ID N0BJI5_9EURY Unreviewed; 147 AA.
AC N0BJI5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Small ribosomal subunit protein uS13 {ECO:0000256|HAMAP-Rule:MF_01315};
GN Name=rps13 {ECO:0000256|HAMAP-Rule:MF_01315};
GN ORFNames=Asulf_00622 {ECO:0000313|EMBL:AGK60641.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK60641.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK60641.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK60641.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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: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}.
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DR EMBL; CP005290; AGK60641.1; -; Genomic_DNA.
DR RefSeq; WP_015590240.1; NC_021169.1.
DR AlphaFoldDB; N0BJI5; -.
DR STRING; 387631.Asulf_00622; -.
DR GeneID; 15392265; -.
DR KEGG; ast:Asulf_00622; -.
DR eggNOG; arCOG01722; Archaea.
DR HOGENOM; CLU_103849_0_0_2; -.
DR OrthoDB; 372127at2157; -.
DR Proteomes; UP000013307; Chromosome.
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: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; IPR019977; Ribosomal_uS13_archaeal.
DR InterPro; IPR018269; Ribosomal_uS13_CS.
DR NCBIfam; TIGR03629; uS13_arch; 1.
DR PANTHER; PTHR10871; 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18; 1.
DR PANTHER; PTHR10871:SF3; 40S RIBOSOMAL PROTEIN S18; 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:UP000013307};
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01315};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01315}.
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 17103 MW; 0FE55D4BDE0E156D CRC64;
MSEFKHIIRI ADTDIDGKKK VVFALTQIKG IGCRVAKSIT NYLGIDPNAK LGELDDETVD
RLKKFVEEDI EQMPDWMMNR RKDRYSGRDL HLLSKDVDFA RMVDIEMMMR MKCYRGIRHA
KGKKVRGQRT RSTGRSGRTV GVIRRKK
//
