ID   RR5_THAPS               Reviewed;         179 AA.
AC   A0T0Y9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=30S ribosomal protein S5, chloroplastic;
GN   Name=rps5;
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA   Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA   Green B.R.;
RT   "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT   Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT   lineage.";
RL   Mol. Genet. Genomics 277:427-439(2007).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and contacts
CC       protein S4. The interaction surface between S4 and S5 is involved in
CC       control of translational fidelity.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; EF067921; ABK20824.1; -; Genomic_DNA.
DR   RefSeq; YP_874601.1; NC_008589.1.
DR   AlphaFoldDB; A0T0Y9; -.
DR   SMR; A0T0Y9; -.
DR   PRIDE; A0T0Y9; -.
DR   GeneID; 4524764; -.
DR   InParanoid; A0T0Y9; -.
DR   Proteomes; UP000001449; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Plastid; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..179
FT                   /note="30S ribosomal protein S5, chloroplastic"
FT                   /id="PRO_0000277028"
FT   DOMAIN          26..89
FT                   /note="S5 DRBM"
SQ   SEQUENCE   179 AA;  19297 MW;  498B3CD40A8F445D CRC64;
     MSTEFNQVNK LKKTPRRNDN LNEAKFVERL IKISRVTKVT KGGKKLSFRA VVVIGDENGK
     VGVGVGKAED VVNAFKKAKT DGRKNLIDVP ITKSLSIPHA VIGDLGACKI IMRPSIEGSG
     VIAGGAVRTV LEVAGIKNVI AKQLGSDNLL NNARTAIVAL ESLTTLDEVK RKRYHKSVL