RL2_THET2
ID RL2_THET2 Reviewed; 276 AA.
AC Q72I07;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=TT_C1325;
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: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AE017221; AAS81667.1; -; Genomic_DNA.
DR RefSeq; WP_011173712.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; B=1-276.
DR PDB; 4V4J; X-ray; 3.83 A; B=1-276.
DR PDB; 4V63; X-ray; 3.21 A; BD/DD=1-276.
DR PDB; 4V67; X-ray; 3.00 A; BD/DD=1-276.
DR PDB; 4V7P; X-ray; 3.62 A; BC/CC=2-276.
DR PDB; 4V83; X-ray; 3.50 A; BC/DC=2-272.
DR PDB; 4V84; X-ray; 3.40 A; BC/DC=2-272.
DR PDB; 4V9J; X-ray; 3.86 A; BD/DD=2-276.
DR PDB; 4V9K; X-ray; 3.50 A; BD/DD=2-276.
DR PDB; 4V9L; X-ray; 3.50 A; BD/DD=2-276.
DR PDB; 4V9M; X-ray; 4.00 A; BD/DD=2-276.
DR PDB; 4V9N; X-ray; 3.40 A; BD/DD=2-272.
DR PDB; 4V9Q; X-ray; 3.40 A; AD/CD=2-272.
DR PDB; 4W29; X-ray; 3.80 A; BD/DD=2-276.
DR PDB; 4XEJ; X-ray; 3.80 A; AL02/BL02=2-272.
DR PDB; 5J4D; X-ray; 3.10 A; E/JB=2-276.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; Q72I07; -.
DR SMR; Q72I07; -.
DR IntAct; Q72I07; 4.
DR STRING; 262724.TT_C1325; -.
DR EnsemblBacteria; AAS81667; AAS81667; TT_C1325.
DR GeneID; 3168720; -.
DR KEGG; tth:TT_C1325; -.
DR eggNOG; COG0090; Bacteria.
DR HOGENOM; CLU_036235_2_1_0; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 961486at2; -.
DR EvolutionaryTrace; Q72I07; -.
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:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..276
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000237259"
FT REGION 223..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4V9Q"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 67..72
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4V84"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:4V9Q"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4V9K"
SQ SEQUENCE 276 AA; 30468 MW; 7CF40C2BD586349B CRC64;
MAVKKFKPYT PSRRFMTVAD FSEITKTEPE KSLVKPLKKT GGRNNQGRIT VRFRGGGHKR
LYRIIDFKRW DKVGIPAKVA AIEYDPNRSA RIALLHYVDG EKRYIIAPDG LQVGQQVVAG
PDAPIQVGNA LPLRFIPVGT VVHAVELEPK KGAKLARAAG TSAQIQGREG DYVILRLPSG
ELRKVHGECY ATVGAVGNAD HKNIVLGKAG RSRWLGRRPH VRGAAMNPVD HPHGGGEGRA
PRGRPPASPW GWQTKGLKTR KRRKPSSRFI IARRKK
