ID   RS13_NANEQ              Reviewed;         153 AA.
AC   Q74M95;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=NEQ467;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: Located at the top of the head of the 30S subunit, it
CC       contacts several helices of the 16S rRNA. In the 70S ribosome it
CC       contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit
CC       (bridge B1b), connecting the 2 subunits; these bridges are implicated
CC       in subunit movement. {ECO:0000255|HAMAP-Rule:MF_01315}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose heterodimer
CC       with protein S19. Forms two bridges to the 50S subunit in the 70S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01315}.
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DR   EMBL; AE017199; AAR39310.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74M95; -.
DR   SMR; Q74M95; -.
DR   STRING; 228908.NEQ467; -.
DR   EnsemblBacteria; AAR39310; AAR39310; NEQ467.
DR   KEGG; neq:NEQ467; -.
DR   PATRIC; fig|228908.8.peg.481; -.
DR   HOGENOM; CLU_103849_0_0_2; -.
DR   OMA; IRAYRGI; -.
DR   Proteomes; UP000000578; Chromosome.
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   Gene3D; 4.10.910.10; -; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR   InterPro; IPR001892; Ribosomal_S13.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR019977; Ribosomal_S13_archaeal.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   TIGRFAMs; TIGR03629; uS13_arch; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..153
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000306760"
FT   REGION          132..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..153
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   153 AA;  17917 MW;  8AF1FBF1A9F5D9B9 CRC64;
     MAKKPYGEVT KDIVHIADVD LDGHKPIYVE LRKVVGVNWM FAHAVCAALG IDKWRKIGSL
     SDEELEKLED ALRNPWKYGI PSWLYNRRRD PETGKDLHLV GNDYKITMEF DIKREMQINS
     WRGYRHREGL PVRGQRTRSH HRKGRTVGVI KKK