RL3_THET2
ID RL3_THET2 Reviewed; 206 AA.
AC Q72I04;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=TT_C1328;
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, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR EMBL; AE017221; AAS81670.1; -; Genomic_DNA.
DR RefSeq; WP_011173714.1; NC_005835.1.
DR PDB; 4V4I; X-ray; 3.71 A; C=1-206.
DR PDB; 4V4J; X-ray; 3.83 A; C=1-206.
DR PDB; 4V63; X-ray; 3.21 A; BE/DE=1-206.
DR PDB; 4V67; X-ray; 3.00 A; BE/DE=1-206.
DR PDB; 4V7P; X-ray; 3.62 A; BD/CD=1-206.
DR PDB; 4V83; X-ray; 3.50 A; BD/DD=1-204.
DR PDB; 4V84; X-ray; 3.40 A; BD/DD=1-204.
DR PDB; 4V9J; X-ray; 3.86 A; BE/DE=1-205.
DR PDB; 4V9K; X-ray; 3.50 A; BE/DE=1-205.
DR PDB; 4V9L; X-ray; 3.50 A; BE/DE=1-205.
DR PDB; 4V9M; X-ray; 4.00 A; BE/DE=1-205.
DR PDB; 4V9N; X-ray; 3.40 A; BE/DE=1-204.
DR PDB; 4V9Q; X-ray; 3.40 A; AE/CE=1-204.
DR PDB; 4W29; X-ray; 3.80 A; BE/DE=1-205.
DR PDB; 4XEJ; X-ray; 3.80 A; AL03/BL03=1-204.
DR PDB; 5J4D; X-ray; 3.10 A; F/KB=1-206.
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; Q72I04; -.
DR SMR; Q72I04; -.
DR IntAct; Q72I04; 4.
DR STRING; 262724.TT_C1328; -.
DR EnsemblBacteria; AAS81670; AAS81670; TT_C1328.
DR GeneID; 3167929; -.
DR KEGG; tth:TT_C1328; -.
DR eggNOG; COG0087; Bacteria.
DR HOGENOM; CLU_044142_4_1_0; -.
DR OMA; KRMAGRY; -.
DR OrthoDB; 1270636at2; -.
DR EvolutionaryTrace; Q72I04; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..206
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000241428"
FT STRAND 3..16
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 56..62
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:4V9Q"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 159..176
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 206 AA; 22408 MW; A920741478CB6028 CRC64;
MKGILGVKVG MTRIFRDDRA VPVTVILAGP CPVVQRRTPE KDGYTAVQLG FLPQNPKRVN
RPLKGHFAKA GVEPVRILRE IRDFNPEGDT VTVEIFKPGE RVDVTGTSKG RGFAGVMKRW
NFAGGPDSHG AHKIHRHPGS IGNRKTPGRV YKGKKMAGHY GAERVTVMNL EVVDVIPEEN
LLLVKGAVPG PNGGLVIVRE TKKAAK
