ID   RK12_GRATL              Reviewed;         131 AA.
AC   Q6B905;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=50S ribosomal protein L12, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00368};
GN   Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=Grc000049;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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, chloroplast.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR   EMBL; AY673996; AAT79630.1; -; Genomic_DNA.
DR   RefSeq; YP_063555.1; NC_006137.1.
DR   AlphaFoldDB; Q6B905; -.
DR   SMR; Q6B905; -.
DR   GeneID; 2944036; -.
DR   GO; GO:0009507; C:chloroplast; 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:UniProtKB-UniRule.
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   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..131
FT                   /note="50S ribosomal protein L12, chloroplastic"
FT                   /id="PRO_0000157618"
FT   REGION          106..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  14410 MW;  8418E448E10696CD CRC64;
     MNTKITNIIE DLKSLTLLEA AELIKQIEET FDVDASITSQ SQAIVMPTAV DNSNKNEIEE
     KTEFDIILEE VPAAKKIAIL KVVRSITGLG LKEAKALVES APKMIKDNTN KENSEEIKQQ
     LEEAGAKVSI K