ID   J4K7Y3_9FIRM            Unreviewed;       122 AA.
AC   J4K7Y3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Small ribosomal subunit protein uS13 {ECO:0000256|ARBA:ARBA00035166, ECO:0000256|HAMAP-Rule:MF_01315};
GN   Name=rpsM {ECO:0000256|HAMAP-Rule:MF_01315,
GN   ECO:0000313|EMBL:EJP20071.1};
GN   ORFNames=HMPREF1142_0239 {ECO:0000313|EMBL:EJP20071.1};
OS   Peptostreptococcaceae bacterium AS15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP20071.1, ECO:0000313|Proteomes:UP000006605};
RN   [1] {ECO:0000313|EMBL:EJP20071.1, ECO:0000313|Proteomes:UP000006605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS15 {ECO:0000313|EMBL:EJP20071.1,
RC   ECO:0000313|Proteomes:UP000006605};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_01315}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000256|ARBA:ARBA00008080, ECO:0000256|HAMAP-Rule:MF_01315,
CC       ECO:0000256|RuleBase:RU003830}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJP20071.1}.
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DR   EMBL; ALJM01000038; EJP20071.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4K7Y3; -.
DR   PATRIC; fig|936556.4.peg.1800; -.
DR   OrthoDB; 9803610at2; -.
DR   Proteomes; UP000006605; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; 1.10.8.50; -; 1.
DR   Gene3D; 4.10.910.10; 30s ribosomal protein s13, domain 2; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; Rbsml_uS13_C.
DR   InterPro; IPR001892; Ribosomal_uS13.
DR   InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR   InterPro; IPR019980; Ribosomal_uS13_bac-type.
DR   InterPro; IPR018269; Ribosomal_uS13_CS.
DR   NCBIfam; TIGR03631; uS13_bact; 1.
DR   PANTHER; PTHR10871; 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18; 1.
DR   PANTHER; PTHR10871:SF1; 37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL; 1.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006605};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01315};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_01315}.
FT   REGION          100..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..122
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  13969 MW;  F9B553F55B30CC95 CRC64;
     MARIAGVDLP RDKRVIIGLT YIFGIGKQTS AKILATTGID ESIRIKDLSE EQVNLLRKEI
     DNNYTVEGDL KREISLNIKR LRDIRCYRGL RHMKGLPVRG QKTKTNARTR KGPKRIVGRK
     KK
//