ID A0A1Q9JIJ8_9FIRM Unreviewed; 77 AA.
AC A0A1Q9JIJ8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BHK98_08125 {ECO:0000313|EMBL:OLR56030.1};
OS Hornefia porci.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR56030.1, ECO:0000313|Proteomes:UP000187404};
RN [1] {ECO:0000313|EMBL:OLR56030.1, ECO:0000313|Proteomes:UP000187404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-3-10 {ECO:0000313|EMBL:OLR56030.1,
RC ECO:0000313|Proteomes:UP000187404};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR56030.1}.
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DR EMBL; MJIE01000001; OLR56030.1; -; Genomic_DNA.
DR RefSeq; WP_075713248.1; NZ_MJIE01000001.1.
DR AlphaFoldDB; A0A1Q9JIJ8; -.
DR STRING; 1261640.BHK98_08125; -.
DR OrthoDB; 9812008at2; -.
DR Proteomes; UP000187404; 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:UP000187404};
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}.
SQ SEQUENCE 77 AA; 8912 MW; 3C694ED22499DA02 CRC64;
MDNRRHGGPR RRKVCQFCAD KSEAIDYKDV EKLKKYVTER GKILPKRITG TCAKHQRELT
TAIKRARIVA LLPYVAD
//