ID A0A060JPW1_9MICO Unreviewed; 91 AA.
AC A0A060JPW1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Small ribosomal subunit protein bS18 {ECO:0000256|ARBA:ARBA00035141, ECO:0000256|HAMAP-Rule:MF_00270};
GN Name=rpsR {ECO:0000256|HAMAP-Rule:MF_00270};
GN ORFNames=Rhola_00013900 {ECO:0000313|EMBL:AIC48179.1};
OS Rhodoluna lacicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC48179.1, ECO:0000313|Proteomes:UP000067708};
RN [1] {ECO:0000313|EMBL:AIC48179.1, ECO:0000313|Proteomes:UP000067708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC48179.1,
RC ECO:0000313|Proteomes:UP000067708};
RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT with stream-lined genome.";
RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
CC -!- FUNCTION: Binds as a heterodimer with protein bS6 to the central domain
CC of the 16S rRNA, where it helps stabilize the platform of the 30S
CC subunit. {ECO:0000256|HAMAP-Rule:MF_00270}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight heterodimer
CC with protein bS6. {ECO:0000256|HAMAP-Rule:MF_00270}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.
CC {ECO:0000256|ARBA:ARBA00005589, ECO:0000256|HAMAP-Rule:MF_00270,
CC ECO:0000256|RuleBase:RU003910}.
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DR EMBL; CP007490; AIC48179.1; -; Genomic_DNA.
DR RefSeq; WP_038503433.1; NZ_CP007490.1.
DR AlphaFoldDB; A0A060JPW1; -.
DR STRING; 529884.Rhola_00013900; -.
DR KEGG; rla:Rhola_00013900; -.
DR PATRIC; fig|529884.3.peg.1349; -.
DR eggNOG; COG0238; Bacteria.
DR HOGENOM; CLU_148710_2_2_11; -.
DR OrthoDB; 9812008at2; -.
DR Proteomes; UP000067708; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Ribosomal protein S18; 1.
DR HAMAP; MF_00270; Ribosomal_S18; 1.
DR InterPro; IPR001648; Ribosomal_bS18.
DR InterPro; IPR018275; Ribosomal_bS18_CS.
DR InterPro; IPR036870; Ribosomal_bS18_sf.
DR NCBIfam; TIGR00165; S18; 1.
DR PANTHER; PTHR13479:SF40; 28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13479; 30S RIBOSOMAL PROTEIN S18; 1.
DR Pfam; PF01084; Ribosomal_S18; 1.
DR PRINTS; PR00974; RIBOSOMALS18.
DR SUPFAM; SSF46911; Ribosomal protein S18; 1.
DR PROSITE; PS00057; RIBOSOMAL_S18; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000067708};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00270};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00270}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00270};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00270}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 91 AA; 10145 MW; 6E52DA2879F52DDE CRC64;
MALSKSDPRN AAKRDAPKRA SKFAKEAPAK FQKVGIIDYK DIATLRKFVS DRGKIRARRI
TGVSVQEQRL ISRAIKNARE MALMPYAGAG R
//