ID RL10_THET8 Reviewed; 173 AA. AC Q8VVE3; Q5SLT4; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 127. DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000305}; DE AltName: Full=50S ribosomal protein L10; GN Name=rplJ; OrderedLocusNames=TTHA0209; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Huang Y., Sprinzl M.; RT "Ribosomal protein L12 and L10 from Thermus thermophilus, dissertation."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-11, AND BLOCKAGE OF N-TERMINUS. RX PubMed=11154066; DOI=10.1515/bc.2000.133; RA Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., RA Choli-Papadopoulou T.; RT "Identification of the 50S ribosomal proteins from the eubacterium Thermus RT thermophilus."; RL Biol. Chem. 381:1079-1087(2000). RN [4] RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY. RX PubMed=15923259; DOI=10.1073/pnas.0502193102; RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., RA Robinson C.V.; RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found RT by tandem MS of intact ribosomes from thermophilic bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005). RN [5] RP MASS SPECTROMETRY. RX PubMed=16287167; DOI=10.1002/pmic.200402111; RA Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.; RT "Extending ribosomal protein identifications to unsequenced bacterial RT strains using matrix-assisted laser desorption/ionization mass RT spectrometry."; RL Proteomics 5:4818-4831(2005). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in CC the interaction of the ribosome with GTP-bound translation factors. CC {ECO:0000305}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the ribosomal CC stalk which helps the ribosome interact with GTP-bound translation CC factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 CC forms an elongated spine to which 3 L12 dimers bind in a sequential CC fashion. {ECO:0000269|PubMed:15923259}. CC -!- PTM: The N-terminus is blocked. CC -!- MASS SPECTROMETRY: Mass=96075; Mass_error=13; Method=Electrospray; CC Note=Isolated L10(L12)6.; Evidence={ECO:0000269|PubMed:15923259}; CC -!- MASS SPECTROMETRY: Mass=18434; Mass_error=1; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:15923259}; CC -!- MASS SPECTROMETRY: Mass=18436; Method=MALDI; CC Evidence={ECO:0000269|PubMed:16287167}; CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family. CC {ECO:0000305}. CC -!- CAUTION: Note that in PubMed:11154066 it was found that the N-terminus CC is blocked, whereas the mass determined in PubMed:16287167 suggests CC that the initiator methionine is removed. No extra mass for a blocking CC group was found. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ419825; CAD11986.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70032.1; -; Genomic_DNA. DR RefSeq; WP_008630583.1; NC_006461.1. DR RefSeq; YP_143475.1; NC_006461.1. DR PDB; 4V51; X-ray; 2.80 A; J=2-173. DR PDB; 4V6F; X-ray; 3.10 A; DY=1-173. DR PDB; 4V7J; X-ray; 3.30 A; AJ/BJ=1-173. DR PDB; 4V7K; X-ray; 3.60 A; AJ/BJ=1-173. DR PDB; 4W2E; X-ray; 2.90 A; J=1-173. DR PDB; 4WPO; X-ray; 2.80 A; AK/CK=1-173. DR PDB; 4WQF; X-ray; 2.80 A; AK/CK=1-173. DR PDB; 4WQU; X-ray; 2.80 A; AK/CK=1-173. DR PDB; 4WQY; X-ray; 2.80 A; AK/CK=1-173. DR PDB; 5A9Z; EM; 4.70 A; AI=4-156. DR PDB; 5AA0; EM; 5.00 A; AI=4-156. DR PDB; 5HAU; X-ray; 3.00 A; 1J/2J=1-173. DR PDB; 5IMQ; EM; 3.80 A; 2=1-173. DR PDB; 5IMR; EM; -; 2=1-173. DR PDB; 5J8B; X-ray; 2.60 A; J=1-173. DR PDB; 5ZLU; EM; 3.60 A; e=1-173. DR PDB; 6GSL; X-ray; 3.16 A; 38=1-173. DR PDB; 6QNQ; X-ray; 3.50 A; 38=1-173. DR PDB; 6QNR; X-ray; 3.10 A; 38=1-173. DR PDBsum; 4V51; -. DR PDBsum; 4V6F; -. DR PDBsum; 4V7J; -. DR PDBsum; 4V7K; -. DR PDBsum; 4W2E; -. DR PDBsum; 4WPO; -. DR PDBsum; 4WQF; -. DR PDBsum; 4WQU; -. DR PDBsum; 4WQY; -. DR PDBsum; 5A9Z; -. DR PDBsum; 5AA0; -. DR PDBsum; 5HAU; -. DR PDBsum; 5IMQ; -. DR PDBsum; 5IMR; -. DR PDBsum; 5J8B; -. DR PDBsum; 5ZLU; -. DR PDBsum; 6GSL; -. DR PDBsum; 6QNQ; -. DR PDBsum; 6QNR; -. DR AlphaFoldDB; Q8VVE3; -. DR EMDB; EMD-6934; -. DR SMR; Q8VVE3; -. DR IntAct; Q8VVE3; 52. DR EnsemblBacteria; BAD70032; BAD70032; BAD70032. DR GeneID; 3168578; -. DR KEGG; ttj:TTHA0209; -. DR PATRIC; fig|300852.9.peg.207; -. DR eggNOG; COG0244; Bacteria. DR HOGENOM; CLU_092227_1_2_0; -. DR PhylomeDB; Q8VVE3; -. DR EvolutionaryTrace; Q8VVE3; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd05797; Ribosomal_L10; 1. DR Gene3D; 3.30.70.1730; -; 1. DR Gene3D; 6.10.250.290; -; 1. DR HAMAP; MF_00362; Ribosomal_uL10; 1. DR InterPro; IPR001790; Ribosomal_uL10. DR InterPro; IPR043141; Ribosomal_uL10-like_sf. DR InterPro; IPR022973; Ribosomal_uL10_bac. DR InterPro; IPR047865; Ribosomal_uL10_bac_type. DR PANTHER; PTHR11560; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1. DR PANTHER; PTHR11560:SF8; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1. DR Pfam; PF00466; Ribosomal_L10; 1. DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11154066" FT CHAIN 2..173 FT /note="Large ribosomal subunit protein uL10" FT /id="PRO_0000154736" FT CONFLICT 127..128 FT /note="EL -> DV (in Ref. 1; CAD11986)" FT /evidence="ECO:0000305" FT CONFLICT 137..138 FT /note="EL -> DV (in Ref. 1; CAD11986)" FT /evidence="ECO:0000305" FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:4W2E" FT TURN 11..16 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:4W2E" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:4W2E" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:4W2E" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:4V6F" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:4V7J" FT TURN 88..91 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:4V7J" FT TURN 105..111 FT /evidence="ECO:0007829|PDB:4W2E" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:4W2E" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:4V6F" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:4W2E" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:4V6F" SQ SEQUENCE 173 AA; 18566 MW; 266CF72B036C6D5F CRC64; MPNKRNVELL ATLKENLERA QGSFFLVNYQ GLPAKETHAL RQALKQNGAR LFVAKNTLIR LALKELGLPE LDGLQGPSAV VFYEDPVAAA KTLVQFAKSN PKGIPQVKSG LLQGQILTAK DVEALAELPT MDELRAELVG VLQAPMAELV GVLGGVAREL VGILEAYAEK KAA //