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Database: UniProt
Entry: RS15_MYCS2
LinkDB: RS15_MYCS2
Original site: RS15_MYCS2 
ID   RS15_MYCS2              Reviewed;          89 AA.
AC   A0QVQ3; I7G919;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Small ribosomal subunit protein uS15 {ECO:0000255|HAMAP-Rule:MF_01343};
DE   AltName: Full=30S ribosomal protein S15 {ECO:0000305};
GN   Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343};
GN   OrderedLocusNames=MSMEG_2654, MSMEI_2591;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK73765.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP39059.1; -; Genomic_DNA.
DR   RefSeq; WP_003894036.1; NZ_SIJM01000064.1.
DR   RefSeq; YP_886991.1; NC_008596.1.
DR   PDB; 5O5J; EM; 3.45 A; O=1-89.
DR   PDB; 5O61; EM; 3.31 A; BO=1-89.
DR   PDB; 5XYU; EM; 3.45 A; O=1-89.
DR   PDB; 5ZEB; EM; 3.40 A; o=1-89.
DR   PDB; 5ZEP; EM; 3.40 A; o=1-89.
DR   PDB; 5ZEU; EM; 3.70 A; o=1-89.
DR   PDB; 6DZI; EM; 3.46 A; x=2-89.
DR   PDB; 6DZK; EM; 3.60 A; O=2-89.
DR   PDB; 8FR8; EM; 2.76 A; p=2-89.
DR   PDBsum; 5O5J; -.
DR   PDBsum; 5O61; -.
DR   PDBsum; 5XYU; -.
DR   PDBsum; 5ZEB; -.
DR   PDBsum; 5ZEP; -.
DR   PDBsum; 5ZEU; -.
DR   PDBsum; 6DZI; -.
DR   PDBsum; 6DZK; -.
DR   PDBsum; 8FR8; -.
DR   AlphaFoldDB; A0QVQ3; -.
DR   EMDB; EMD-29397; -.
DR   EMDB; EMD-3748; -.
DR   EMDB; EMD-3751; -.
DR   EMDB; EMD-6790; -.
DR   EMDB; EMD-6920; -.
DR   EMDB; EMD-6921; -.
DR   EMDB; EMD-6923; -.
DR   EMDB; EMD-8932; -.
DR   EMDB; EMD-8934; -.
DR   SMR; A0QVQ3; -.
DR   IntAct; A0QVQ3; 2.
DR   STRING; 246196.MSMEG_2654; -.
DR   PaxDb; 246196-MSMEI_2591; -.
DR   GeneID; 66734063; -.
DR   KEGG; msg:MSMEI_2591; -.
DR   KEGG; msm:MSMEG_2654; -.
DR   PATRIC; fig|246196.19.peg.2620; -.
DR   eggNOG; COG0184; Bacteria.
DR   OrthoDB; 9799262at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR   Gene3D; 6.10.250.3130; -; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   HAMAP; MF_01343_B; Ribosomal_uS15_B; 1.
DR   InterPro; IPR000589; Ribosomal_uS15.
DR   InterPro; IPR005290; Ribosomal_uS15_bac-type.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   NCBIfam; TIGR00952; S15_bact; 1.
DR   PANTHER; PTHR23321:SF26; 37S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23321; RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:18955433"
FT   CHAIN           2..89
FT                   /note="Small ribosomal subunit protein uS15"
FT                   /id="PRO_1000054819"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           25..46
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           50..73
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           75..85
FT                   /evidence="ECO:0007829|PDB:5XYU"
SQ   SEQUENCE   89 AA;  10344 MW;  A5711F279E833190 CRC64;
     MALTAEQKKE ILGQYGLHDT DTGSPEAQVA LLTKRIQDLT EHLKVHKHDH HSRRGLLLLV
     GRRRRLLKYV AQVDVARYRS LIERLGLRR
//
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