ID   RS13_METBF              Reviewed;         162 AA.
AC   Q46GC7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN   Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=Mbar_A0078;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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. {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; CP000099; AAZ69065.1; -; Genomic_DNA.
DR   RefSeq; WP_011305120.1; NC_007355.1.
DR   AlphaFoldDB; Q46GC7; -.
DR   SMR; Q46GC7; -.
DR   STRING; 269797.Mbar_A0078; -.
DR   EnsemblBacteria; AAZ69065; AAZ69065; Mbar_A0078.
DR   GeneID; 3627572; -.
DR   KEGG; mba:Mbar_A0078; -.
DR   eggNOG; arCOG01722; Archaea.
DR   HOGENOM; CLU_103849_0_1_2; -.
DR   OMA; IRAYRGI; -.
DR   OrthoDB; 84219at2157; -.
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: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; IPR019977; Ribosomal_S13_archaeal.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   TIGRFAMs; TIGR03629; uS13_arch; 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.
FT   CHAIN           1..162
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000230586"
FT   REGION          140..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   162 AA;  18329 MW;  E205F251C676B2C6 CRC64;
     MLYTFPWREY MVEEKNNEEI RHLVRIMNTD LKGAKPVEYA LTGLPGIGRR TAILIAKGAG
     VDPTATLGYL PDEEVAKLDR AIGNFEGIVP SWMLNRQKDL ATGQDKHLLG TDILLTFRED
     INNLKKVRAY RGLRHERGLK VRGQRTKSTG RRGSTVGVSR RK