ID   RS11_ALCBS              Reviewed;         132 AA.
AC   Q0VSI0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN   Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=ABO_0420;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
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DR   EMBL; AM286690; CAL15868.1; -; Genomic_DNA.
DR   RefSeq; WP_011587706.1; NC_008260.1.
DR   AlphaFoldDB; Q0VSI0; -.
DR   SMR; Q0VSI0; -.
DR   STRING; 393595.ABO_0420; -.
DR   EnsemblBacteria; CAL15868; CAL15868; ABO_0420.
DR   KEGG; abo:ABO_0420; -.
DR   eggNOG; COG0100; Bacteria.
DR   HOGENOM; CLU_072439_5_0_6; -.
DR   OMA; KWGVAHI; -.
DR   OrthoDB; 1713391at2; -.
DR   Proteomes; UP000008871; 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   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..132
FT                   /note="30S ribosomal protein S11"
FT                   /id="PRO_0000294709"
SQ   SEQUENCE   132 AA;  14049 MW;  3E705D7CA2A58A36 CRC64;
     MAKSKKDSGA RRKKVTRTVA DGIAHVHASF NNTIITITDR QGNALSWATS GGAGFRGSRK
     STPFAAQVAA ENAGNAAKDY GLKNLEVRVK GPGPGRESSI RALNGCGYKI THIEDVTPIP
     HNGCRPPKKR RV