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Database: UniProt
Entry: F0S110_DESTD
LinkDB: F0S110_DESTD
Original site: F0S110_DESTD 
ID   F0S110_DESTD            Unreviewed;       141 AA.
AC   F0S110;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000256|HAMAP-Rule:MF_00736};
GN   Name=rplK {ECO:0000256|HAMAP-Rule:MF_00736};
GN   OrderedLocusNames=Dester_0156 {ECO:0000313|EMBL:ADY72814.1};
OS   Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Desulfurobacterium.
OX   NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY72814.1, ECO:0000313|Proteomes:UP000007102};
RN   [1] {ECO:0000313|EMBL:ADY72814.1, ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX   PubMed=22675590; DOI=10.4056/sigs.2465574;
RA   Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA   Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer
RT   Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT   hydrothermal vent.";
RL   Stand. Genomic Sci. 5:407-415(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL   Submitted (FEB-2011) 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; CP002543; ADY72814.1; -; Genomic_DNA.
DR   RefSeq; WP_013637774.1; NC_015185.1.
DR   AlphaFoldDB; F0S110; -.
DR   STRING; 868864.Dester_0156; -.
DR   KEGG; dte:Dester_0156; -.
DR   eggNOG; COG0080; Bacteria.
DR   HOGENOM; CLU_074237_2_1_0; -.
DR   InParanoid; F0S110; -.
DR   OrthoDB; 9802408at2; -.
DR   Proteomes; UP000007102; Chromosome.
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:UP000007102};
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}.
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;  15150 MW;  180E332D22603EAD CRC64;
     MAKKVVAEVK LQLPAGEATP APPVGPALGQ HGVNIMEFVK AFNAATADKK GLVIPVVITI
     YADRSFTFVL KTPPASVLIK KAAGIEKGAH QPKKEWVGQI TKEQLRQIAE QKMQDLNCYD
     IESAMKIIAG TAENMGVKVV E
//
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