RL7_DESVM
ID RL7_DESVM Reviewed; 127 AA.
AC P02393; B8DLM6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=DvMF_1454;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
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 Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-127, AND METHYLATION AT LYS-77 AND LYS-88.
RA Itoh T., Otaka E.;
RT "Complete amino-acid sequence of an L7/L12-type ribosomal protein from
RT Desulfovibrio vulgaris, Miyazaki.";
RL Biochim. Biophys. Acta 789:229-233(1984).
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; CP001197; ACL08402.1; -; Genomic_DNA.
DR PIR; A02769; R5DV7.
DR RefSeq; WP_012612583.1; NC_011769.1.
DR AlphaFoldDB; P02393; -.
DR SMR; P02393; -.
DR STRING; 883.DvMF_1454; -.
DR EnsemblBacteria; ACL08402; ACL08402; DvMF_1454.
DR KEGG; dvm:DvMF_1454; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_0_7; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1822695at2; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Methylation; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..127
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157527"
FT MOD_RES 77
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 88
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.2"
FT CONFLICT 42..43
FT /note="AM -> MA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 13344 MW; F157103261E081C9 CRC64;
MSSITKEQVV EFIANMTVLE LSEFIKELEE KFGVSAAAPA MAMVAAGPAE AAPAEEEKTE
FDVILKAAGA NKIGVIKVVR ALTGLGLKEA KDKVDGAPST LKEAVSKEEA EEAKKQLVEA
GAEVEVK
