ID   RS5_NATPD               Reviewed;         211 AA.
AC   Q3IMW8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=NP_4894A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4.
CC       {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; CR936257; CAI50538.1; -; Genomic_DNA.
DR   RefSeq; WP_011324150.1; NC_007426.1.
DR   AlphaFoldDB; Q3IMW8; -.
DR   SMR; Q3IMW8; -.
DR   STRING; 348780.NP_4894A; -.
DR   EnsemblBacteria; CAI50538; CAI50538; NP_4894A.
DR   GeneID; 3703184; -.
DR   KEGG; nph:NP_4894A; -.
DR   eggNOG; arCOG04087; Archaea.
DR   HOGENOM; CLU_065898_0_1_2; -.
DR   OMA; KRGCGSW; -.
DR   OrthoDB; 60954at2157; -.
DR   Proteomes; UP000002698; 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_A; Ribosomal_S5_A; 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; IPR005711; Ribosomal_S5_euk/arc.
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; TIGR01020; uS5_euk_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 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..211
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000293215"
FT   DOMAIN          46..109
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   REGION          191..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  23036 MW;  263B2B8140BA5D2F CRC64;
     MSNGWEPRTR LGRKVADGEI TSMQDALQSG LPLKEPELVD QLLPGLEDEV LDINMVQRMT
     DSGRRVKFRC VVVIGNRDGY VGYAQGRDDQ VGGAIQKAID VAKLNIIDVP LGSGSWEDRP
     GGRNSLMRRT TGKAGSVEVE LKPAPRGLGL AAAPTVRHVL ELAGVEDAWT KCHGNTRTTL
     NLAKATYNAL RNASESRTPE HTRQVRQEAQ E