ID   RS13_UREPA              Reviewed;         132 AA.
AC   Q9PQN6;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Synonyms=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=UU255;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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; AF222894; AAF30664.1; -; Genomic_DNA.
DR   RefSeq; WP_006688863.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQN6; -.
DR   SMR; Q9PQN6; -.
DR   STRING; 273119.UU255; -.
DR   EnsemblBacteria; AAF30664; AAF30664; UU255.
DR   GeneID; 29672542; -.
DR   KEGG; uur:UU255; -.
DR   eggNOG; COG0099; Bacteria.
DR   HOGENOM; CLU_103849_1_2_14; -.
DR   OMA; YRGLRHK; -.
DR   Proteomes; UP000000423; 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..132
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000132165"
FT   REGION          101..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..122
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   132 AA;  15048 MW;  FD726B5F0693A890 CRC64;
     MARILGVDIP NDKRVVISLT YIFGIGKSTS QQILKLANID ENIRVKDLAD EQIAEIRRVA
     LNFVKANGEK LQLEGDLRRT VAMDIKRLME IGSYRGIRHR RGLPVRGQRT KTNARTRKGP
     RKTVANKKIE TR