ID A0A0U4V2D5_9GAMM Unreviewed; 557 AA.
AC A0A0U4V2D5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN Name=rpsA {ECO:0000313|EMBL:ALZ76855.1};
GN ORFNames=ATY27_14535 {ECO:0000313|EMBL:ALZ76855.1};
OS Rheinheimera sp. F8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ76855.1, ECO:0000313|Proteomes:UP000059499};
RN [1] {ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA Schuster A.K., Szewzyk U.;
RT "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT which produces large amounts of extracellular DNA.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALZ76855.1, ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:ALZ76855.1,
RC ECO:0000313|Proteomes:UP000059499};
RX PubMed=26966195;
RA Schuster A.K., Szewzyk U.;
RT "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT Which Produces Large Amounts of Extracellular DNA.";
RL Genome Announc. 4:0-0(2016).
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; CP013656; ALZ76855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4V2D5; -.
DR Proteomes; UP000059499; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000059499};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:ALZ76855.1}; 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 557 AA; 61258 MW; C0D0AAE1DB63C5DB CRC64;
MTENFAQLFE ESLKTIETRP GSIVKGRIVA IHKDVVLVDA GLKSEAAIPV EQFKNLAGEI
EVNVGDIIDV ALDAVEDGFG ETLLSREKAK RHESWVRLEK ACEDKVTVIG VITGKVKGGF
TVEVDGIRAF LPGSLVDVRP VRDTLHLEHK ELEFKVIKLD QKRNNVVVSR RAVIESESSA
ERDTLLQNLE EGMEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
IPVKVLKFDR EKQRVSLGLK QMGEDPWAAI ASRYPEGARI TGRVTNLTDY GCFVEIEEGV
EGLVHVSEMD WTNKNIHPSK VVNLGDSVEV MVLEIDEERR RISLGLKQCK ANPWEEFAKG
FNKGDRVSGK IKSITDFGIF IGLDGGIDGL VHLSDISWNS TGEDAVREFK KGDEVSAVVL
QVDPERERIS LGIKQLDEDP FNGYLADNKK GAIVKGTVTA VDAKGATVLL EGGVEGYVRV
SDIARERIED ATTALKVGEE VEARLMGVDR KNRVISLSIK AKFEAEEKEA LESIKQDDTA
FGGNAMAEAF KAAQKSE
//