RL7_ACIF5
ID RL7_ACIF5 Reviewed; 128 AA.
AC B5ELX1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=Lferr_0489;
OS Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS (Leptospirillum ferrooxidans (ATCC 53993)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=380394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53993 / BNL-5-31;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Borole A.P.;
RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL Submitted (AUG-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; CP001132; ACH82743.1; -; Genomic_DNA.
DR RefSeq; WP_009568779.1; NC_011206.1.
DR AlphaFoldDB; B5ELX1; -.
DR SMR; B5ELX1; -.
DR GeneID; 66431375; -.
DR KEGG; afe:Lferr_0489; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_6; -.
DR OMA; LEDKWGV; -.
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..128
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_1000121380"
SQ SEQUENCE 128 AA; 12814 MW; 6BD47DEAF1FC1616 CRC64;
MALSKAEILD AIAGMTVLEL SELIKEMEEK FGVSAAAVAV AAPAGGAAAG EGAAAVEEQT
EFDVILTAAG ANKVNTIKVV RAITGLGLKE AKDLVDGAPK PVKEGVAKAE AESVKAQLVE
AGAEAEIK