RL7_THET2
ID RL7_THET2 Reviewed; 125 AA.
AC Q72GS2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=TT_C1776;
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: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. Is thus essential for
CC accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S ribosomal
CC subunit. Forms a multimeric L10(L12)X complex, where L10 forms an
CC elongated spine to which 2 to 4 L12 dimers bind in a sequential
CC fashion. Binds GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00368}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR EMBL; AE017221; AAS82118.1; -; Genomic_DNA.
DR RefSeq; WP_008630582.1; NC_005835.1.
DR PDB; 4V9J; X-ray; 3.86 A; Be/De=51-122.
DR PDB; 4V9K; X-ray; 3.50 A; Be/De=51-122.
DR PDB; 4V9L; X-ray; 3.50 A; Be/De=51-122.
DR PDB; 4V9M; X-ray; 4.00 A; Be/De=51-122.
DR PDB; 4W29; X-ray; 3.80 A; Be/De=51-122.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4W29; -.
DR AlphaFoldDB; Q72GS2; -.
DR SMR; Q72GS2; -.
DR IntAct; Q72GS2; 1.
DR STRING; 262724.TT_C1776; -.
DR EnsemblBacteria; AAS82118; AAS82118; TT_C1776.
DR GeneID; 3168576; -.
DR KEGG; tth:TT_C1776; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_0; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1822695at2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00387; Ribosomal_L7_L12; 1.
DR Gene3D; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR TIGRFAMs; TIGR00855; L12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..125
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000243518"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 69..77
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 79..84
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4V9K"
SQ SEQUENCE 125 AA; 13067 MW; 3919CBF76605AC87 CRC64;
MALDIERIKE ELSQATVLEL KQLIDALKEA WGVTAAAPVA VAAAPAAGAA AAPAEEKTEF
DVILKEAGAK KLEVIKELRA ITGLGLKEAK DLAEKGGPVK EGVSKQEAEE IKKKLEAVGA
VVELK