ID   RS5_CARRP               Reviewed;         139 AA.
AC   Q05FJ9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=30S ribosomal protein S5;
GN   Name=rpsE; OrderedLocusNames=CRP_141;
OS   Carsonella ruddii (strain PV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=387662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV;
RX   PubMed=17038615; DOI=10.1126/science.1134196;
RA   Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA   Hattori M.;
RT   "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL   Science 314:267-267(2006).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- FUNCTION: Located at the back of the 30S subunit body where it
CC       stabilizes the conformation of the head with respect to the body.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and S8
CC       (By similarity). {ECO:0000250}.
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; AP009180; BAF35172.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05FJ9; -.
DR   SMR; Q05FJ9; -.
DR   STRING; 387662.CRP_141; -.
DR   EnsemblBacteria; BAF35172; BAF35172; CRP_141.
DR   KEGG; crp:CRP_141; -.
DR   HOGENOM; CLU_065898_2_2_6; -.
DR   OMA; KRGCGSW; -.
DR   Proteomes; UP000000777; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
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   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..139
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000293195"
FT   DOMAIN          1..64
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
SQ   SEQUENCE   139 AA;  15538 MW;  B5DDB36883F054AB CRC64;
     MEKKLIKIHR VTKVVKGGRI FSYTATSIVG NRKKNIGLGR GKSREVLESI KKSYLKAKKN
     ILKLNFSKNI IPYFLFAKHC ATKVFLYPAN DIIGLIASKY VKQVLNIIGV FSVFSKIHGS
     TNAINVVICT IKALSLIKK