ID A0A1G7MMR3_9BACT Unreviewed; 144 AA.
AC A0A1G7MMR3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN05444167_2851 {ECO:0000313|EMBL:SDF63027.1};
OS Terriglobus roseus.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=392734 {ECO:0000313|EMBL:SDF63027.1, ECO:0000313|Proteomes:UP000182427};
RN [1] {ECO:0000313|EMBL:SDF63027.1, ECO:0000313|Proteomes:UP000182427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS232 {ECO:0000313|EMBL:SDF63027.1,
RC ECO:0000313|Proteomes:UP000182427};
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; LT629690; SDF63027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7MMR3; -.
DR OrthoDB; 9802408at2; -.
DR Proteomes; UP000182427; Chromosome i.
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; 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.
PE 3: Inferred from homology;
KW Methylation {ECO:0000256|HAMAP-Rule:MF_00736,
KW ECO:0000256|RuleBase:RU003979};
KW Reference proteome {ECO:0000313|Proteomes:UP000182427};
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|HAMAP-Rule:MF_00736,
KW ECO:0000256|RuleBase:RU003979};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00736,
KW ECO:0000256|RuleBase:RU003979}.
FT DOMAIN 10..69
FT /note="Large ribosomal subunit protein uL11 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03946"
FT DOMAIN 74..142
FT /note="Large ribosomal subunit protein uL11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00298"
SQ SEQUENCE 144 AA; 15224 MW; E04EB90E55433556 CRC64;
MAPKKITGYV KLQVMAGKAT PAPPIGPALG QAQVNIMEFC KQFNDRTKDP SMAGLTIPVV
ISVYADRTFS FITKTPPAPV LLKKAAKIEK GSGTPNKAKV GTVTEAQVRE IATQKMPDLN
AATVEAAIKM IKGTARSMGL DVVV
//
