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Database: UniProt
Entry: A9MHX1_SALAR
LinkDB: A9MHX1_SALAR
Original site: A9MHX1_SALAR 
ID   A9MHX1_SALAR            Unreviewed;       557 AA.
AC   A9MHX1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   OrderedLocusNames=SARI_01981 {ECO:0000313|EMBL:ABX21861.1};
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX21861.1, ECO:0000313|Proteomes:UP000002084};
RN   [1] {ECO:0000313|EMBL:ABX21861.1, ECO:0000313|Proteomes:UP000002084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC   {ECO:0000313|Proteomes:UP000002084};
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
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DR   EMBL; CP000880; ABX21861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MHX1; -.
DR   STRING; 41514.SARI_01981; -.
DR   KEGG; ses:SARI_01981; -.
DR   HOGENOM; CLU_015805_2_1_6; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR   CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR   CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR   CDD; cd05689; S1_RPS1_repeat_ec4; 1.
DR   CDD; cd05690; S1_RPS1_repeat_ec5; 1.
DR   CDD; cd05691; S1_RPS1_repeat_ec6; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_bS1.
DR   InterPro; IPR035104; Ribosomal_protein_S1-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00717; rpsA; 1.
DR   PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR   PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002084};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          21..87
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          105..171
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          192..260
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          277..347
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          364..434
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          451..520
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   557 AA;  61187 MW;  351C2CF7981ECDB1 CRC64;
     MTESFAQLFE ESLKEIETRP GSIVRGVVVA IDKDIVLVDA GLKSESAIPA EQFKNAQGEL
     EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK AYEDAETVTG VINGKVKGGF
     TVELNGIRAF LPGSLVDVRP VRDTLHLEGK ELEFKVIKLD QKRNNVVVSR RAVIESENSA
     ERDQLLENLQ EGMEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
     INVKVLKFDR ERTRVSLGLK QLGEDPWVAI AKRYPEGTKL TGRVTNLTDY GCFVEIEEGV
     EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK SNPWQQFAET
     HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNV AGEEAVREYK KGDEIAAVVL
     QVDAERERIS LGVKQLAEDP FNNWVALNKK GAIVTGKVTA VDAKGATVEL ADGVEGYLRA
     SEASRDRVED ATLVLSVGDD VEAKFTGVDR KNRAISLSVR AKDEADEKDA IATVNKQEDA
     NFSNNAMAEA FKAAKGE
//
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