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RS1_SHIFL
ID   RS1_SHIFL               Reviewed;         557 AA.
AC   P0AG70; P02349; P77352;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=30S ribosomal protein S1;
GN   Name=rpsA; OrderedLocusNames=SF0907, S0971;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC       point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC       purine-rich sequence (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Some nascent polypeptide
CC       chains are able to cross-link to this protein in situ. Can be cross-
CC       linked to mRNA in the ribosome (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated; probably on a serine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN42537.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16423.1; -; Genomic_DNA.
DR   RefSeq; NP_706830.1; NC_004337.2.
DR   RefSeq; WP_000140327.1; NZ_WPGW01000072.1.
DR   AlphaFoldDB; P0AG70; -.
DR   BMRB; P0AG70; -.
DR   SMR; P0AG70; -.
DR   STRING; 198214.SF0907; -.
DR   PRIDE; P0AG70; -.
DR   EnsemblBacteria; AAN42537; AAN42537; SF0907.
DR   EnsemblBacteria; AAP16423; AAP16423; S0971.
DR   GeneID; 1023876; -.
DR   GeneID; 67414201; -.
DR   KEGG; sfl:SF0907; -.
DR   KEGG; sfx:S0971; -.
DR   PATRIC; fig|198214.7.peg.1056; -.
DR   HOGENOM; CLU_015805_2_1_6; -.
DR   OMA; SLNEFRY; -.
DR   OrthoDB; 1235756at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 6.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR000110; Ribosomal_S1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR10724:SF7; PTHR10724:SF7; 2.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; SSF50249; 6.
DR   TIGRFAMs; TIGR00717; rpsA; 1.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding.
FT   CHAIN           1..557
FT                   /note="30S ribosomal protein S1"
FT                   /id="PRO_0000196046"
FT   DOMAIN          21..87
FT                   /note="S1 motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          105..171
FT                   /note="S1 motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          192..260
FT                   /note="S1 motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          277..347
FT                   /note="S1 motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          364..434
FT                   /note="S1 motif 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          451..520
FT                   /note="S1 motif 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   MOD_RES         229
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         363
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  61158 MW;  0ABCDEB9E510C267 CRC64;
     MTESFAQLFE ESLKEIETRP GSIVRGVVVA IDKDVVLVDA GLKSESAIPA EQFKNAQGEL
     EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK AYEDAETVTG VINGKVKGGF
     TVELNGIRAF LPGSLVDVRP VRDTLHLEGK ELEFKVIKLD QKRNNVVVSR RAVIESENSA
     ERDQLLENLQ EGMEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
     ITVKVLKFDR ERTRVSLGLK QLGEDPWVAI AKRYPEGTKL TGRVTNLTDY GCFVEIEEGV
     EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK ANPWQQFAET
     HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNV AGEEAVREYK KGDEIAAVVL
     QVDAERERIS LGVKQLAEDP FNNWVALNKK GAIVTGKVTA VDAKGATVEL ADGVEGYLRA
     SEASRDRVED ATLVLSVGDE VEAKFTGVDR KNRAISLSVR AKDEADEKDA IATVNKQEDA
     NFSNNAMAEA FKAAKGE
 
 
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