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Database: UniProt
Entry: J3EQR2_9LACO
LinkDB: J3EQR2_9LACO
Original site: J3EQR2_9LACO 
ID   J3EQR2_9LACO            Unreviewed;       122 AA.
AC   J3EQR2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368};
GN   ORFNames=A11Y_26308 {ECO:0000313|EMBL:EJN55785.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55785.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN55785.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) 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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00368}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000256|ARBA:ARBA00007197, ECO:0000256|HAMAP-Rule:MF_00368}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJN55785.1}.
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DR   EMBL; AKFP01000033; EJN55785.1; -; Genomic_DNA.
DR   RefSeq; WP_003678659.1; NZ_AKFP01000033.1.
DR   AlphaFoldDB; J3EQR2; -.
DR   STRING; 1185325.A11Y_26308; -.
DR   GeneID; 65916599; -.
DR   PATRIC; fig|1185325.3.peg.1442; -.
DR   Proteomes; UP000007271; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; 3.30.1390.10; -; 1.
DR   Gene3D; 1.20.5.710; Single helix bin; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_bL12.
DR   InterPro; IPR013823; Ribosomal_bL12_C.
DR   InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR   InterPro; IPR008932; Ribosomal_bL12_oligo.
DR   InterPro; IPR036235; Ribosomal_bL12_oligo_N_sf.
DR   NCBIfam; TIGR00855; L12; 1.
DR   PANTHER; PTHR45987; 39S RIBOSOMAL PROTEIN L12; 1.
DR   PANTHER; PTHR45987:SF4; 39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
DR   SUPFAM; SSF48300; Ribosomal protein L7/12, oligomerisation (N-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007271};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00368};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00368}.
FT   DOMAIN          5..51
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          56..122
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
SQ   SEQUENCE   122 AA;  12294 MW;  4AAF688762A1F21F CRC64;
     MALDKDAIIA QLKEATILEL SDLVKGIEDE FGVSAAAPVA AAGAAGGDAA AAKTEFDVEL
     TGAGSAKIKV IKAVREITGA GLKDAKDMVD GAPTVIKEGV SEDEANELKA KLEEAGAEVT
     VK
//
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