ID A0A3N1XG98_9FIRM Unreviewed; 94 AA.
AC A0A3N1XG98;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=EDD66_11082 {ECO:0000313|EMBL:ROR25726.1};
OS Mobilisporobacter senegalensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mobilisporobacter.
OX NCBI_TaxID=1329262 {ECO:0000313|EMBL:ROR25726.1, ECO:0000313|Proteomes:UP000273083};
RN [1] {ECO:0000313|EMBL:ROR25726.1, ECO:0000313|Proteomes:UP000273083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26537 {ECO:0000313|EMBL:ROR25726.1,
RC ECO:0000313|Proteomes:UP000273083};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROR25726.1}.
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DR EMBL; RJVG01000010; ROR25726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1XG98; -.
DR OrthoDB; 9812008at2; -.
DR Proteomes; UP000273083; Unassembled WGS sequence.
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:UP000273083};
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..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 94 AA; 10972 MW; E391B193A5246630 CRC64;
MPFNKNDRND RGDRGDSSFK RRGGRRRKKV CVFCADKNHT GIDYKDINKL KRYVSERGKI
LPRRITGNCA KHQRALTVAI KRARHIALMP YTLD
//
