ID   RL12_AERPE              Reviewed;         111 AA.
AC   Q9Y9W9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=50S ribosomal protein L12 {ECO:0000255|HAMAP-Rule:MF_01478};
GN   Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_01478}; OrderedLocusNames=APE_2170;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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 a heptameric L10(L12)2(L12)2(L12)2 complex,
CC       where L10 forms an elongated spine to which the L12 dimers bind in a
CC       sequential fashion. {ECO:0000255|HAMAP-Rule:MF_01478}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01478}.
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DR   EMBL; BA000002; BAA81181.1; -; Genomic_DNA.
DR   PIR; E72524; E72524.
DR   PDB; 5YT0; X-ray; 1.89 A; B=91-111.
DR   PDB; 6JI2; X-ray; 3.00 A; X=95-111.
DR   PDBsum; 5YT0; -.
DR   PDBsum; 6JI2; -.
DR   AlphaFoldDB; Q9Y9W9; -.
DR   SMR; Q9Y9W9; -.
DR   STRING; 272557.APE_2170; -.
DR   EnsemblBacteria; BAA81181; BAA81181; APE_2170.
DR   KEGG; ape:APE_2170; -.
DR   eggNOG; arCOG04287; Archaea.
DR   OMA; EYIYAAM; -.
DR   Proteomes; UP000002518; Chromosome.
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   CDD; cd05832; Ribosomal_L12p; 1.
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   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..111
FT                   /note="50S ribosomal protein L12"
FT                   /id="PRO_0000157625"
FT   REGION          75..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:5YT0"
SQ   SEQUENCE   111 AA;  11794 MW;  2330740B03C6412A CRC64;
     MAQEGKAYIH LALAIYYAGG KIDEETLKKA AEAIGMQVDE AKIKMLVASL EEVNLEEVLK
     QAVAAPVAAA AAAPAAAPAA EEKAEEEKKE EEEEKKEEEV DLSGLSGMFG F