RS13_MYCPU
ID RS13_MYCPU Reviewed; 132 AA.
AC Q98Q06;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=MYPU_5630;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; AL445565; CAC13736.1; -; Genomic_DNA.
DR PIR; C90582; C90582.
DR RefSeq; WP_010925364.1; NC_002771.1.
DR AlphaFoldDB; Q98Q06; -.
DR SMR; Q98Q06; -.
DR STRING; 272635.MYPU_5630; -.
DR EnsemblBacteria; CAC13736; CAC13736; CAC13736.
DR KEGG; mpu:MYPU_5630; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_14; -.
DR OMA; YRGLRHK; -.
DR OrthoDB; 1772647at2; -.
DR BioCyc; MPUL272635:G1GT6-576-MON; -.
DR Proteomes; UP000000528; 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..132
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132111"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 15002 MW; 1C68EF03E0B622D0 CRC64;
MARILNIEIP SNKRVVISLT YILGIGKSLS KEIIVKANEK LAKAKEKTFT EDSRVKDLSE
EQLQAIRDSA KTYLTEGDLR REVSLNIKRL MEIKCYRGIR HRKGLPVRGQ VTQKNARTRK
GPRKTVAGKK GK
