ID   RS13_CUTAK              Reviewed;         123 AA.
AC   Q6A6Q8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=PPA1829;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83555.1; -; Genomic_DNA.
DR   RefSeq; WP_002514834.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A6Q8; -.
DR   SMR; Q6A6Q8; -.
DR   STRING; 267747.PPA1829; -.
DR   EnsemblBacteria; AAT83555; AAT83555; PPA1829.
DR   GeneID; 66621737; -.
DR   KEGG; pac:PPA1829; -.
DR   eggNOG; COG0099; Bacteria.
DR   HOGENOM; CLU_103849_1_2_11; -.
DR   OMA; YRGLRHK; -.
DR   Proteomes; UP000000603; 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..123
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000230549"
FT   REGION          89..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..123
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   123 AA;  13996 MW;  87F4E3B870BC986B CRC64;
     MARLIGVDLP RDKRLEVALT YIYGIGRTRA TETLKATGIS GDLRVHELTD DQLVALRDHI
     EANYHVEGDL RREVAADIRR KIEIGTYQGR RHRSGLPVRG QRTRTNARTR KGKRKAVAKK
     KAK