ID   RK12_PROWI              Reviewed;         130 AA.
AC   O99010;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=50S ribosomal protein L12, plastid;
GN   Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_00368};
OS   Prototheca wickerhamii.
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Prototheca.
OX   NCBI_TaxID=3111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=263-11;
RX   PubMed=12111556; DOI=10.1007/s00438-002-0681-6;
RA   Knauf U., Hachtel W.;
RT   "The genes encoding subunits of ATP synthase are conserved in the reduced
RT   plastid genome of the heterotrophic alga Prototheca wickerhamii.";
RL   Mol. Genet. Genomics 267:492-497(2002).
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. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC   -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S ribosomal
CC       subunit. Forms a multimeric L10(L12)X complex, where L10 forms an
CC       elongated spine to which 2 to 4 L12 dimers bind in a sequential
CC       fashion. Binds GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00368}.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB38448.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ236874; CAB38448.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; O99010; -.
DR   SMR; O99010; -.
DR   PRIDE; O99010; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   3: Inferred from homology;
KW   Plastid; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..130
FT                   /note="50S ribosomal protein L12, plastid"
FT                   /id="PRO_0000157623"
SQ   SEQUENCE   130 AA;  14135 MW;  523BA477D6E7E0F7 CRC64;
     MSATTLEILE KLKAITLLEA TELVSQIEKT FGVDASAPAV SGLRPILVEP IKQEDIIEEK
     TTFDVILEEV PSDKRVPILK VIRALTSLDL KQAKESITDL PKTILQGVSK EESEAAKQQL
     EAVGGKIKVS