RS13_THEVO
ID RS13_THEVO Reviewed; 171 AA.
AC Q97B96;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=TV0561;
GN ORFNames=TVG0550096;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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. {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; BA000011; BAB59703.1; -; Genomic_DNA.
DR AlphaFoldDB; Q97B96; -.
DR SMR; Q97B96; -.
DR STRING; 273116.14324776; -.
DR EnsemblBacteria; BAB59703; BAB59703; BAB59703.
DR KEGG; tvo:TVG0550096; -.
DR eggNOG; arCOG01722; Archaea.
DR HOGENOM; CLU_103849_0_0_2; -.
DR OMA; IRAYRGI; -.
DR PhylomeDB; Q97B96; -.
DR Proteomes; UP000001017; 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: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..171
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132194"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 19515 MW; 6FFDA4C171034D21 CRC64;
MGKASANNVK SDKEAAKPAA KKDENKDFQY IVRIANKDLN GERPIPLALS DLKGIGLRLG
YAIAERLNLQ PTKKIGELKE DEIEKLKEYV ENKEYDLPDW LLNHRREPVT GKNLNLVTTD
LDVQVQEDIN LMKKIRSYKG IRHEKGKKVR GQRTRSNGRR GLSIGVVRKK E