RL1_THET2
ID RL1_THET2 Reviewed; 229 AA.
AC Q72GV9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=TT_C1739;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC the ribosome, and is involved in E site tRNA release.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; AE017221; AAS82081.1; -; Genomic_DNA.
DR RefSeq; WP_011174098.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; A=1-229.
DR PDB; 4V4J; X-ray; 3.83 A; A=1-229.
DR PDB; 4V8Y; EM; 4.30 A; L/y=1-229.
DR PDB; 4V9J; X-ray; 3.86 A; BC/DC=2-229.
DR PDB; 4V9K; X-ray; 3.50 A; BC/DC=2-229.
DR PDB; 4V9L; X-ray; 3.50 A; BC/DC=2-229.
DR PDB; 4V9M; X-ray; 4.00 A; BC/DC=2-229.
DR PDB; 4W29; X-ray; 3.80 A; BC/DC=2-229.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4W29; -.
DR AlphaFoldDB; Q72GV9; -.
DR SMR; Q72GV9; -.
DR IntAct; Q72GV9; 1.
DR STRING; 262724.TT_C1739; -.
DR EnsemblBacteria; AAS82081; AAS82081; TT_C1739.
DR KEGG; tth:TT_C1739; -.
DR eggNOG; COG0081; Bacteria.
DR HOGENOM; CLU_062853_0_0_0; -.
DR OMA; GWTDVDV; -.
DR OrthoDB; 1671455at2; -.
DR EvolutionaryTrace; Q72GV9; -.
DR Proteomes; UP000000592; 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; Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..229
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125763"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 11..17
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 97..107
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 129..136
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4V9K"
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