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Database: UniProt
Entry: A0A0B1YK73_9RALS
LinkDB: A0A0B1YK73_9RALS
Original site: A0A0B1YK73_9RALS 
ID   A0A0B1YK73_9RALS        Unreviewed;       562 AA.
AC   A0A0B1YK73;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:KHK58930.1};
GN   ORFNames=PI87_04230 {ECO:0000313|EMBL:KHK58930.1};
OS   Ralstonia sp. A12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1217052 {ECO:0000313|EMBL:KHK58930.1, ECO:0000313|Proteomes:UP000030970};
RN   [1] {ECO:0000313|EMBL:KHK58930.1, ECO:0000313|Proteomes:UP000030970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A12 {ECO:0000313|EMBL:KHK58930.1,
RC   ECO:0000313|Proteomes:UP000030970};
RA   Chen J.W., Yin W.F., Chan K.G.;
RT   "Draft Genome of Ralstonia A12.";
RL   Submitted (NOV-2014) 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|ARBA:ARBA00025604,
CC       ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHK58930.1}.
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DR   EMBL; JSZO01000001; KHK58930.1; -; Genomic_DNA.
DR   RefSeq; WP_039596369.1; NZ_JSZO01000001.1.
DR   AlphaFoldDB; A0A0B1YK73; -.
DR   STRING; 1217052.PI87_04230; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000030970; Unassembled WGS sequence.
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; 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:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:KHK58930.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          24..90
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          108..174
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          195..263
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          280..350
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          367..437
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          454..523
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   562 AA;  61529 MW;  4A15D078C2F12D69 CRC64;
     MSQINESFAA LFEESIAKSN MKAGEVISAE VVRIDHNFVV VNAGLKSEAF VPVEEFLNDQ
     GELEVQVGDY VSVAIDALEN GYGDTILSRD KAKRLASWLN LEKALESGEI ISGTVTGKVK
     GGLTVMVNGI RAFLPGSLVD VRPIKDTTPY EGKTLEFKVI KLDRKRNNVV LSRRAVVEAT
     LGEERQKLME TLKEGAIVNG IVKNITDYGA FVDLGGIDGL LHITDLAWRR VRHPSEVLSV
     GQEITAKILK FDQEKNRVSL GVKQLGEDPW VGISRRYPQG TRLFGKVTNL TDYGAFVEIE
     AGIEGLVHVS EMDWTNKNVA PSKVVQLGDE VEVMVLDIDE DKRRISLGMK QCKANPWDDF
     GRNHKKGDKL SGQIKSITDF GVFIGLPGGI DGLVHLSDLS WQETGEEAVR KYKKGDEVEA
     VVLAIDIDKE RISLGIKQLS GDPFNNFVST NDKGSIVQVT IKTVDPKGAV VQLADDVEGY
     LRASEISSDR VEDARNVLKE GETMTAMIVN IDRKSRNINV SIKAKDSADQ QEAMQKFSAD
     TGAAGTTNLG ALLKAKLNET NQ
//
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