RS13_PSELT
ID RS13_PSELT Reviewed; 128 AA.
AC A8F4T6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=Tlet_0604;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) 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; CP000812; ABV33170.1; -; Genomic_DNA.
DR RefSeq; WP_012002651.1; NC_009828.1.
DR AlphaFoldDB; A8F4T6; -.
DR SMR; A8F4T6; -.
DR STRING; 416591.Tlet_0604; -.
DR PRIDE; A8F4T6; -.
DR EnsemblBacteria; ABV33170; ABV33170; Tlet_0604.
DR KEGG; tle:Tlet_0604; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_0; -.
DR OMA; YRGLRHK; -.
DR OrthoDB; 1772647at2; -.
DR Proteomes; UP000002016; 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..128
FT /note="30S ribosomal protein S13"
FT /id="PRO_1000067521"
FT REGION 97..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 128 AA; 14796 MW; D292929BBD5712D7 CRC64;
MARIVGVELP GNKKCFVALT YLYGVGRTRA FEILKNTGIN PDKRVKDLTD EEVSKITKFI
QDHYKVEGEL RTDINRNIKR LIDIGCYRGF RHKLGLPVRG QRTRSNARTR KGPRPSRIKT
KKKKEQTV
