ID   RS15_TREPA              Reviewed;          89 AA.
AC   O83857;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN   Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=TP_0887;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it helps nucleate assembly of the platform of the 30S
CC       subunit by binding and bridging several RNA helices of the 16S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC       the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the 50S
CC       subunit in the 70S ribosome, contacting the 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR   EMBL; AE000520; AAC26577.1; -; Genomic_DNA.
DR   PIR; D71269; D71269.
DR   RefSeq; WP_010882330.1; NC_021490.2.
DR   AlphaFoldDB; O83857; -.
DR   SMR; O83857; -.
DR   STRING; 243276.TPANIC_0887; -.
DR   EnsemblBacteria; AAC26577; AAC26577; TP_0887.
DR   GeneID; 57879401; -.
DR   KEGG; tpa:TP_0887; -.
DR   eggNOG; COG0184; Bacteria.
DR   HOGENOM; CLU_148518_0_0_12; -.
DR   OMA; FKTHVKD; -.
DR   OrthoDB; 1990141at2; -.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR   InterPro; IPR000589; Ribosomal_S15.
DR   InterPro; IPR005290; Ribosomal_S15_bac-type.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   PANTHER; PTHR23321; PTHR23321; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
DR   TIGRFAMs; TIGR00952; S15_bact; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..89
FT                   /note="30S ribosomal protein S15"
FT                   /id="PRO_0000115577"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   89 AA;  10056 MW;  478CD7A8096BD5B7 CRC64;
     MALTKERTAS VVQQYGSGEK DTGSSSVQIA LLTERIRQLT DHCKVHPKDK SSNRGLLVLV
     GRRRRLLRYS RRVSMGAYRS LVKSLGLRK