RL11_AROAE
ID RL11_AROAE Reviewed; 143 AA.
AC Q5P343;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=AZOSEA21460;
GN ORFNames=ebA3812;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(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 -!- PTM: One or more lysine residues are methylated. {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; CR555306; CAI08271.1; -; Genomic_DNA.
DR RefSeq; WP_011237962.1; NC_006513.1.
DR AlphaFoldDB; Q5P343; -.
DR SMR; Q5P343; -.
DR STRING; 76114.ebA3812; -.
DR EnsemblBacteria; CAI08271; CAI08271; ebA3812.
DR KEGG; eba:ebA3812; -.
DR eggNOG; COG0080; Bacteria.
DR HOGENOM; CLU_074237_2_0_4; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 1702697at2; -.
DR Proteomes; UP000006552; 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; IPR006519; Ribosomal_L11_bac-typ.
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 TIGRFAMs; TIGR01632; L11_bact; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..143
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000258119"
SQ SEQUENCE 143 AA; 15030 MW; 0D8F011D58E67E36 CRC64;
MAKKITGYIK LQVPAGKANP SPPIGPALGQ RGLNIMEFCK AFNARTQGLE PGLPIPVVIT
AFADKSFTFI MKTPPATILI KKAAKITKGS PKPHTDKVGS ITRAQVEEIA KTKMADLTAA
DMEAAVRTIA GSARSMGITV EGL