ID   RS13_HELAH              Reviewed;         120 AA.
AC   Q17ZB7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=Hac_0157;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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. Contacts the tRNAs in the A and P-sites.
CC       {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; AM260522; CAJ99009.1; -; Genomic_DNA.
DR   RefSeq; WP_000090804.1; NC_008229.1.
DR   AlphaFoldDB; Q17ZB7; -.
DR   SMR; Q17ZB7; -.
DR   STRING; 382638.Hac_0157; -.
DR   EnsemblBacteria; CAJ99009; CAJ99009; Hac_0157.
DR   KEGG; hac:Hac_0157; -.
DR   eggNOG; COG0099; Bacteria.
DR   HOGENOM; CLU_103849_1_2_7; -.
DR   OMA; YRGLRHK; -.
DR   OrthoDB; 1772647at2; -.
DR   BioCyc; HACI382638:HAC_RS00695-MON; -.
DR   Proteomes; UP000000775; 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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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; IPR019980; Ribosomal_S13_bac-type.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   PANTHER; PTHR10871:SF1; PTHR10871:SF1; 1.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   TIGRFAMs; TIGR03631; uS13_bact; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..120
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000306619"
FT   REGION          93..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  13547 MW;  C0D77A6B19B7389A CRC64;
     MARIAGVDLP KKKRVEYALT YIYGIGLKSS REILEAVGIS FDKRVHELSE DEASSIAKKI
     QQSYLVEGDL RKKVQMDIKS LMDLGNYRGI RHRKGLPVRG QTTKNNARTR KGKKKTVGSK