RL10_THET8
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 25-MAY-2022, entry version 120.
DE RecName: Full=50S ribosomal protein L10;
GN Name=rplJ; OrderedLocusNames=TTHA0209;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; 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}.
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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 SMR; Q8VVE3; -.
DR IntAct; Q8VVE3; 52.
DR STRING; 300852.55771591; -.
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 OMA; VRDQKQA; -.
DR PhylomeDB; Q8VVE3; -.
DR EvolutionaryTrace; Q8VVE3; -.
DR Proteomes; UP000000532; Chromosome.
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 HAMAP; MF_00362; Ribosomal_L10; 1.
DR InterPro; IPR022973; Ribosomal_L10.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR PANTHER; PTHR11560; PTHR11560; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; SSF160369; 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="50S ribosomal protein L10"
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
