ID   RS13_LEGPC              Reviewed;         118 AA.
AC   A5IHP4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=LPC_2993;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000675; ABQ56894.1; -; Genomic_DNA.
DR   RefSeq; WP_010946100.1; NC_009494.2.
DR   AlphaFoldDB; A5IHP4; -.
DR   SMR; A5IHP4; -.
DR   GeneID; 66489549; -.
DR   KEGG; lpc:LPC_2993; -.
DR   HOGENOM; CLU_103849_1_2_6; -.
DR   OMA; YRGLRHK; -.
DR   BioCyc; LPNE400673:LPC_RS02020-MON; -.
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..118
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000306634"
FT   REGION          94..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  13134 MW;  02FEF849E0C7431A CRC64;
     MARIAGVNIP DHKHVVIALT AIYGIGKTTS LKLCKTVDID PSVKVSQLSD AQLESLRTEI
     AKITVEGDLR RVVTMNIKRL MDLGCYRGLR HRRGLPLRGQ RTKTNARTRK GRRKGTSS