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RL11_META1
ID   RL11_META1              Reviewed;         147 AA.
AC   B3PM28;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
GN   OrderedLocusNames=MARTH_orf144;
OS   Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=243272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=158L3-1;
RX   PubMed=18573899; DOI=10.1128/iai.00516-08;
RA   Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA   Loraine A.E.;
RT   "Genome of Mycoplasma arthritidis.";
RL   Infect. Immun. 76:4000-4008(2008).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC       Interacts with L10 and the large rRNA to form the base of the stalk.
CC       L10 forms an elongated spine to which L12 dimers bind in a sequential
CC       fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- PTM: One or more lysine residues are methylated. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR   EMBL; CP001047; ACF07080.1; -; Genomic_DNA.
DR   RefSeq; WP_012498037.1; NC_011025.1.
DR   AlphaFoldDB; B3PM28; -.
DR   SMR; B3PM28; -.
DR   STRING; 243272.MARTH_orf144; -.
DR   EnsemblBacteria; ACF07080; ACF07080; MARTH_orf144.
DR   KEGG; mat:MARTH_orf144; -.
DR   eggNOG; COG0080; Bacteria.
DR   HOGENOM; CLU_074237_2_2_14; -.
DR   OMA; CKQFNAK; -.
DR   OrthoDB; 1702697at2; -.
DR   Proteomes; UP000008812; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00349; Ribosomal_L11; 1.
DR   Gene3D; 1.10.10.250; -; 1.
DR   Gene3D; 3.30.1550.10; -; 1.
DR   HAMAP; MF_00736; Ribosomal_L11; 1.
DR   InterPro; IPR000911; Ribosomal_L11/L12.
DR   InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR   InterPro; IPR006519; Ribosomal_L11_bac-typ.
DR   InterPro; IPR020783; Ribosomal_L11_C.
DR   InterPro; IPR036769; Ribosomal_L11_C_sf.
DR   InterPro; IPR020785; Ribosomal_L11_CS.
DR   InterPro; IPR020784; Ribosomal_L11_N.
DR   PANTHER; PTHR11661; PTHR11661; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF46906; SSF46906; 1.
DR   SUPFAM; SSF54747; SSF54747; 1.
DR   TIGRFAMs; TIGR01632; L11_bact; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   3: Inferred from homology;
KW   Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..147
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_1000195677"
SQ   SEQUENCE   147 AA;  16262 MW;  81481AD7FCA74568 CRC64;
     MAKEIVRKAK LQFPAGQAKP GPALAGVGIN MPEFTKAFND QTRDRGQEPV PVLITVYKDK
     SFEFKLFTSP TAYKLTQIAK IKKGSSKANK EKVATITLDQ LKEIAEYKLP DLNTNNIDSA
     MRQIAGTAKQ MGIEIEGYAE WLKKGTN
 
 
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