RS13_POLNS
ID RS13_POLNS Reviewed; 121 AA.
AC B1XSS4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=Pnec_0073;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(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. 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; CP001010; ACB43401.1; -; Genomic_DNA.
DR RefSeq; WP_012357168.1; NC_010531.1.
DR AlphaFoldDB; B1XSS4; -.
DR SMR; B1XSS4; -.
DR STRING; 452638.Pnec_0073; -.
DR EnsemblBacteria; ACB43401; ACB43401; Pnec_0073.
DR KEGG; pne:Pnec_0073; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_4; -.
DR OMA; YRGLRHK; -.
DR OrthoDB; 1772647at2; -.
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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT CHAIN 1..121
FT /note="30S ribosomal protein S13"
FT /id="PRO_1000141299"
FT REGION 94..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 121 AA; 13557 MW; AA7B5BD3CF0F6B99 CRC64;
MARIAGVNIP NHQHTVIGLT AIFGIGTTRA HQICKTTGVA IDKKVKDLID ADLEKLRDEV
GKFVTEGDLR REVTMSIKRL MDLGCYRGVR HRKDLPVRGQ RTKTNARTRK GPRKSGVQLK
K