ID   RL11_SERMA              Reviewed;         142 AA.
AC   P09763;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NO1011;
RX   PubMed=3323840; DOI=10.1007/bf00337758;
RA   Sor F., Nomura M.;
RT   "Cloning and DNA sequence determination of the L11 ribosomal protein operon
RT   of Serratia marcescens and Proteus vulgaris: translational feedback
RT   regulation of the Escherichia coli L11 operon by heterologous L1
RT   proteins.";
RL   Mol. Gen. Genet. 210:52-59(1987).
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; X12584; CAA31095.1; -; Genomic_DNA.
DR   PIR; S01967; R5SE11.
DR   RefSeq; WP_004929911.1; NZ_WNKC01000011.1.
DR   AlphaFoldDB; P09763; -.
DR   SMR; P09763; -.
DR   STRING; 273526.SMDB11_4373; -.
DR   GeneID; 61123644; -.
DR   OrthoDB; 1702697at2; -.
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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..142
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104357"
SQ   SEQUENCE   142 AA;  14908 MW;  921DEB6FA97EEBED CRC64;
     MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT
     VYSDRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK VTRAQVREIA ETKAADMTGS
     DVEAMTRSIE GTARSMGLVV ED