RS13_PYRAR
ID RS13_PYRAR Reviewed; 152 AA.
AC A4WM28;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=Pars_1894;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-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. {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; CP000660; ABP51445.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WM28; -.
DR SMR; A4WM28; -.
DR STRING; 340102.Pars_1894; -.
DR EnsemblBacteria; ABP51445; ABP51445; Pars_1894.
DR KEGG; pas:Pars_1894; -.
DR HOGENOM; CLU_103849_0_0_2; -.
DR OMA; IRAYRGI; -.
DR PhylomeDB; A4WM28; -.
DR Proteomes; UP000001567; 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..152
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000306763"
SQ SEQUENCE 152 AA; 16697 MW; 26FD8C259DBA9041 CRC64;
MSQELRAIVR VGDTDLEGNK QVAYALAKIR GIGIASAYAI CWKLGIDPHA VLGALPEEQI
NKLDWAVRNL HEVAPAWFLN RRKDPETGRD MHLIGSELVL AAKRDVDLMK KLKSWKGIRH
SLGLKVRGQR TVTTGRLGAV AGVTKKKATP GK