ID   RL7_MICLU               Reviewed;         118 AA.
AC   P02395;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE   AltName: Full=MA1/MA2;
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX   PubMed=7250376; DOI=10.1016/0014-5793(81)80342-0;
RA   Itoh T.;
RT   "Primary structure of an acidic ribosomal protein from Micrococcus
RT   lysodeikticus.";
RL   FEBS Lett. 127:67-70(1981).
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   -!- PTM: Acetylation of Met-1 converts MA1 to MA2.
CC       {ECO:0000269|PubMed:7250376}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
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   PIR; A02771; R7MCML.
DR   AlphaFoldDB; P02395; -.
DR   SMR; P02395; -.
DR   iPTMnet; P02395; -.
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   Acetylation; Direct protein sequencing; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..118
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_0000157548"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in form MA2"
FT                   /evidence="ECO:0000269|PubMed:7250376"
SQ   SEQUENCE   118 AA;  12372 MW;  09BA7F548B278946 CRC64;
     MNKEQILEAI KAMTVLELND LVKAIEEEFG VTAAAPVVAG GAAAAAEEKT EFDVVLASAG
     AEKIKVIKVV REITGLGLKE AKEVVDNAPK ALKEGVSKDE AEEIKAKLEE VGASVEVK