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Database: UniProt
Entry: Q5NGU2_FRATT
LinkDB: Q5NGU2_FRATT
Original site: Q5NGU2_FRATT 
ID   Q5NGU2_FRATT            Unreviewed;       122 AA.
AC   Q5NGU2; A0A0G2RPJ1;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Heat shock protein 15 {ECO:0000256|PIRNR:PIRNR016821};
GN   Name=hslR {ECO:0000313|EMBL:CAG45372.1};
GN   OrderedLocusNames=FTT_0739c {ECO:0000313|EMBL:CAG45372.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45372.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG45372.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- SIMILARITY: Belongs to the HSP15 family.
CC       {ECO:0000256|ARBA:ARBA00008396, ECO:0000256|PIRNR:PIRNR016821}.
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DR   EMBL; AJ749949; CAG45372.1; -; Genomic_DNA.
DR   RefSeq; WP_003020573.1; NZ_CP010290.1.
DR   RefSeq; YP_169750.1; NC_006570.2.
DR   AlphaFoldDB; Q5NGU2; -.
DR   DNASU; 3190937; -.
DR   EnsemblBacteria; CAG45372; CAG45372; FTT_0739c.
DR   KEGG; ftu:FTT_0739c; -.
DR   PATRIC; fig|177416.36.peg.67; -.
DR   OrthoDB; 9797176at2; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:InterPro.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0034605; P:cellular response to heat; IEA:InterPro.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   InterPro; IPR025708; HSP15.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   Pfam; PF01479; S4; 1.
DR   PIRSF; PIRSF016821; HSP15; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR016821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR016821};
KW   Stress response {ECO:0000313|EMBL:CAG45372.1}.
FT   DOMAIN          3..66
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          97..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  14267 MW;  F0F9B1EDC2EF470B CRC64;
     MSVRLDKWLW ATRFYKTRAL AKKAIEGGKV HFQGQKTKVS KIVNIGDTYQ IQQGYIKKTV
     IVEALDEVRK SASEAQKLYR ETAESIEKRE QETILRKTAN LISPEKPTKK QRRQIIDFKR
     ND
//
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