ID   RL7_ACTP7               Reviewed;         122 AA.
AC   B3GYU7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=APP7_1781;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE62433.1; -; Genomic_DNA.
DR   RefSeq; WP_005599214.1; NC_010939.1.
DR   AlphaFoldDB; B3GYU7; -.
DR   SMR; B3GYU7; -.
DR   EnsemblBacteria; ACE62433; ACE62433; APP7_1781.
DR   GeneID; 66258478; -.
DR   KEGG; apa:APP7_1781; -.
DR   HOGENOM; CLU_086499_3_2_6; -.
DR   OMA; LEDKWGV; -.
DR   BioCyc; APLE537457:APP7_RS09245-MON; -.
DR   Proteomes; UP000001226; Chromosome.
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   CHAIN           1..122
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_1000121381"
SQ   SEQUENCE   122 AA;  12329 MW;  8BD356062C25C2E7 CRC64;
     MSLTNEQLIE AIASKSVSEI VELIAAMEEK FGVSAAAAVA AAPAAGAAAA EEKTEFDVIL
     AEAGANKVAV IKAVRGATGL GLKEAKDLVE SAPAALKEGI SKPEAEALKK ELEEAGAKVE
     IK