ID RL7_BIFAA Reviewed; 126 AA.
AC A1A033;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE AltName: Full=50S ribosomal protein L7/L12 {ECO:0000305};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=BAD_0285;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) 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; AP009256; BAF39066.1; -; Genomic_DNA.
DR RefSeq; WP_003807866.1; NC_008618.1.
DR AlphaFoldDB; A1A033; -.
DR SMR; A1A033; -.
DR STRING; 367928.BAD_0285; -.
DR PaxDb; 1680-BADO_0293; -.
DR GeneID; 56674348; -.
DR KEGG; bad:BAD_0285; -.
DR HOGENOM; CLU_086499_3_0_11; -.
DR Proteomes; UP000008702; Chromosome.
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_bL12; 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; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..126
FT /note="Large ribosomal subunit protein bL12"
FT /id="PRO_1000006963"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 126 AA; 13249 MW; AA79431D14D5DEFA CRC64;
MAKYTNDELL EAFGEMTLVE LSEFVKAFEE KFDVEAAAPV AAVAAAPAAG AAAEEEKDEF
DVILSAVGDK KIQVIKAVRA ITNLGLAEAK ALVDGAPKAV LEKAKKEDAE KAKSQLEEAG
ATVELK
//
