RL11_NATPD
ID RL11_NATPD Reviewed; 163 AA.
AC Q3INI5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=NP_4454A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
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:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; CR936257; CAI50318.1; -; Genomic_DNA.
DR RefSeq; WP_011323933.1; NC_007426.1.
DR AlphaFoldDB; Q3INI5; -.
DR SMR; Q3INI5; -.
DR STRING; 348780.NP_4454A; -.
DR EnsemblBacteria; CAI50318; CAI50318; NP_4454A.
DR GeneID; 3703121; -.
DR KEGG; nph:NP_4454A; -.
DR eggNOG; arCOG04372; Archaea.
DR HOGENOM; CLU_074237_4_0_2; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 98187at2157; -.
DR Proteomes; UP000002698; Chromosome.
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; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..163
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000258250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 17129 MW; 44FCCD9ABEB1AA6A CRC64;
MAGTIEVLVA GGQADPGPPL GPELGPTPVD VQAVVNEIND QTEAFDGTEV PVTIDYDDDG
SFDIDVGVPP TAALIKDELD FETGSGEPNE EFVADMSAEQ LKTVAEQKLP DLLAYDTRNA
AKEVAGTCVS LGVTIEGEDA RTFNQRLDNG EFDDVFAEAE PAA
