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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
 
 
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