ID E1R295_SEDSS Unreviewed; 103 AA.
AC E1R295;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Small ribosomal subunit protein bS18 {ECO:0000256|HAMAP-Rule:MF_00270};
GN Name=rpsR {ECO:0000256|HAMAP-Rule:MF_00270};
GN OrderedLocusNames=Spirs_2877 {ECO:0000313|EMBL:ADK81980.1};
OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS (Spirochaeta smaragdinae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Sediminispirochaeta.
OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK81980.1, ECO:0000313|Proteomes:UP000002318};
RN [1] {ECO:0000313|EMBL:ADK81980.1, ECO:0000313|Proteomes:UP000002318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC {ECO:0000313|Proteomes:UP000002318};
RX PubMed=21304743; DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
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; CP002116; ADK81980.1; -; Genomic_DNA.
DR RefSeq; WP_013255439.1; NC_014364.1.
DR AlphaFoldDB; E1R295; -.
DR STRING; 573413.Spirs_2877; -.
DR KEGG; ssm:Spirs_2877; -.
DR eggNOG; COG0238; Bacteria.
DR HOGENOM; CLU_148710_0_2_12; -.
DR OMA; CKDKATY; -.
DR OrthoDB; 9812008at2; -.
DR Proteomes; UP000002318; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002318};
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..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 103 AA; 11898 MW; 1E1839928F3231B0 CRC64;
MADENNRDYR SKDRDDSRDS GNRGGRSSFR GGKRPFFKKK VCRFCTGNMV ADYKDPDALG
RFVTERGKIL PRRITGTCAK HQRLLAKEIK RARVLAYLPF VKK
//