ID   RL12_METVA              Reviewed;          99 AA.
AC   P10623;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=50S ribosomal protein L12 {ECO:0000255|HAMAP-Rule:MF_01478};
GN   Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_01478};
OS   Methanococcus vannielii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2834382; DOI=10.1016/s0021-9258(18)68675-2;
RA   Strobel O., Koepke A.K.E., Kamp R.M., Boeck A., Wittmann-Liebold B.;
RT   "Primary structure of the archaebacterial Methanococcus vannielii ribosomal
RT   protein L12. Amino acid sequence determination, oligonucleotide
RT   hybridization, and sequencing of the gene.";
RL   J. Biol. Chem. 263:6538-6546(1988).
RN   [2]
RP   SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX   PubMed=20467040; DOI=10.1074/mcp.m000072-mcp201;
RA   Gordiyenko Y., Videler H., Zhou M., McKay A.R., Fucini P., Biegel E.,
RA   Muller V., Robinson C.V.;
RT   "Mass spectrometry defines the stoichiometry of ribosomal stalk complexes
RT   across the phylogenetic tree.";
RL   Mol. Cell. Proteomics 9:1774-1783(2010).
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:0000255|HAMAP-Rule:MF_01478}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Homodimer, it forms part of
CC       the ribosomal stalk which helps the ribosome interact with GTP-bound
CC       translation factors. Forms both a pentameric L10(L12)2(L12)2 and
CC       heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated
CC       spine to which the L12 dimers bind in a sequential fashion. The
CC       proportion of heptameric complexes increases during cell growth.
CC       {ECO:0000269|PubMed:20467040}.
CC   -!- MASS SPECTROMETRY: Mass=95405.27; Mass_error=23.6; Method=Electrospray;
CC       Note=Isolated L10(L12)6.; Evidence={ECO:0000269|PubMed:20467040};
CC   -!- MASS SPECTROMETRY: Mass=75342.7; Mass_error=20.7; Method=Electrospray;
CC       Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:20467040};
CC   -!- MASS SPECTROMETRY: Mass=9819.7; Mass_error=2.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20467040};
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01478}.
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DR   EMBL; J03187; AAA72191.1; -; Genomic_DNA.
DR   PIR; B28152; R6MXL2.
DR   AlphaFoldDB; P10623; -.
DR   SMR; P10623; -.
DR   GeneID; 5324705; -.
DR   OMA; EYIYAAM; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR   InterPro; IPR022295; Ribosomal_L12_arc.
DR   TIGRFAMs; TIGR03685; ribo_P1_arch; 1.
PE   1: Evidence at protein level;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..99
FT                   /note="50S ribosomal protein L12"
FT                   /id="PRO_0000157633"
SQ   SEQUENCE   99 AA;  9818 MW;  94E91B61C201BED2 CRC64;
     MEYIYAALLL NSANKEVTEE AVKAVLVAGG IEANDARVKA LVAALEGVDI AEAIAKAAIA
     PVAAAAPVAA AAAPAEVKKE EKKEDTTAAA AAGLGALFM