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RS13_BORGP
ID   RS13_BORGP              Reviewed;         125 AA.
AC   Q661C0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=BG0512;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(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; CP000013; AAU07351.1; -; Genomic_DNA.
DR   RefSeq; WP_004791369.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q661C0; -.
DR   SMR; Q661C0; -.
DR   STRING; 290434.BG0512; -.
DR   EnsemblBacteria; AAU07351; AAU07351; BG0512.
DR   GeneID; 66542690; -.
DR   KEGG; bga:BG0512; -.
DR   eggNOG; COG0099; Bacteria.
DR   HOGENOM; CLU_103849_1_2_12; -.
DR   OMA; YRGLRHK; -.
DR   OrthoDB; 1772647at2; -.
DR   Proteomes; UP000002276; 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..125
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000230481"
FT   REGION          95..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   125 AA;  14037 MW;  1A8C5D77B53827E7 CRC64;
     MARISGIDLP SNKQLKIALT SIYGIGRTRA LEVCNKSSIS PSKIAKDLDN DEVNRLRKVI
     ESDYVVEGKL RSEVAMSIKR LMDIACYRGV RHRKGLPLRG QRTKTNARTR KGKRKTVANK
     KIASK
 
 
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