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Database: UniProt
Entry: D8ICS6_BRAP9
LinkDB: D8ICS6_BRAP9
Original site: D8ICS6_BRAP9 
ID   D8ICS6_BRAP9            Unreviewed;       114 AA.
AC   D8ICS6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Small ribosomal subunit protein bS18 {ECO:0000256|HAMAP-Rule:MF_00270};
GN   Name=rpsR {ECO:0000256|HAMAP-Rule:MF_00270,
GN   ECO:0000313|EMBL:ADK30949.1};
GN   OrderedLocusNames=BP951000_0955 {ECO:0000313|EMBL:ADK30949.1};
OS   Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30949.1, ECO:0000313|Proteomes:UP000000332};
RN   [1] {ECO:0000313|EMBL:ADK30949.1, ECO:0000313|Proteomes:UP000000332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX   PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA   Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA   Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT   "The complete genome sequence of the pathogenic intestinal spirochete
RT   Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL   PLoS ONE 5:E11455-E11455(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; CP002025; ADK30949.1; -; Genomic_DNA.
DR   RefSeq; WP_013243903.1; NC_014330.1.
DR   AlphaFoldDB; D8ICS6; -.
DR   STRING; 759914.BP951000_0955; -.
DR   GeneID; 76624098; -.
DR   KEGG; bpo:BP951000_0955; -.
DR   eggNOG; COG0238; Bacteria.
DR   HOGENOM; CLU_148710_0_1_12; -.
DR   InParanoid; D8ICS6; -.
DR   OMA; NCLKHQH; -.
DR   Proteomes; UP000000332; 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:UP000000332};
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..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   114 AA;  13497 MW;  47FE1721C6E152DE CRC64;
     MELENTENIE NTSNNNEEEN KVKADKKQHF NKEVNEKDAA SRKKFFKKKI CYFCKNNIDV
     LDYKDIKLLK KYVKESGKII PKRLNGTCSK HQRLVTKAIK RARNIALLPY ETKY
//
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