RS11_LACLM
ID RS11_LACLM Reviewed; 127 AA.
AC A2RNM8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=llmg_2355;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- FUNCTION: Located on the platform of the 30S subunit, it bridges
CC several disparate RNA helices of the 16S rRNA. Forms part of the Shine-
CC Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with proteins S7
CC and S18. Binds to IF-3. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000255|HAMAP-Rule:MF_01310}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM406671; CAL98919.1; -; Genomic_DNA.
DR RefSeq; WP_010906297.1; NZ_WJVF01000005.1.
DR PDB; 5MYJ; EM; 5.60 A; AK=1-127.
DR PDBsum; 5MYJ; -.
DR AlphaFoldDB; A2RNM8; -.
DR SMR; A2RNM8; -.
DR STRING; 416870.llmg_2355; -.
DR EnsemblBacteria; CAL98919; CAL98919; llmg_2355.
DR GeneID; 60357143; -.
DR GeneID; 61110401; -.
DR GeneID; 66443067; -.
DR KEGG; llm:llmg_2355; -.
DR eggNOG; COG0100; Bacteria.
DR HOGENOM; CLU_072439_5_0_9; -.
DR OMA; KWGVAHI; -.
DR PhylomeDB; A2RNM8; -.
DR BioCyc; LLAC416870:LLMG_RS11815-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F: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 Gene3D; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR019981; Ribosomal_S11_bac-type.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR TIGRFAMs; TIGR03632; uS11_bact; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..127
FT /note="30S ribosomal protein S11"
FT /id="PRO_0000294779"
SQ SEQUENCE 127 AA; 13287 MW; DA111E88474BA7C7 CRC64;
MAKITRKRRV KKNIESGIVH IQSTFNNTIV MITDVHGNAL AWSSAGALGF KGSKKSTPFA
AQMASEAAAK AAQEQGLKTV SVTVKGPGSG RESAIRALAA AGLNVTSISD VTPVPHNGAR
PPKRRRV