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Database: UniProt
Entry: A0A241VD05_9GAMM
LinkDB: A0A241VD05_9GAMM
Original site: A0A241VD05_9GAMM 
ID   A0A241VD05_9GAMM        Unreviewed;       558 AA.
AC   A0A241VD05;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=B9T38_03455 {ECO:0000313|EMBL:OTG73480.1};
OS   Acinetobacter sp. ANC 4218.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977880 {ECO:0000313|EMBL:OTG73480.1, ECO:0000313|Proteomes:UP000194947};
RN   [1] {ECO:0000313|EMBL:OTG73480.1, ECO:0000313|Proteomes:UP000194947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4218 {ECO:0000313|EMBL:OTG73480.1,
RC   ECO:0000313|Proteomes:UP000194947};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-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:OTG73480.1}.
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DR   EMBL; NEGD01000003; OTG73480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241VD05; -.
DR   STRING; 1977880.B9T38_03455; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000194947; 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; 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:OTG73480.1}; 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   558 AA;  61109 MW;  9A3249E67E2697C6 CRC64;
     MTESFAALFE ESELNLNVEK GAVIQGVVVN IDSDWVTVDT GLKSEGIVDR AEFLNDQREL
     EVQVGDTVDV VVEALDNGMG QTVLSREKAK RAETWTKLEK IFEDGEIVTG VISGKVKGGF
     TVDIGPVRAF LPGSLVDTRP IRDTTHLEGK ELEFKVIKLD AKRNNVVVSR RAVMEAESSA
     DREALLAQLE EGQTVTGTIK NLTDYGAFVD LGGIDGLLHI TDMAWKRIKH PSEVVEVGQE
     VTVKVLKFDR ERNRVSLGLK QLGEDPWLAI MNRYPKGSIV KARVTNLTDY GCFAEIAEGV
     EGLVHVSEMD HTNKNIHPSK VVQIGDEVDV MVLEVDEERR RISLGIKQTR ANPWEEFAKD
     HDKGEKVSGT IKSITDFGIF IGLPGGIDGL VHLSDISWNE QGEEAIRRYK KGDTVEAVIL
     SVDAEGNRIS LGIKQMNSDP FNDFLAANER GALVKGTVTA VDARGATVKL ADEVEATLKA
     SEINRDRVED ATKFLEVGQE VEAKIINVDR KSRSINLSIK AKDEAEEKEA VANLKTAAAG
     QDNGPKTIGD LIKAQMGN
//
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