RS15_BACSU
ID RS15_BACSU Reviewed; 89 AA.
AC P21473; P70988;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
DE AltName: Full=BS18;
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=BSU16680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9108293; DOI=10.1007/s004380050393;
RA Coquard D., Huecas M., Ott M., van Dijl J.M., van Loon A.P., Hohmann H.P.;
RT "Molecular cloning and characterisation of the ribC gene from Bacillus
RT subtilis: a point mutation in ribC results in riboflavin overproduction.";
RL Mol. Gen. Genet. 254:81-84(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-38.
RX PubMed=6806564; DOI=10.1007/bf00330792;
RA Higo K., Otaka E., Osawa S.;
RT "Purification and characterization of 30S ribosomal proteins from Bacillus
RT subtilis: correlation to Escherichia coli 30S proteins.";
RL Mol. Gen. Genet. 185:239-244(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-89.
RX PubMed=8825779; DOI=10.1046/j.1365-2958.1996.380907.x;
RA Luttinger A., Hahn J., Dubnau D.;
RT "Polynucleotide phosphorylase is necessary for competence development in
RT Bacillus subtilis.";
RL Mol. Microbiol. 19:343-356(1996).
RN [5] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-89 WITH AND WITHOUT
RP VIRGINIAMYCIN M, AND SUBUNIT.
RX PubMed=30126986; DOI=10.1073/pnas.1808535115;
RA Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M.,
RA Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.;
RT "Structural basis for antibiotic resistance mediated by the Bacillus
RT subtilis ABCF ATPase VmlR.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018).
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 (PubMed:30126986). Forms a
CC bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_01343,
CC ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR EMBL; Z80835; CAB02560.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13541.1; -; Genomic_DNA.
DR EMBL; U29668; AAC43594.1; -; Genomic_DNA.
DR PIR; F69700; F69700.
DR RefSeq; NP_389550.1; NC_000964.3.
DR RefSeq; WP_003220957.1; NZ_JNCM01000035.1.
DR PDB; 3J9W; EM; 3.90 A; AO=1-89.
DR PDB; 5NJT; EM; 3.80 A; O=2-89.
DR PDB; 6HA1; EM; 3.10 A; o=1-89.
DR PDB; 6HA8; EM; 3.50 A; o=1-89.
DR PDB; 6HTQ; EM; 4.50 A; o=4-88.
DR PDB; 7O5B; EM; 3.33 A; O=1-89.
DR PDB; 7QV1; EM; 3.50 A; o=1-89.
DR PDB; 7QV2; EM; 3.50 A; o=1-89.
DR PDB; 7QV3; EM; 5.14 A; o=1-89.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P21473; -.
DR SMR; P21473; -.
DR STRING; 224308.BSU16680; -.
DR jPOST; P21473; -.
DR PaxDb; P21473; -.
DR PRIDE; P21473; -.
DR EnsemblBacteria; CAB13541; CAB13541; BSU_16680.
DR GeneID; 64303561; -.
DR GeneID; 938814; -.
DR KEGG; bsu:BSU16680; -.
DR PATRIC; fig|224308.179.peg.1809; -.
DR eggNOG; COG0184; Bacteria.
DR InParanoid; P21473; -.
DR OMA; FKTHVKD; -.
DR PhylomeDB; P21473; -.
DR BioCyc; BSUB:BSU16680-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
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 CDD; cd00353; Ribosomal_S15p_S13e; 1.
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.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6806564"
FT CHAIN 2..89
FT /note="30S ribosomal protein S15"
FT /id="PRO_0000115381"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 35..38
FT /note="SINN -> BIBS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 89 AA; 10573 MW; C49E6E418C54330C CRC64;
MAITQERKNQ LINEFKTHES DTGSPEVQIA ILTDSINNLN EHLRTHKKDH HSRRGLLKMV
GKRRNLLTYL RNKDVTRYRE LINKLGLRR
