ID   RS1_MYCTO               Reviewed;         481 AA.
AC   P9WH42; L0TA09; O06147;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=30S ribosomal protein S1;
GN   Name=rpsA; OrderedLocusNames=MT1666;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45936.1; -; Genomic_DNA.
DR   PIR; D70559; D70559.
DR   RefSeq; WP_003408066.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WH42; -.
DR   SMR; P9WH42; -.
DR   EnsemblBacteria; AAK45936; AAK45936; MT1666.
DR   KEGG; mtc:MT1666; -.
DR   PATRIC; fig|83331.31.peg.1789; -.
DR   HOGENOM; CLU_015805_4_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR10724:SF7; PTHR10724:SF7; 1.
DR   Pfam; PF00575; S1; 4.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   PROSITE; PS50126; S1; 4.
PE   3: Inferred from homology;
KW   Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT   CHAIN           1..481
FT                   /note="30S ribosomal protein S1"
FT                   /id="PRO_0000428252"
FT   DOMAIN          36..105
FT                   /note="S1 motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          123..188
FT                   /note="S1 motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          209..277
FT                   /note="S1 motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          294..363
FT                   /note="S1 motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   REGION          429..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  53202 MW;  FD73D8A5D051DBE1 CRC64;
     MPSPTVTSPQ VAVNDIGSSE DFLAAIDKTI KYFNDGDIVE GTIVKVDRDE VLLDIGYKTE
     GVIPARELSI KHDVDPNEVV SVGDEVEALV LTKEDKEGRL ILSKKRAQYE RAWGTIEALK
     EKDEAVKGTV IEVVKGGLIL DIGLRGFLPA SLVEMRRVRD LQPYIGKEIE AKIIELDKNR
     NNVVLSRRAW LEQTQSEVRS EFLNNLQKGT IRKGVVSSIV NFGAFVDLGG VDGLVHVSEL
     SWKHIDHPSE VVQVGDEVTV EVLDVDMDRE RVSLSLKATQ EDPWRHFART HAIGQIVPGK
     VTKLVPFGAF VRVEEGIEGL VHISELAERH VEVPDQVVAV GDDAMVKVID IDLERRRISL
     SLKQANEDYT EEFDPAKYGM ADSYDEQGNY IFPEGFDAET NEWLEGFEKQ RAEWEARYAE
     AERRHKMHTA QMEKFAAAEA AGRGADDQSS ASSAPSEKTA GGSLASDAQL AALREKLAGS
     A