ID   RS18_CLAM3              Reviewed;          87 AA.
AC   A5CVA9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270};
GN   Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; OrderedLocusNames=CMM_2961;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN03048.1; -; Genomic_DNA.
DR   RefSeq; WP_012039648.1; NC_009480.1.
DR   AlphaFoldDB; A5CVA9; -.
DR   SMR; A5CVA9; -.
DR   STRING; 443906.CMM_2961; -.
DR   EnsemblBacteria; CAN03048; CAN03048; CMM_2961.
DR   GeneID; 56887321; -.
DR   KEGG; cmi:CMM_2961; -.
DR   eggNOG; COG0238; Bacteria.
DR   HOGENOM; CLU_148710_1_0_11; -.
DR   OMA; CKDKATY; -.
DR   OrthoDB; 1940575at2; -.
DR   Proteomes; UP000001564; 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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..87
FT                   /note="30S ribosomal protein S18"
FT                   /id="PRO_1000003481"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   87 AA;  9434 MW;  2CA8352FD528689C CRC64;
     MAGKSSGDRR KPLRGAKGGK NAAPAKSIRV GVIDYKDVAT LRKFISERGK IRARRITGVS
     VQEQRLIARA VKNAREMALL PYAGSGR