HSLR_ECOLI
ID HSLR_ECOLI Reviewed; 133 AA.
AC P0ACG8; P45802; Q2M765;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Heat shock protein 15;
DE Short=HSP15;
GN Name=hslR; Synonyms=yrfH; OrderedLocusNames=b3400, JW3363;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-9.
RX PubMed=9867837; DOI=10.1074/jbc.274.1.249;
RA Korber P., Zander T., Herschlag D., Bardwell J.C.A.;
RT "A new heat shock protein that binds nucleic acids.";
RL J. Biol. Chem. 274:249-256(1999).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10675343; DOI=10.1093/emboj/19.4.741;
RA Korber P., Stahl J.M., Nierhaus K.H., Bardwell J.C.A.;
RT "Hsp15: a ribosome-associated heat shock protein.";
RL EMBO J. 19:741-748(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10675344; DOI=10.1093/emboj/19.4.749;
RA Staker B.L., Korber P., Bardwell J.C.A., Saper M.A.;
RT "Structure of Hsp15 reveals a novel RNA-binding motif.";
RL EMBO J. 19:749-757(2000).
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.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P0ACG8; P06993: malT; NbExp=2; IntAct=EBI-562824, EBI-542934;
CC P0ACG8; P28224: mliC; NbExp=3; IntAct=EBI-562824, EBI-562851;
CC P0ACG8; P0A7V0: rpsB; NbExp=3; IntAct=EBI-562824, EBI-543439;
CC P0ACG8; Q79E92: ykgN; NbExp=2; IntAct=EBI-562824, EBI-9131095;
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the HSP15 family. {ECO:0000305}.
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DR EMBL; U18997; AAA58197.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76425.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77891.1; -; Genomic_DNA.
DR PIR; C65135; C65135.
DR RefSeq; NP_417859.1; NC_000913.3.
DR RefSeq; WP_000660483.1; NZ_SSZK01000008.1.
DR PDB; 1DM9; X-ray; 2.00 A; A/B=1-133.
DR PDB; 3BBU; EM; 10.00 A; A=5-108.
DR PDBsum; 1DM9; -.
DR PDBsum; 3BBU; -.
DR AlphaFoldDB; P0ACG8; -.
DR SMR; P0ACG8; -.
DR BioGRID; 4260979; 268.
DR BioGRID; 852221; 13.
DR DIP; DIP-48014N; -.
DR IntAct; P0ACG8; 37.
DR STRING; 511145.b3400; -.
DR jPOST; P0ACG8; -.
DR PaxDb; P0ACG8; -.
DR PRIDE; P0ACG8; -.
DR EnsemblBacteria; AAC76425; AAC76425; b3400.
DR EnsemblBacteria; BAE77891; BAE77891; BAE77891.
DR GeneID; 947912; -.
DR KEGG; ecj:JW3363; -.
DR KEGG; eco:b3400; -.
DR PATRIC; fig|1411691.4.peg.3330; -.
DR EchoBASE; EB2765; -.
DR eggNOG; COG1188; Bacteria.
DR HOGENOM; CLU_101003_2_1_6; -.
DR InParanoid; P0ACG8; -.
DR OMA; IDKYLWC; -.
DR PhylomeDB; P0ACG8; -.
DR BioCyc; EcoCyc:G7743-MON; -.
DR EvolutionaryTrace; P0ACG8; -.
DR PRO; PR:P0ACG8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:EcoCyc.
DR GO; GO:0034605; P:cellular response to heat; IEP:EcoCyc.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Reference proteome;
KW RNA-binding; Stress response.
FT CHAIN 1..133
FT /note="Heat shock protein 15"
FT /id="PRO_0000201741"
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"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1DM9"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1DM9"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1DM9"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1DM9"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1DM9"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:1DM9"
SQ SEQUENCE 133 AA; 15496 MW; 4B3D40FAECC42D5B CRC64;
MKEKPAVEVR LDKWLWAARF YKTRALAREM IEGGKVHYNG QRSKPSKIVE LNATLTLRQG
NDERTVIVKA ITEQRRPASE AALLYEETAE SVEKREKMAL ARKLNALTMP HPDRRPDKKE
RRDLLRFKHG DSE
