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Database: UniProt
Entry: A0A127JWV3_9BURK
LinkDB: A0A127JWV3_9BURK
Original site: A0A127JWV3_9BURK 
ID   A0A127JWV3_9BURK        Unreviewed;       558 AA.
AC   A0A127JWV3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:AMO24498.1};
GN   ORFNames=UC35_18710 {ECO:0000313|EMBL:AMO24498.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO24498.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO24498.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO24498.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and
RT   emended description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(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; CP010951; AMO24498.1; -; Genomic_DNA.
DR   RefSeq; WP_061502356.1; NZ_CP010951.1.
DR   EnsemblBacteria; AMO24498; AMO24498; UC35_18710.
DR   PATRIC; fig|94132.3.peg.3821; -.
DR   OrthoDB; 1235756at2; -.
DR   Proteomes; UP000070433; 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   Complete proteome {ECO:0000313|Proteomes:UP000070433};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:AMO24498.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       21     87       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      105    171       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      192    260       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      277    347       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      364    434       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      451    520       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   558 AA;  61445 MW;  E7CA5C1885CFAC3A CRC64;
     MSESFAQLFE ESLQRAEMRA GEVITAEVVR LEHSFVVVNA GLKSEAYVPI DEFKNDKGEI
     EVQVGDFVSV AIDAIENGYG DTILSRDKAK RLASWMALEK ALESGEFVTG TTSGKVKGGL
     TVLVNGIRAF LPGSLIDTRP IKDLTPYENK TLEFKVIKLD RKRNNVVLSR RAVVEASMGE
     ERAKLMETLK EGSIVRGVVK NITEYGAFVD LGGIDGLLHI TDMAWRRVRH PSEVVQAGQE
     ITAKILKFDT EKNRVSLGLK QMGDDPWMGV SRRYPTGTRM FGKITNIADY GAFVELEPGI
     EGLVHVSEMD WTNKNVAPSK IVSLGDEVEV MVLEIDEDKR RISLGMKQCK ANPWQEFAQN
     TRRGDRVKGP IKSITDFGVF VGLAAGIDGL VHLSDLSWNE PGEQAVRNYK KGQEVDAIVL
     AVDVDRERIS LGIKQLDADP FTTFTSVHDK GSSVTGKVKT VDAKGAEIDL GHEIFGYLRA
     SEISRDRVED ARNVLKEGDE VTAVVVNIDR KTRNIQLSIK AKDMADQQEA MSSLSAQSSR
     ESAGTTNLGA LLKAKLEK
//
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