ID A0A1T4W762_9FIRM Unreviewed; 141 AA.
AC A0A1T4W762;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=SAMN02745178_00045 {ECO:0000313|EMBL:SKA72949.1};
OS Gemmiger formicilis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX NCBI_TaxID=745368 {ECO:0000313|EMBL:SKA72949.1, ECO:0000313|Proteomes:UP000190286};
RN [1] {ECO:0000313|EMBL:SKA72949.1, ECO:0000313|Proteomes:UP000190286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27749 {ECO:0000313|EMBL:SKA72949.1,
RC ECO:0000313|Proteomes:UP000190286};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYF01000001; SKA72949.1; -; Genomic_DNA.
DR RefSeq; WP_007046678.1; NZ_WQOH01000021.1.
DR AlphaFoldDB; A0A1T4W762; -.
DR STRING; 745368.SAMN02745178_00045; -.
DR GeneID; 78308204; -.
DR OrthoDB; 9802408at2; -.
DR Proteomes; UP000190286; 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; 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:UP000190286};
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 9..66
FT /note="Large ribosomal subunit protein uL11 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03946"
FT DOMAIN 71..139
FT /note="Large ribosomal subunit protein uL11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00298"
SQ SEQUENCE 141 AA; 14726 MW; C2D7B148C2735BA5 CRC64;
MAQKITGYIK LQIPAGKATP APPVGPALGQ KGVNIMAFTK EFNERTKNQM GMIIPVVITV
YADRSFSFIT KTPPAPVLIK KAAGIDTASG VPNKNKVGSI TLAQAEEIAK TKMPDLNAAS
LEAAVSMIKG TARSMGVTVE G
//
