RS13_THET2
ID RS13_THET2 Reviewed; 126 AA.
AC P62655;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=30S ribosomal protein S13;
GN Name=rpsM; Synonyms=rps13; OrderedLocusNames=TT_C1303;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000305}.
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DR EMBL; AE017221; AAS81645.1; -; Genomic_DNA.
DR RefSeq; WP_008633368.1; NC_005835.1.
DR PDB; 2R1G; EM; 12.50 A; I=2-126.
DR PDB; 4KVB; X-ray; 4.20 A; M=1-126.
DR PDB; 4V4I; X-ray; 3.71 A; n=1-126.
DR PDB; 4V4J; X-ray; 3.83 A; n=1-126.
DR PDB; 4V63; X-ray; 3.21 A; AM/CM=1-126.
DR PDB; 4V67; X-ray; 3.00 A; AM/CM=1-126.
DR PDB; 4V7P; X-ray; 3.62 A; AM/DM=2-118.
DR PDB; 4V83; X-ray; 3.50 A; AM/CM=2-117.
DR PDB; 4V84; X-ray; 3.40 A; AM/CM=2-117.
DR PDB; 4V9J; X-ray; 3.86 A; AM/CM=2-126.
DR PDB; 4V9K; X-ray; 3.50 A; AM/CM=2-126.
DR PDB; 4V9L; X-ray; 3.50 A; AM/CM=2-126.
DR PDB; 4V9M; X-ray; 4.00 A; AM/CM=2-126.
DR PDB; 4V9N; X-ray; 3.40 A; AM/CM=2-118.
DR PDB; 4V9Q; X-ray; 3.40 A; BM/DM=2-118.
DR PDB; 4W29; X-ray; 3.80 A; AM/CM=2-126.
DR PDB; 4XEJ; X-ray; 3.80 A; AS13/BS13=2-118.
DR PDB; 5J4D; X-ray; 3.10 A; AD/VA=1-126.
DR PDBsum; 2R1G; -.
DR PDBsum; 4KVB; -.
DR PDBsum; 4V4I; -.
DR PDBsum; 4V4J; -.
DR PDBsum; 4V63; -.
DR PDBsum; 4V67; -.
DR PDBsum; 4V7P; -.
DR PDBsum; 4V83; -.
DR PDBsum; 4V84; -.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4V9N; -.
DR PDBsum; 4V9Q; -.
DR PDBsum; 4W29; -.
DR PDBsum; 4XEJ; -.
DR PDBsum; 5J4D; -.
DR AlphaFoldDB; P62655; -.
DR SMR; P62655; -.
DR IntAct; P62655; 4.
DR STRING; 262724.TT_C1303; -.
DR EnsemblBacteria; AAS81645; AAS81645; TT_C1303.
DR GeneID; 3167962; -.
DR KEGG; tth:TT_C1303; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_0; -.
DR OMA; YRGLRHK; -.
DR OrthoDB; 1772647at2; -.
DR EvolutionaryTrace; P62655; -.
DR Proteomes; UP000000592; 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 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..126
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132159"
FT REGION 95..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4V67"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:4V67"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4V9N"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4V67"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4V67"
SQ SEQUENCE 126 AA; 14305 MW; C20831747B312415 CRC64;
MARIAGVEIP RNKRVDVALT YIYGIGKARA KEALEKTGIN PATRVKDLTE AEVVRLREYV
ENTWKLEGEL RAEVAANIKR LMDIGCYRGL RHRRGLPVRG QRTRTNARTR KGPRKTVAGK
KKAPRK
