ID   RL7_STRVG               Reviewed;         127 AA.
AC   P48936;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 88.
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 virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675024; DOI=10.1016/0378-1119(96)00067-4;
RA   Katayama M., Sakai Y., Okamoto S., Ihara F., Nihira T., Yamada Y.;
RT   "Gene organization in the ada-rplL region of Streptomyces virginiae.";
RL   Gene 171:135-136(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA09305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D50624; BAA09305.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_033225047.1; NZ_JNYC01000038.1.
DR   AlphaFoldDB; P48936; -.
DR   SMR; P48936; -.
DR   STRING; 1961.JOAK01000021_gene7133; -.
DR   eggNOG; COG0222; Bacteria.
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   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..127
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_0000157594"
SQ   SEQUENCE   127 AA;  13225 MW;  5CB5F0752C95ECBB CRC64;
     MAKLSQDDLL AQFEEMTLIE LSEFVKAFEE KFDVTAAAAV AVAGPAGVGA APEAAEEQDE
     FDVILTGAGD KKIQVIKVVR ELTSLGLKEA KDLVDGAPKP VLEKVAKEAA DKAAESLKAA
     GAAVEVK