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Database: UniProt
Entry: V5SGW8_9RHIZ
LinkDB: V5SGW8_9RHIZ
Original site: V5SGW8_9RHIZ 
ID   V5SGW8_9RHIZ            Unreviewed;       579 AA.
AC   V5SGW8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=W911_17240 {ECO:0000313|EMBL:AHB49742.1};
OS   Hyphomicrobium nitrativorans NL23.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=1029756 {ECO:0000313|EMBL:AHB49742.1, ECO:0000313|Proteomes:UP000018542};
RN   [1] {ECO:0000313|EMBL:AHB49742.1, ECO:0000313|Proteomes:UP000018542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL23 {ECO:0000313|EMBL:AHB49742.1};
RX   PubMed=24435868;
RA   Martineau C., Villeneuve C., Mauffrey F., Villemur R.;
RT   "Complete Genome Sequence of Hyphomicrobium nitrativorans Strain NL23,
RT   a Denitrifying Bacterium Isolated from Biofilm of a Methanol-Fed
RT   Denitrification System Treating Seawater at the Montreal Biodome.";
RL   Genome Announc. 2:e01165-13(2014).
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the
CC       initiation point. It is needed to translate mRNA with a short
CC       Shine-Dalgarno (SD) purine-rich sequence.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
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DR   EMBL; CP006912; AHB49742.1; -; Genomic_DNA.
DR   RefSeq; WP_023788737.1; NC_022997.1.
DR   EnsemblBacteria; AHB49742; AHB49742; W911_17240.
DR   KEGG; hni:W911_17240; -.
DR   PATRIC; fig|1029756.8.peg.3588; -.
DR   KO; K02945; -.
DR   OrthoDB; 1235756at2; -.
DR   BioCyc; HNIT1029756:G1HM5-3354-MONOMER; -.
DR   Proteomes; UP000018542; Chromosome.
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   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_S1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; SSF50249; 6.
DR   TIGRFAMs; TIGR00717; rpsA; 1.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018542};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018542};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:AHB49742.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       32     98       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      116    182       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      203    271       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      288    358       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      375    445       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      461    531       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED       83    103       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   579 AA;  63526 MW;  DC34F4AA3816F9B4 CRC64;
     MTTEISKEYT PTRDEFAALL TESLAKDDVF EGSVVKGKVV GIEKDLAVID VGLKMEGRVP
     LKEFGVGGKL GDLKVGDTVE VYLERIENAL GEAVLSRDKA RREESWTRLE KLSEKGEKVT
     GVIFNKVKGG FTVDLDGAVA FLPGSQVDIR PVRDIGPLMH QPQQFQILKM DRRRGNIVVS
     RRSVLEETRA EQRADIVARL AEGQIIDGLV KNITDYGAFI DLGGIDGLLH VTDMAWRRVN
     HPSEILNVGD TVKVQIIRIN PETQRISLGM KQLQSDPWST IEAKYPIGSR FNGTVTNIAD
     YGAFVELEPG VEGLIHVSEM SWTKKNVHPG KIVSTSQQVE VQILEVDPGK RRISLGLKQT
     QDNPWDAFLA QHPKGTEVEG PIRNITEFGL FIGLEGGVDG MVHLSDLDWQ KAGDEVIKDY
     KKGDTVKAVV LDVDSSKERI SLGIKQLGGD PADALGKYKK GDQVTCEVIQ VQENGIEVRI
     ADSDLTTFIK RSDLSRDRSE QRAERFSVGQ KVDGAVLSVD KAARRIAVSI KALEIAEEKQ
     AVAQYGSSDS GASLGDIFKA AINKKRDAED GEGDEEESA
//
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