ID   RL7_STRGR               Reviewed;         127 AA.
AC   P02396; P36259;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE            Short=SA1;
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N2-3-11;
RX   PubMed=8039667; DOI=10.1111/j.1574-6968.1994.tb06863.x;
RA   Kuberski S., Kasberg T., Distler J.;
RT   "The nusG gene of Streptomyces griseus: cloning of the gene and analysis of
RT   the A-factor binding properties of the gene product.";
RL   FEMS Microbiol. Lett. 119:33-39(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-127.
RA   Itoh T., Sugiyama M., Higo K.;
RT   "The primary structure of an acidic ribosomal protein from Streptomyces
RT   griseus.";
RL   Biochim. Biophys. Acta 701:164-172(1982).
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   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR   EMBL; X72787; CAA51301.1; -; Genomic_DNA.
DR   PIR; S32239; R7SMG.
DR   RefSeq; WP_003966996.1; NZ_UAVD01000027.1.
DR   AlphaFoldDB; P02396; -.
DR   SMR; P02396; -.
DR   GeneID; 6215549; -.
DR   OMA; LEDKWGV; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..127
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_0000157587"
FT   CONFLICT        54
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   127 AA;  13271 MW;  9AB57720E67ED8EC CRC64;
     MAKLSQDDLL AQFEEMTLIE LSEFVKAFEE KFDVTAAAAV AVAGPAAGGA PAEAEAEQDE
     FDVILTGAGE KKIQVIKVVR ELTSLGLKEA KDLVDGTPKP VLEKVAKEAA EKAAESLKAA
     GASVEVK