-229.
DR PDB; 5IMR; EM; -; Z=1-229.
DR PDB; 5J8B; X-ray; 2.60 A; C=2-229.
DR PDBsum; 1AD2; -.
DR PDBsum; 1ZHO; -.
DR PDBsum; 2HW8; -.
DR PDBsum; 2OUM; -.
DR PDBsum; 2OV7; -.
DR PDBsum; 2VPL; -.
DR PDBsum; 3U4M; -.
DR PDBsum; 3U56; -.
DR PDBsum; 3UMY; -.
DR PDBsum; 4F9T; -.
DR PDBsum; 4QG3; -.
DR PDBsum; 4QGB; -.
DR PDBsum; 4QVI; -.
DR PDBsum; 4REO; -.
DR PDBsum; 5IB7; -.
DR PDBsum; 5IB8; -.
DR PDBsum; 5IBB; -.
DR PDBsum; 5IMQ; -.
DR PDBsum; 5IMR; -.
DR PDBsum; 5J8B; -.
DR AlphaFoldDB; P27150; -.
DR SMR; P27150; -.
DR EvolutionaryTrace; P27150; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR InterPro; IPR005878; Ribosom_L1_bac-type.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR TIGRFAMs; TIGR01169; rplA_bact; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Repressor; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1637860,
FT ECO:0000269|PubMed:8136022"
FT CHAIN 2..229
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125765"
FT CONFLICT 2
FT /note="P -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 4..5
FT /note="HG -> TN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="K -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:4REO"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4REO"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4REO"
SQ SEQUENCE 229 AA; 24826 MW; 38C14B2563718175 CRC64;
MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR
GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV
MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS
FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS
