ID A0A1G9KQE1_9ACTN Unreviewed; 143 AA.
AC A0A1G9KQE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000256|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000256|HAMAP-Rule:MF_00736};
GN ORFNames=SAMN04488242_1766 {ECO:0000313|EMBL:SDL51677.1};
OS Tessaracoccus oleiagri.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=686624 {ECO:0000313|EMBL:SDL51677.1, ECO:0000313|Proteomes:UP000199475};
RN [1] {ECO:0000313|EMBL:SDL51677.1, ECO:0000313|Proteomes:UP000199475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9159 {ECO:0000313|EMBL:SDL51677.1,
RC ECO:0000313|Proteomes:UP000199475};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. {ECO:0000256|HAMAP-
CC Rule:MF_00736, ECO:0000256|RuleBase:RU003979}.
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:0000256|HAMAP-
CC Rule:MF_00736}.
CC -!- PTM: One or more lysine residues are methylated. {ECO:0000256|HAMAP-
CC Rule:MF_00736, ECO:0000256|RuleBase:RU003979}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000256|ARBA:ARBA00010537, ECO:0000256|HAMAP-Rule:MF_00736,
CC ECO:0000256|RuleBase:RU003978}.
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DR EMBL; FNGP01000003; SDL51677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9KQE1; -.
DR STRING; 686624.SAMN04488242_1766; -.
DR OrthoDB; 9802408at2; -.
DR Proteomes; UP000199475; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein L11, C-terminal domain; 1.
DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_uL11.
DR InterPro; IPR006519; Ribosomal_uL11_bac-typ.
DR InterPro; IPR020783; Ribosomal_uL11_C.
DR InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR InterPro; IPR020785; Ribosomal_uL11_CS.
DR InterPro; IPR020784; Ribosomal_uL11_N.
DR InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR NCBIfam; TIGR01632; L11_bact; 1.
DR PANTHER; PTHR11661:SF1; 39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 3: Inferred from homology;
KW Methylation {ECO:0000256|HAMAP-Rule:MF_00736,
KW ECO:0000256|RuleBase:RU003979};
KW Reference proteome {ECO:0000313|Proteomes:UP000199475};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00736};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00736};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00736};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00736}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..143
FT /note="Large ribosomal subunit protein uL11"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011597917"
FT DOMAIN 11..68
FT /note="Large ribosomal subunit protein uL11 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03946"
FT DOMAIN 73..141
FT /note="Large ribosomal subunit protein uL11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00298"
SQ SEQUENCE 143 AA; 15070 MW; ED3516E79AB960E3 CRC64;
MPPKKKVSAI VKIALNAGAA TPAPPVGTAL GPHGVNMMEF VKAYNAQTES QRGNVIPVEI
TIYEDRTFTF VTKTPPAAEL IKKAAGISKG SGSPLKEKVG KLTKAQVREI AETKLPDLNA
NDVDAAMKIV EGTARQMGVT ITD
//
