RL7_THET8
ID RL7_THET8 Reviewed; 125 AA.
AC Q8VVE2; Q5SLT3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=TTHA0210;
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 2-30.
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, PHOSPHORYLATION, 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11511350; DOI=10.1016/s0092-8674(01)00435-4;
RA Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.;
RT "The path of messenger RNA through the ribosome.";
RL Cell 106:233-241(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
RX PubMed=11283358; DOI=10.1126/science.1060089;
RA Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N.,
RA Cate J.H.D., Noller H.F.;
RT "Crystal structure of the ribosome at 5.5 A resolution.";
RL Science 292:883-896(2001).
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. It extends beyond the surface of the 70S
CC ribosome. The stalk is preferentially stabilized in 70S versus 50S
CC crystals.
CC -!- SUBUNIT: Homodimer. Part of the 50S ribosomal subunit; present in 6
CC copies per ribosome. Forms part of the ribosomal stalk which helps the
CC ribosome interact with GTP-bound translation factors. Forms a
CC heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated
CC spine to which 3 L12 dimers bind in a sequential fashion. Contacts
CC protein L11. {ECO:0000269|PubMed:15923259}.
CC -!- PTM: The ion at m/z 13016 is probably phosphorylated; treatment with
CC phosphatase in the presence of kinase inhibitors decreases it weight.
CC This form is only detected on 70S ribosomes and not in isolated
CC ribosomal stalk complexes. {ECO:0000269|PubMed:15923259}.
CC -!- PTM: The ion at m/z 12978 is suggested to be the N-acetylated form of
CC the protein (L7). The ion at m/z 12964 is suggested to be consistent
CC with dimethylation or formylation and is present in very small
CC quantities in the sample.
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=77670; Mass_error=9; Method=Electrospray;
CC Note=Isolated (L12)6.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=13016; Mass_error=1.9; Method=Electrospray;
CC Note=Probably phosphorylated, more strongly associated with the 50S
CC ribosomal subunit.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=12936; Mass_error=0.5; Method=Electrospray;
CC Note=Not phosphorylated.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=12937; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287167};
CC -!- MASS SPECTROMETRY: Mass=12964; Method=MALDI; Note=May be N-acetylated.;
CC Evidence={ECO:0000269|PubMed:16287167};
CC -!- MASS SPECTROMETRY: Mass=12978; Method=MALDI; Note=May be dimethylated
CC or formylated.; Evidence={ECO:0000269|PubMed:16287167};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR EMBL; AJ419825; CAD11987.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70033.1; -; Genomic_DNA.
DR RefSeq; WP_008630582.1; NC_006461.1.
DR RefSeq; YP_143476.1; NC_006461.1.
DR PDB; 4V42; X-ray; 5.50 A; BI/BJ=32-125.
DR PDB; 4V4P; X-ray; 5.50 A; I/J=32-125.
DR PDB; 4V51; X-ray; 2.80 A; L/M=2-125.
DR PDB; 4V6F; X-ray; 3.10 A; DI/DJ=1-125.
DR PDB; 6GSL; X-ray; 3.16 A; 18/28=1-125.
DR PDBsum; 4V42; -.
DR PDBsum; 4V4P; -.
DR PDBsum; 4V51; -.
DR PDBsum; 4V6F; -.
DR PDBsum; 6GSL; -.
DR AlphaFoldDB; Q8VVE2; -.
DR SMR; Q8VVE2; -.
DR IntAct; Q8VVE2; 1.
DR STRING; 300852.55771592; -.
DR EnsemblBacteria; BAD70033; BAD70033; BAD70033.
DR GeneID; 3168576; -.
DR KEGG; ttj:TTHA0210; -.
DR PATRIC; fig|300852.9.peg.208; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_0; -.
DR OMA; LEDKWGV; -.
DR PhylomeDB; Q8VVE2; -.
DR EvolutionaryTrace; Q8VVE2; -.
DR Proteomes; UP000000532; 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; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11154066"
FT CHAIN 2..125
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157597"
FT CONFLICT 77..78
FT /note="EL -> DV (in Ref. 1; CAD11987)"
FT /evidence="ECO:0000305"
FT TURN 2..7
FT /evidence="ECO:0007829|PDB:4V6F"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:4V6F"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:4V6F"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4V6F"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4V6F"
SQ SEQUENCE 125 AA; 13067 MW; 3919CBF76605AC87 CRC64;
MALDIERIKE ELSQATVLEL KQLIDALKEA WGVTAAAPVA VAAAPAAGAA AAPAEEKTEF
DVILKEAGAK KLEVIKELRA ITGLGLKEAK DLAEKGGPVK EGVSKQEAEE IKKKLEAVGA
VVELK
