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Database: UniProt
Entry: A0A1K1NM54_9PROT
LinkDB: A0A1K1NM54_9PROT
Original site: A0A1K1NM54_9PROT 
ID   A0A1K1NM54_9PROT        Unreviewed;       545 AA.
AC   A0A1K1NM54;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=SAMN05216414_1245 {ECO:0000313|EMBL:SFW36357.1};
OS   Nitrosovibrio sp. Nv17.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosovibrio.
OX   NCBI_TaxID=1855339 {ECO:0000313|EMBL:SFW36357.1, ECO:0000313|Proteomes:UP000183249};
RN   [1] {ECO:0000313|EMBL:SFW36357.1, ECO:0000313|Proteomes:UP000183249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nv17 {ECO:0000313|EMBL:SFW36357.1,
RC   ECO:0000313|Proteomes:UP000183249};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPIQ01000024; SFW36357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1NM54; -.
DR   Proteomes; UP000183249; 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: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:UP000183249};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:SFW36357.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          4..70
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          88..154
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          175..243
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          260..330
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          347..417
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          434..503
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   545 AA;  60089 MW;  2B36251D06C8BC16 CRC64;
     MRVGEVITAE VVRVDYNIVV VNAGLKSESF IPVEEFKNDR GEIEVKPGDF VSVAIEALED
     GYGETRLSRD KAKRLTAWHD LEAAMASGAI VCGLVSGKVK GGLTAMINGI RAFLPGSLVD
     IRPVKDTTPY ENKEMEFKVI KLDRKRNNVV VSRRAVLEES QGADRQSLLA SLVEGAVVKG
     IVKNITDYGA FVDLGGIDGL LHITDLAWRR VKHPSEVISV GDEVTAKVLK FDQEKSRVSL
     GMKQLSEDPW VGLSRRYPQH TRLFGKVSNL TDYGAFVEIE QGIEGLVHVS EMDWTNKNVY
     PSKVVQLGDE VEVMILEIDE ERRRISLGMK QCKVNPWEDF ALNHQKGDKV RGQIKSITDF
     GVFIGLQGGI DGLVHLSDLS WNQAGEEAVR NYKKGDEVEA MVLSIDVERE RISLGIKQLE
     GDPFSGFVSV HDKNSVVRGT VKSIDAKGAV IALENDVEGY LRASEVSRDR VEDIRTHLKE
     GDAVEAMIIN IDRKNRSINL SIKAKDLHEE SDAIQKVASD NAGNAGTTSL GALLKAKMDV
     KNTEQ
//
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