ID   RS13_SULMW              Reviewed;         126 AA.
AC   A8Z688;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=SMGWSS_242;
OS   Sulcia muelleri (strain GWSS).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=444179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS;
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an ancient
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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; CP000770; ABS30639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8Z688; -.
DR   SMR; A8Z688; -.
DR   STRING; 444179.SMGWSS_242; -.
DR   EnsemblBacteria; ABS30639; ABS30639; SMGWSS_242.
DR   KEGG; smg:SMGWSS_242; -.
DR   HOGENOM; CLU_103849_1_2_10; -.
DR   OMA; YRGLRHK; -.
DR   Proteomes; UP000000781; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..126
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_1000086267"
FT   REGION          101..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..126
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   126 AA;  14485 MW;  7367DAC9EAFA0693 CRC64;
     MAIVSGIEIP NNKIGLIALT YIFGIGISTS KRIFKDTGID ENIKVINWSD EDINKIRKYI
     SSNIRIEGEL RFEIQLDIKR MIEIGCYRGI RHRIGLPVRG QKTKNNCRTR KGKKKTVANK
     KKKINK