RS13_GEOSE
ID RS13_GEOSE Reviewed; 120 AA.
AC P15757;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=30S ribosomal protein S13;
DE AltName: Full=BS14;
GN Name=rpsM;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE OF 2-120, AND CROSS-LINKING TO S19.
RC STRAIN=799;
RX PubMed=3291949; DOI=10.1021/bi00409a038;
RA Brockmoeller J., Kamp R.M.;
RT "Cross-linked amino acids in the protein pair S13-S19 and sequence analysis
RT of protein S13 of Bacillus stearothermophilus ribosomes.";
RL Biochemistry 27:3372-3381(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RX PubMed=4607606; DOI=10.1016/0014-5793(74)80391-1;
RA Yaguchi M., Matheson A.T., Visentin L.P.;
RT "Procaryotic ribosomal proteins: N-terminal sequence homologies and
RT structural correspondence of 30 S ribosomal proteins from Escherichia coli
RT and Bacillus stearothermophilus.";
RL FEBS Lett. 46:296-300(1974).
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 tRNA in the A and P-sites (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Has been shown to cross-
CC link to S19 forming a loose heterodimer. Forms two bridges to the 50S
CC subunit in the 70S ribosome (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000305}.
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DR PIR; A28679; R3BS3F.
DR AlphaFoldDB; P15757; -.
DR SMR; P15757; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3291949,
FT ECO:0000269|PubMed:4607606"
FT CHAIN 2..120
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132064"
FT REGION 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 13703 MW; 9848FDA2887B3535 CRC64;
MARIAGVDIP RDKRVVISLT YIYGIGKPTA QILKEAGVSE DTRVRDLTEE ELGRIREIVG
RLKVEGDLRR EVSLNIKRLM EIGCYRGLRH RRGLPVRGQN TKNNARTRKG PRRTVANKKK
