RL1_THET8
ID RL1_THET8 Reviewed; 229 AA.
AC Q5SLP7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=50S ribosomal protein L1;
GN Name=rplA; OrderedLocusNames=TTHA0246;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-26.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=11154066; DOI=10.1515/bc.2000.133;
RA Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H.,
RA Choli-Papadopoulou T.;
RT "Identification of the 50S ribosomal proteins from the eubacterium Thermus
RT thermophilus.";
RL Biol. Chem. 381:1079-1087(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-181.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=1447157; DOI=10.1128/jb.174.23.7859-7863.1992;
RA Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.;
RT "Identification of the gene encoding transcription factor NusG of Thermus
RT thermophilus.";
RL J. Bacteriol. 174:7859-7863(1992).
RN [4]
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16287167; DOI=10.1002/pmic.200402111;
RA Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.;
RT "Extending ribosomal protein identifications to unsequenced bacterial
RT strains using matrix-assisted laser desorption/ionization mass
RT spectrometry.";
RL Proteomics 5:4818-4831(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11511350; DOI=10.1016/s0092-8674(01)00435-4;
RA Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.;
RT "The path of messenger RNA through the ribosome.";
RL Cell 106:233-241(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11283358; DOI=10.1126/science.1060089;
RA Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N.,
RA Cate J.H.D., Noller H.F.;
RT "Crystal structure of the ribosome at 5.5 A resolution.";
RL Science 292:883-896(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2,
RP AND SUBUNIT.
RX PubMed=18988853; DOI=10.1126/science.1164840;
RA Weixlbaumer A., Jin H., Neubauer C., Voorhees R.M., Petry S., Kelley A.C.,
RA Ramakrishnan V.;
RT "Insights into translational termination from the structure of RF2 bound to
RT the ribosome.";
RL Science 322:953-956(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH RF2,
RP AND SUBUNIT.
RX PubMed=20421507; DOI=10.1073/pnas.1003995107;
RA Jin H., Kelley A.C., Loakes D., Ramakrishnan V.;
RT "Structure of the 70S ribosome bound to release factor 2 and a substrate
RT analog provides insights into catalysis of peptide release.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8593-8598(2010).
CC -!- FUNCTION: Directly binds to 23S rRNA. Forms what is known as the L1
CC stalk, which protrudes beyond the 70S ribosome surface. The stalk is
CC preferentially stabilized in 70S versus 50S crystals. Interacts with
CC the E site tRNA, blocking the exit path. This blockage implies that
CC this section of the ribosome must be able to move to release the
CC deacetylated tRNA.
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:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- MASS SPECTROMETRY: Mass=24698; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287167};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD70069.1; -; Genomic_DNA.
DR RefSeq; WP_011227804.1; NC_006461.1.
DR RefSeq; YP_143512.1; NC_006461.1.
DR PDB; 1ML5; EM; 14.00 A; c=2-229.
DR PDB; 2OM7; EM; 7.30 A; K=1-229.
DR PDB; 3TG8; X-ray; 1.95 A; A=1-229.
DR PDB; 4V42; X-ray; 5.50 A; BC=2-229.
DR PDB; 4V4P; X-ray; 5.50 A; AC=2-229.
DR PDB; 4V4X; X-ray; 5.00 A; BC=1-229.
DR PDB; 4V4Y; X-ray; 5.50 A; BC=1-229.
DR PDB; 4V4Z; X-ray; 4.51 A; BC=1-229.
DR PDB; 4V51; X-ray; 2.80 A; BC/DC=2-229.
DR PDB; 4V5A; X-ray; 3.50 A; BC/DC=2-229.
DR PDB; 4V5C; X-ray; 3.30 A; BC/DC=1-229.
DR PDB; 4V5D; X-ray; 3.50 A; BC/DC=1-229.
DR PDB; 4V5E; X-ray; 3.45 A; BC/DC=1-229.
DR PDB; 4V5F; X-ray; 3.60 A; BC/DC=1-229.
DR PDB; 4V5G; X-ray; 3.60 A; BC/DC=1-229.
DR PDB; 4V5J; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V5K; X-ray; 3.20 A; BC/DC=1-229.
DR PDB; 4V5L; X-ray; 3.10 A; BC=1-229.
DR PDB; 4V5M; EM; 7.80 A; BC=1-229.
DR PDB; 4V5N; EM; 7.60 A; BC=1-229.
DR PDB; 4V5P; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V5Q; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V5R; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V5S; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V68; EM; 6.40 A; BC=19-225.
DR PDB; 4V6A; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V7J; X-ray; 3.30 A; AC/BC=1-229.
DR PDB; 4V7K; X-ray; 3.60 A; AC/BC=1-229.
DR PDB; 4V7L; X-ray; 3.00 A; BC/DC=1-229.
DR PDB; 4V7M; X-ray; 3.45 A; BC/DC=1-229.
DR PDB; 4V8J; X-ray; 3.90 A; BC/DC=1-229.
DR PDB; 4V8N; X-ray; 3.10 A; BC/DC=1-229.
DR PDB; 4V8O; X-ray; 3.80 A; BC=1-229.
DR PDB; 4V8Q; X-ray; 3.10 A; AC=1-229.
DR PDB; 4V8U; X-ray; 3.70 A; BC/DC=1-229.
DR PDB; 4V8X; X-ray; 3.35 A; BC/DC=1-229.
DR PDB; 4V90; X-ray; 2.95 A; BC=2-229.
DR PDB; 4V97; X-ray; 3.52 A; BC/DC=1-229.
DR PDB; 4V9H; X-ray; 2.86 A; BC=1-229.
DR PDB; 4WF1; X-ray; 3.09 A; B5=19-225.
DR PDB; 4WPO; X-ray; 2.80 A; AC/CC=2-229.
DR PDB; 4WQF; X-ray; 2.80 A; AC/CC=2-229.
DR PDB; 4WQU; X-ray; 2.80 A; AC/CC=2-229.
DR PDB; 4WQY; X-ray; 2.80 A; AC/CC=2-229.
DR PDB; 4WT8; X-ray; 3.40 A; CA/DA=19-111.
DR PDB; 4WU1; X-ray; 3.20 A; 71/79=1-229.
DR PDB; 4WZD; X-ray; 3.10 A; 71/79=1-229.
DR PDB; 4WZO; X-ray; 3.30 A; 71=1-229.
DR PDB; 5A9Z; EM; 4.70 A; AC=2-229.
DR PDB; 5AA0; EM; 5.00 A; AC=2-229.
DR PDB; 5E7K; X-ray; 3.20 A; 71/79=1-229.
DR PDB; 5E81; X-ray; 2.95 A; 71/79=1-229.
DR PDB; 5EL4; X-ray; 3.15 A; 71=1-229.
DR PDB; 5EL5; X-ray; 3.15 A; 71=1-229.
DR PDB; 5EL6; X-ray; 3.10 A; 71/79=1-229.
DR PDB; 5EL7; X-ray; 3.15 A; 71/79=1-229.
DR PDB; 5HAU; X-ray; 3.00 A; 1C/2C=1-229.
DR PDB; 5NPM; X-ray; 2.70 A; A=10-229.
DR PDB; 5OT7; EM; 3.80 A; f=3-229.
DR PDB; 5UQ7; EM; 3.50 A; C=3-229.
DR PDB; 5UQ8; EM; 3.20 A; C=3-229.
DR PDB; 6C5L; X-ray; 3.20 A; BC/DC=1-229.
DR PDB; 6Q95; EM; 3.70 A; A=1-229.
DR PDB; 6QNQ; X-ray; 3.50 A; 71=1-229.
DR PDB; 6QNR; X-ray; 3.10 A; 71/79=1-229.
DR PDB; 7LH5; X-ray; 3.27 A; BC/DC=1-229.
DR PDBsum; 1ML5; -.
DR PDBsum; 2OM7; -.
DR PDBsum; 3TG8; -.
DR PDBsum; 4V42; -.
DR PDBsum; 4V4P; -.
DR PDBsum; 4V4X; -.
DR PDBsum; 4V4Y; -.
DR PDBsum; 4V4Z; -.
DR PDBsum; 4V51; -.
DR PDBsum; 4V5A; -.
DR PDBsum; 4V5C; -.
DR PDBsum; 4V5D; -.
DR PDBsum; 4V5E; -.
DR PDBsum; 4V5F; -.
DR PDBsum; 4V5G; -.
DR PDBsum; 4V5J; -.
DR PDBsum; 4V5K; -.
DR PDBsum; 4V5L; -.
DR PDBsum; 4V5M; -.
DR PDBsum; 4V5N; -.
DR PDBsum; 4V5P; -.
DR PDBsum; 4V5Q; -.
DR PDBsum; 4V5R; -.
DR PDBsum; 4V5S; -.
DR PDBsum; 4V68; -.
DR PDBsum; 4V6A; -.
DR PDBsum; 4V7J; -.
DR PDBsum; 4V7K; -.
DR PDBsum; 4V7L; -.
DR PDBsum; 4V7M; -.
DR PDBsum; 4V8J; -.
DR PDBsum; 4V8N; -.
DR PDBsum; 4V8O; -.
DR PDBsum; 4V8Q; -.
DR PDBsum; 4V8U; -.
DR PDBsum; 4V8X; -.
DR PDBsum; 4V90; -.
DR PDBsum; 4V97; -.
DR PDBsum; 4V9H; -.
DR PDBsum; 4WF1; -.
DR PDBsum; 4WPO; -.
DR PDBsum; 4WQF; -.
DR PDBsum; 4WQU; -.
DR PDBsum; 4WQY; -.
DR PDBsum; 4WT8; -.
DR PDBsum; 4WU1; -.
DR PDBsum; 4WZD; -.
DR PDBsum; 4WZO; -.
DR PDBsum; 5A9Z; -.
DR PDBsum; 5AA0; -.
DR PDBsum; 5E7K; -.
DR PDBsum; 5E81; -.
DR PDBsum; 5EL4; -.
DR PDBsum; 5EL5; -.
DR PDBsum; 5EL6; -.
DR PDBsum; 5EL7; -.
DR PDBsum; 5HAU; -.
DR PDBsum; 5NPM; -.
DR PDBsum; 5OT7; -.
DR PDBsum; 5UQ7; -.
DR PDBsum; 5UQ8; -.
DR PDBsum; 6C5L; -.
DR PDBsum; 6Q95; -.
DR PDBsum; 6QNQ; -.
DR PDBsum; 6QNR; -.
DR PDBsum; 7LH5; -.
DR AlphaFoldDB; Q5SLP7; -.
DR SMR; Q5SLP7; -.
DR IntAct; Q5SLP7; 9.
DR STRING; 300852.55771628; -.
DR EnsemblBacteria; BAD70069; BAD70069; BAD70069.
DR GeneID; 3168861; -.
DR KEGG; ttj:TTHA0246; -.
DR PATRIC; fig|300852.9.peg.246; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_0; -.
DR OMA; GWTDVDV; -.
DR PhylomeDB; Q5SLP7; -.
DR EvolutionaryTrace; Q5SLP7; -.
DR Proteomes; UP000000532; Chromosome.
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; Reference proteome; Repressor;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11154066"
FT CHAIN 2..229
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125764"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5NPM"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:3TG8"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:3TG8"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3TG8"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3TG8"
SQ SEQUENCE 229 AA; 24831 MW; 99EE7BE00801B1B4 CRC64;
MPKHGKRYRA LLEKVDPNKV YTIDEAARLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR
GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV
MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS
FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS
