RL7_THEMA
ID RL7_THEMA Reviewed; 128 AA.
AC P29396;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=TM_0457;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=1429627; DOI=10.1016/s0021-9258(18)50016-8;
RA Liao D., Dennis P.P.;
RT "The organization and expression of essential transcription translation
RT component genes in the extremely thermophilic eubacterium Thermotoga
RT maritima.";
RL J. Biol. Chem. 267:22787-22797(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8177738; DOI=10.1093/nar/21.21.4904;
RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., Lottspeich F.,
RA Zillig W.;
RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; characterisation
RT of the enzyme and the DNA-sequence of the genes for the large subunits.";
RL Nucleic Acids Res. 21:4904-4908(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10637222; DOI=10.1093/emboj/19.2.174;
RA Wahl M.C., Bourenkov G.P., Bartunik H.D., Huber R.;
RT "Flexibility, conformational diversity and two dimerization modes in
RT complexes of ribosomal protein L12.";
RL EMBO J. 19:174-186(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-30, INTERACTION WITH L10 (RPLJ),
RP AND SUBUNIT.
RX PubMed=15989950; DOI=10.1016/j.cell.2005.04.015;
RA Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M.,
RA Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.;
RT "Structural basis for the function of the ribosomal L7/12 stalk in factor
RT binding and GTPase activation.";
RL Cell 121:991-1004(2005).
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.
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.
CC {ECO:0000269|PubMed:15923259, ECO:0000269|PubMed:15989950}.
CC -!- MASS SPECTROMETRY: Mass=101376; Mass_error=8; Method=Electrospray;
CC Note=Isolated L10(L12)6.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=13477; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15923259};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35540.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z11839; CAA77862.1; -; Genomic_DNA.
DR EMBL; X72695; CAA51245.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35540.1; ALT_INIT; Genomic_DNA.
DR PIR; E44466; R7HG12.
DR RefSeq; NP_228267.1; NC_000853.1.
DR RefSeq; WP_004081509.1; NZ_CP011107.1.
DR PDB; 1DD3; X-ray; 2.00 A; A/B=1-128, C/D=1-32.
DR PDB; 1DD4; X-ray; 2.40 A; A/B=1-128, C/D=1-40.
DR PDB; 1ZAV; X-ray; 1.90 A; U/V/W/X/Y/Z=1-30.
DR PDB; 1ZAW; X-ray; 2.30 A; U/V/W/X/Y/Z=1-30.
DR PDB; 1ZAX; X-ray; 2.10 A; U/V/W/X/Y/Z=1-30.
DR PDB; 4V42; X-ray; 5.50 A; BI/BJ=1-128.
DR PDBsum; 1DD3; -.
DR PDBsum; 1DD4; -.
DR PDBsum; 1ZAV; -.
DR PDBsum; 1ZAW; -.
DR PDBsum; 1ZAX; -.
DR PDBsum; 4V42; -.
DR AlphaFoldDB; P29396; -.
DR SMR; P29396; -.
DR IntAct; P29396; 1.
DR STRING; 243274.THEMA_02405; -.
DR EnsemblBacteria; AAD35540; AAD35540; TM_0457.
DR KEGG; tma:TM0457; -.
DR PATRIC; fig|243274.5.peg.464; -.
DR eggNOG; COG0222; Bacteria.
DR InParanoid; P29396; -.
DR OMA; LEDKWGV; -.
DR EvolutionaryTrace; P29396; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
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; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..128
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157596"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1ZAV"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:1ZAV"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:1DD3"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:1DD3"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1DD3"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:1DD3"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1DD3"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1DD3"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:1DD3"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1DD3"
SQ SEQUENCE 128 AA; 13458 MW; FCA849CFE85906BE CRC64;
MTIDEIIEAI EKLTVSELAE LVKKLEDKFG VTAAAPVAVA AAPVAGAAAG AAQEEKTEFD
VVLKSFGQNK IQVIKVVREI TGLGLKEAKD LVEKAGSPDA VIKSGVSKEE AEEIKKKLEE
AGAEVELK
