ID   HSLR_ECOL6              Reviewed;         133 AA.
AC   P0ACG9; P45802;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Heat shock protein 15;
DE            Short=HSP15;
GN   Name=hslR; OrderedLocusNames=c4171;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in the recycling of free 50S ribosomal subunits that
CC       still carry a nascent chain. Binds RNA more specifically than DNA.
CC       Binds with very high affinity to the free 50S ribosomal subunit. Does
CC       not bind it when it is part of the 70S ribosome (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HSP15 family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82609.1; -; Genomic_DNA.
DR   RefSeq; WP_000660483.1; NC_004431.1.
DR   AlphaFoldDB; P0ACG9; -.
DR   SMR; P0ACG9; -.
DR   STRING; 199310.c4171; -.
DR   PRIDE; P0ACG9; -.
DR   EnsemblBacteria; AAN82609; AAN82609; c4171.
DR   KEGG; ecc:c4171; -.
DR   eggNOG; COG1188; Bacteria.
DR   HOGENOM; CLU_101003_2_1_6; -.
DR   OMA; IDKYLWC; -.
DR   BioCyc; ECOL199310:C4171-MON; -.
DR   Proteomes; UP000001410; 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; -; 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   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   DNA-binding; RNA-binding; Stress response.
FT   CHAIN           1..133
FT                   /note="Heat shock protein 15"
FT                   /id="PRO_0000201743"
FT   DOMAIN          9..71
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   REGION          105..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   133 AA;  15496 MW;  4B3D40FAECC42D5B CRC64;
     MKEKPAVEVR LDKWLWAARF YKTRALAREM IEGGKVHYNG QRSKPSKIVE LNATLTLRQG
     NDERTVIVKA ITEQRRPASE AALLYEETAE SVEKREKMAL ARKLNALTMP HPDRRPDKKE
     RRDLLRFKHG DSE