ID   RL7_CAMJD               Reviewed;         125 AA.
AC   A7H4Q6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
GN   OrderedLocusNames=JJD26997_1457;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) 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; CP000768; ABS44165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H4Q6; -.
DR   SMR; A7H4Q6; -.
DR   EnsemblBacteria; ABS44165; ABS44165; JJD26997_1457.
DR   KEGG; cjd:JJD26997_1457; -.
DR   HOGENOM; CLU_086499_3_2_7; -.
DR   OMA; LEDKWGV; -.
DR   Proteomes; UP000002302; 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..125
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_1000006982"
SQ   SEQUENCE   125 AA;  13045 MW;  186CDE6D9D921238 CRC64;
     MAISKEDVLE YISNLSVLEL SELVKEFEEK FGVSAVPVMV AGGAAAGGAA AAAEEKTEFD
     IVLTDGGAKK IEVIKIVRAL TGLGLKEAKD AVEQTPSTLK EGVAKAEAEE AKKQLEEAGA
     KVELK