RS13_COREF
ID RS13_COREF Reviewed; 122 AA.
AC Q8FS35;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=CE0569;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC17379.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC17379.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011075046.1; NZ_GG700687.1.
DR AlphaFoldDB; Q8FS35; -.
DR SMR; Q8FS35; -.
DR STRING; 196164.23492405; -.
DR PRIDE; Q8FS35; -.
DR EnsemblBacteria; BAC17379; BAC17379; BAC17379.
DR KEGG; cef:CE0569; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_11; -.
DR OrthoDB; 1772647at2; -.
DR Proteomes; UP000001409; 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 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..122
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132085"
FT REGION 93..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13833 MW; F4D6782B960C0077 CRC64;
MARLAGVDLP RNKRMEIALT YIYGIGPARA KQLLEETGVS PDLRTDNLTD EQIASLRDVI
EATWKVEGDL RREVQADIRR KIEIGSYQGL RHRRGLPVRG QRTKTNARTR KGPKKTIAGK
KK
