ID   RS5_PHYAS               Reviewed;         171 AA.
AC   B1VAD1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=PA0570;
OS   Phytoplasma australiense.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/jb.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(2008).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
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:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC       S8. {ECO:0000255|HAMAP-Rule:MF_01307}.
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:0000255|HAMAP-Rule:MF_01307}.
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DR   EMBL; AM422018; CAM11904.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VAD1; -.
DR   SMR; B1VAD1; -.
DR   STRING; 59748.PA0570; -.
DR   EnsemblBacteria; CAM11904; CAM11904; PA0570.
DR   KEGG; pal:PA0570; -.
DR   eggNOG; COG0098; Bacteria.
DR   OMA; KRGCGSW; -.
DR   Proteomes; UP000008323; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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   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   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; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..171
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_1000214321"
FT   DOMAIN          15..78
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ   SEQUENCE   171 AA;  18623 MW;  72C1CA99B9FA49F4 CRC64;
     MKTIKKEFVK KTSPYEEKVV KIKRITKVVK GGRRFRFSAL VVVGNKKDQI GFATAKAQEI
     VDAIKKAVEK AKKQLIRIPI VGTTIPHDTI GHFGASKFLL RPASKGTGIV AGGAAARTVL
     ELVGISDVLT KTFGSRTSIN VIRAVMDGLK NLRTKEEVAK LRGLTLAKNE Q