ID   RS18_CLOAB              Reviewed;          90 AA.
AC   Q97CX4;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270};
GN   Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; OrderedLocusNames=CA_C3722;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Binds as a heterodimer with protein S6 to the central domain
CC       of the 16S rRNA, where it helps stabilize the platform of the 30S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_00270}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight heterodimer
CC       with protein S6. {ECO:0000255|HAMAP-Rule:MF_00270}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00270}.
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DR   EMBL; AE001437; AAK81642.1; -; Genomic_DNA.
DR   PIR; G97356; G97356.
DR   RefSeq; NP_350302.1; NC_003030.1.
DR   RefSeq; WP_010966982.1; NC_003030.1.
DR   AlphaFoldDB; Q97CX4; -.
DR   SMR; Q97CX4; -.
DR   STRING; 272562.CA_C3722; -.
DR   PRIDE; Q97CX4; -.
DR   EnsemblBacteria; AAK81642; AAK81642; CA_C3722.
DR   GeneID; 45000218; -.
DR   KEGG; cac:CA_C3722; -.
DR   PATRIC; fig|272562.8.peg.3911; -.
DR   eggNOG; COG0238; Bacteria.
DR   HOGENOM; CLU_148710_0_3_9; -.
DR   OMA; QKKYCRF; -.
DR   OrthoDB; 1940575at2; -.
DR   Proteomes; UP000000814; 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; 4.10.640.10; -; 1.
DR   HAMAP; MF_00270; Ribosomal_S18; 1.
DR   InterPro; IPR001648; Ribosomal_S18.
DR   InterPro; IPR018275; Ribosomal_S18_CS.
DR   InterPro; IPR036870; Ribosomal_S18_sf.
DR   PANTHER; PTHR13479; PTHR13479; 1.
DR   Pfam; PF01084; Ribosomal_S18; 1.
DR   PRINTS; PR00974; RIBOSOMALS18.
DR   SUPFAM; SSF46911; SSF46911; 1.
DR   TIGRFAMs; TIGR00165; S18; 1.
DR   PROSITE; PS00057; RIBOSOMAL_S18; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..90
FT                   /note="30S ribosomal protein S18"
FT                   /id="PRO_0000111144"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   90 AA;  10507 MW;  FD68F8FF15FFA198 CRC64;
     MARDNGNKDR DGKRPNGGRN RKMKRKICSF CMEKSESIDY KDINKLRKYV TERGKILPRR
     ISGNCAKHQR ELTIAIKRAR NIALLPFTTE