RL12_PYRHO
ID RL12_PYRHO Reviewed; 108 AA.
AC O57705;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=50S ribosomal protein L12 {ECO:0000255|HAMAP-Rule:MF_01478};
DE AltName: Full=Acidic ribosomal protein P1 homolog;
GN Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_01478}; OrderedLocusNames=PH1998;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17804412; DOI=10.1074/jbc.m705412200;
RA Maki Y., Hashimoto T., Zhou M., Naganuma T., Ohta J., Nomura T.,
RA Robinson C.V., Uchiumi T.;
RT "Three binding sites for stalk protein dimers are generally present in
RT ribosomes from archaeal organism.";
RL J. Biol. Chem. 282:32827-32833(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 1-58, AND SUBUNIT.
RX PubMed=20007716; DOI=10.1074/jbc.m109.068098;
RA Naganuma T., Nomura N., Yao M., Mochizuki M., Uchiumi T., Tanaka I.;
RT "Structural basis for translation factor recruitment to the
RT eukaryotic/archaeal ribosomes.";
RL J. Biol. Chem. 285:4747-4756(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. The
CC stalk complex of P.horikoshii binds to E.coli large subunits and
CC confers on them the ability to interact with eukaryotic elongation
CC factors. Each succesive L12 dimer bound along the P0 spine increases
CC the GTPase activity of elongation factors and increases translation by
CC reconsituted ribosomes. {ECO:0000255|HAMAP-Rule:MF_01478,
CC ECO:0000269|PubMed:17804412}.
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 P0(L12)2(L12)2(L12)2 complex,
CC where P0 forms an elongated spine to which the L12 dimers bind in a
CC sequential fashion. {ECO:0000269|PubMed:17804412,
CC ECO:0000269|PubMed:20007716}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01478}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31125.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA31125.1; ALT_INIT; Genomic_DNA.
DR PIR; F71216; F71216.
DR RefSeq; WP_010886059.1; NC_000961.1.
DR PDB; 3A1Y; X-ray; 2.13 A; A/B/C/D/E/F=1-58.
DR PDB; 3WY9; X-ray; 2.30 A; C/D=77-108.
DR PDB; 5H7L; X-ray; 3.10 A; E/G=98-108.
DR PDBsum; 3A1Y; -.
DR PDBsum; 3WY9; -.
DR PDBsum; 5H7L; -.
DR AlphaFoldDB; O57705; -.
DR SMR; O57705; -.
DR STRING; 70601.3258442; -.
DR EnsemblBacteria; BAA31125; BAA31125; BAA31125.
DR GeneID; 1442841; -.
DR KEGG; pho:PH1998; -.
DR eggNOG; arCOG04287; Archaea.
DR OMA; EYIYAAM; -.
DR OrthoDB; 128352at2157; -.
DR EvolutionaryTrace; O57705; -.
DR Proteomes; UP000000752; 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; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..108
FT /note="50S ribosomal protein L12"
FT /id="PRO_0000157635"
FT REGION 67..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3A1Y"
FT HELIX 84..106
FT /evidence="ECO:0007829|PDB:3WY9"
SQ SEQUENCE 108 AA; 11403 MW; CE3E35D79FCAAA82 CRC64;
MEYVYAALLL HSVGKEINEE NLKAVLQAAG VEPEEARIKA LVAALEGVNI DEVIEKAAMP
VAVAAAPAAA PAEAGGEEKK EEEKKEEEEK EEEVSEEEAL AGLSALFG
