ID   RL12_SACS2              Reviewed;         106 AA.
AC   P96040;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=50S ribosomal protein L12 {ECO:0000255|HAMAP-Rule:MF_01478};
GN   Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_01478}; Synonyms=rpl12Ab;
GN   OrderedLocusNames=SSO0342;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9252104; DOI=10.1016/s0167-4838(97)00073-3;
RA   Geiger M., Groebner P., Piendl W.;
RT   "Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12
RT   ribosomal proteins from the thermophilic archaeon Sulfolobus
RT   solfataricus.";
RL   Biochim. Biophys. Acta 1340:170-177(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U85262; AAB99527.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40672.1; -; Genomic_DNA.
DR   PIR; A90177; A90177.
DR   RefSeq; WP_009990630.1; NC_002754.1.
DR   AlphaFoldDB; P96040; -.
DR   SMR; P96040; -.
DR   STRING; 273057.SSO0342; -.
DR   EnsemblBacteria; AAK40672; AAK40672; SSO0342.
DR   GeneID; 44129313; -.
DR   KEGG; sso:SSO0342; -.
DR   PATRIC; fig|273057.12.peg.333; -.
DR   eggNOG; arCOG04287; Archaea.
DR   HOGENOM; CLU_114656_2_0_2; -.
DR   InParanoid; P96040; -.
DR   OMA; EYIYAAM; -.
DR   PhylomeDB; P96040; -.
DR   Proteomes; UP000001974; 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   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..106
FT                   /note="50S ribosomal protein L12"
FT                   /id="PRO_0000157637"
FT   REGION          66..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   106 AA;  11291 MW;  38879BB1C0861653 CRC64;
     MEYIYASLLL HSAKKEISED ALKNVLTAAG ISVDEVRLKA VVAALKEVNI DEVLKNAAAM
     PVAVAAQPQA TQAQPAAEEK KEEKKEEEKK GPSEEEIASG LASLFG