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Database: UniProt
Entry: A0A0A7PGV7_9SPHN
LinkDB: A0A0A7PGV7_9SPHN
Original site: A0A0A7PGV7_9SPHN 
ID   A0A0A7PGV7_9SPHN        Unreviewed;       570 AA.
AC   A0A0A7PGV7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:AJA09179.1};
GN   ORFNames=SKP52_11405 {ECO:0000313|EMBL:AJA09179.1};
OS   Sphingopyxis fribergensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA09179.1, ECO:0000313|Proteomes:UP000030907};
RN   [1] {ECO:0000313|EMBL:AJA09179.1, ECO:0000313|Proteomes:UP000030907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA09179.1,
RC   ECO:0000313|Proteomes:UP000030907};
RX   PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA   Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA   Tischler D.;
RT   "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT   the ability to degrade styrene and phenylacetic acid.";
RL   Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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}.
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DR   EMBL; CP009122; AJA09179.1; -; Genomic_DNA.
DR   RefSeq; WP_039574807.1; NZ_CP009122.1.
DR   AlphaFoldDB; A0A0A7PGV7; -.
DR   STRING; 1515612.SKP52_11405; -.
DR   KEGG; sphk:SKP52_11405; -.
DR   HOGENOM; CLU_015805_2_1_5; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000030907; 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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 5.
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:AJA09179.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          29..95
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          113..179
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          200..268
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          285..355
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          372..442
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          464..533
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   570 AA;  61597 MW;  C3272A0D11EC0FCF CRC64;
     MATTAFPTRD DFAAMLDESL GGADGGFEGR VVKGTVTAIE NDLAVIDIGL KSEGRVPLRE
     FAMPGQKADI NVGDEVEVYV DRVENANGET MLSRDRARRE AAWDRLEEEF NKEARVEGVI
     FGRVKGGFTV DLGGAVAFLP GSQVDIRPVR DVGPLMDLPQ PFQILKMDRR RGNIVVSRRA
     ILEETRAEQR SGLILNLEEG QIIEGAVKNI TDYGAFVDLG GIDGLLHVTD MSYKRVNHPS
     EVINIGDTVR VQIIRINRDT QRISLGMKQL ESDPWEGVAA KYPVGAKLSG TVTNITDYGA
     FVELEAGIEG LVHVSEMSWV KKNVHPGKIV STSQEVDVIV LEVDSDKRRI SLGLKQAQSN
     PWGAFAETHP VGSVVEGEVK NATEFGLFVG LPGDVDGMVH MSDIAWGISG EEALHLHRKG
     EAVQVVVLDV DVEKERISLG IKQLEKGAPA VGGGTAAAGS VKKNDVVTVT VLEVRDNGLE
     VQAGDDGATG FIKRADLGRD RDEQRAERYQ VGQKFDAMVI GFDRSKKPNF SVKAMQIAEE
     KQAVAQYGSS DSGASLGDIL GEALKAGKKD
//
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