RS15_PETMO
ID RS15_PETMO Reviewed; 91 AA.
AC A9BH72;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; OrderedLocusNames=Pmob_0568;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000879; ABX31302.1; -; Genomic_DNA.
DR RefSeq; WP_012208406.1; NC_010003.1.
DR AlphaFoldDB; A9BH72; -.
DR SMR; A9BH72; -.
DR STRING; 403833.Pmob_0568; -.
DR EnsemblBacteria; ABX31302; ABX31302; Pmob_0568.
DR KEGG; pmo:Pmob_0568; -.
DR eggNOG; COG0184; Bacteria.
DR HOGENOM; CLU_148518_0_0_0; -.
DR OMA; FKTHVKD; -.
DR OrthoDB; 1990141at2; -.
DR Proteomes; UP000000789; 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 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 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..91
FT /note="30S ribosomal protein S15"
FT /id="PRO_0000354211"
SQ SEQUENCE 91 AA; 10714 MW; 64B4F0B8E804833E CRC64;
MSRGLDPEKK EELIEEFKIN DKDTGSVEVQ VALLSARIKH LTEHLKQHPK DYHSRRGLMM
MVGKRRKMLK YLRKSKPLVY QEIINKLGIR G