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Database: UniProt
Entry: A0A2A2ADV1_9BURK
LinkDB: A0A2A2ADV1_9BURK
Original site: A0A2A2ADV1_9BURK 
ID   A0A2A2ADV1_9BURK        Unreviewed;       562 AA.
AC   A0A2A2ADV1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=CK625_09440 {ECO:0000313|EMBL:PAT36705.1};
OS   Vandammella animalimorsus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Vandammella.
OX   NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT36705.1, ECO:0000313|Proteomes:UP000218054};
RN   [1] {ECO:0000313|EMBL:PAT36705.1, ECO:0000313|Proteomes:UP000218054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT36705.1,
RC   ECO:0000313|Proteomes:UP000218054};
RA   Bernier A.-M., Bernard K.;
RT   "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT   infections in humans.";
RL   Submitted (AUG-2017) 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:PAT36705.1}.
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DR   EMBL; NSJB01000007; PAT36705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2ADV1; -.
DR   Proteomes; UP000218054; 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   Reference proteome {ECO:0000313|Proteomes:UP000218054};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:PAT36705.1}; 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   562 AA;  61274 MW;  EEB25273EE689BAB CRC64;
     MSESFAALFE ESLQRTEMRP GEVITAEVVR IEHNFVVVNA GLKSESFIPL EEFKNDQGEV
     EVQVGDFVSV AIGSIENGYG DTILSRDTAK RLASWLALEK ALESGEFVTG TTSGRVKGGL
     TVLVNGIRAF LPGSLVDTRP VKDLTPYENK TMEFKVIKLD RKRNNVVLSH RAVVEASMGE
     EREKLLATLK EGAIVNGVVK NITEYGAFVD LGGIDGLLHI TDMAWRRVRH PSEVVQAGQE
     ITAKVLKFDA EKSRVSLGLK QMGEDPWIGV SRRYPANTRL YGKVTNIAEY GAFVELEPGI
     EGLVHVSEMD WTNKNVAPSK VVSLGEEVEV MVLDIDEDKR RISLGMKQTK VNPWKDFAQN
     TNRGDRVKGP IKSITDFGVF VGLASGIDGL VHLSDLSWNE PGESAVRNYK KGQEVEAIVL
     AVDVDRERIS LGIKQLDADP FTTFVSVNDR GQAVTGKVKS VDAKGAEIEL GEDVTGYLRA
     SDISADRVED ARNVLKEGDE VTAVITNIDR KNRSIQLSIK AKDAADQQEA LDHLAQQSAG
     NAGTTSLGAL LKAKLGGAVE EK
//
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