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
//