ID A0A1M5PGB7_9FLAO Unreviewed; 145 AA.
AC A0A1M5PGB7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=SAMN04488116_3221 {ECO:0000313|EMBL:SHH00856.1};
OS Allomuricauda flava.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=570519 {ECO:0000313|EMBL:SHH00856.1, ECO:0000313|Proteomes:UP000184532};
RN [1] {ECO:0000313|Proteomes:UP000184532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22638 {ECO:0000313|Proteomes:UP000184532};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQWL01000007; SHH00856.1; -; Genomic_DNA.
DR RefSeq; WP_073181477.1; NZ_FQWL01000007.1.
DR AlphaFoldDB; A0A1M5PGB7; -.
DR STRING; 570519.SAMN04488116_3221; -.
DR OrthoDB; 9802408at2; -.
DR Proteomes; UP000184532; 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 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 145 AA; 15358 MW; 2CBB7B6BFF86BE09 CRC64;
MAKEVDKVVK LQVRGGAANP SPPVGPALGA AGVNIMEFCK QFNARTQDKP GKVLPVVITV
YKDKSFEFVV KTPPAAVQLL EAAKIKKGSG EPNRVKSGSV SWDQVKAIAE DKMVDLNAFT
VESAMSMVAG TARSMGLKVA GKRPF
//
