RL7_ACAM1
ID RL7_ACAM1 Reviewed; 129 AA.
AC B0CAD2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
GN Synonyms=rpl12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN OrderedLocusNames=AM1_2868;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW27867.1; -; Genomic_DNA.
DR RefSeq; WP_012163306.1; NC_009925.1.
DR AlphaFoldDB; B0CAD2; -.
DR SMR; B0CAD2; -.
DR STRING; 329726.AM1_2868; -.
DR EnsemblBacteria; ABW27867; ABW27867; AM1_2868.
DR KEGG; amr:AM1_2868; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_0_3; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1822695at2; -.
DR Proteomes; UP000000268; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..129
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_1000079778"
FT REGION 95..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 129 AA; 13388 MW; B114767BDC31AD2E CRC64;
MSATEEILEK LKSLTLLEAA DLVKQIEETF GVSAAPAAGV MMAAPGAGGA AGGEEAEEKT
EFDVVLEEVP SDKKIAVLKV VRTLTGLGLK EAKEMVESTP KSIKEGVSKE DAEEAKKSLE
DAGGKASLK