USPE_ECOLI
ID USPE_ECOLI Reviewed; 316 AA.
AC P0AAC0; P03807; P77421;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Universal stress protein E;
GN Name=uspE; Synonyms=ydaA; OrderedLocusNames=b1333, JW1327;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RX PubMed=6292868; DOI=10.1093/nar/10.19.6119;
RA Shaw D.J., Guest J.R.;
RT "Nucleotide sequence of the fnr gene and primary structure of the Enr
RT protein of Escherichia coli.";
RL Nucleic Acids Res. 10:6119-6130(1982).
RN [5]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP FUNCTION, GENE NAME, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11849540; DOI=10.1046/j.1365-2958.2002.02720.x;
RA Gustavsson N., Diez A., Nystroem T.;
RT "The universal stress protein paralogues of Escherichia coli are co-
RT ordinately regulated and co-operate in the defence against DNA damage.";
RL Mol. Microbiol. 43:107-117(2002).
CC -!- FUNCTION: Required for resistance to DNA-damaging agents.
CC {ECO:0000269|PubMed:11849540}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: During growth inhibition caused by the exhaustion of any of
CC a variety of nutrients (carbon, nitrogen, phosphate, sulfate, required
CC amino acid) or by the presence of a variety of toxic agents. Positively
CC regulated by guanosine 3',5'-bisphosphate (ppGpp) and by a RecA/FtsK-
CC dependent regulatory pathway. {ECO:0000269|PubMed:11849540}.
CC -!- SIMILARITY: Belongs to the universal stress protein A family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74415.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14926.1; -; Genomic_DNA.
DR EMBL; J01608; AAA87982.1; -; Genomic_DNA.
DR PIR; H64882; QQECX.
DR RefSeq; NP_415849.1; NC_000913.3.
DR RefSeq; WP_001262123.1; NZ_STEB01000005.1.
DR PDB; 5CB0; X-ray; 3.21 A; A/B=1-316.
DR PDBsum; 5CB0; -.
DR AlphaFoldDB; P0AAC0; -.
DR SMR; P0AAC0; -.
DR BioGRID; 4260143; 13.
DR DIP; DIP-48118N; -.
DR IntAct; P0AAC0; 3.
DR MINT; P0AAC0; -.
DR STRING; 511145.b1333; -.
DR SWISS-2DPAGE; P0AAC0; -.
DR jPOST; P0AAC0; -.
DR PaxDb; P0AAC0; -.
DR PRIDE; P0AAC0; -.
DR EnsemblBacteria; AAC74415; AAC74415; b1333.
DR EnsemblBacteria; BAA14926; BAA14926; BAA14926.
DR GeneID; 66674839; -.
DR GeneID; 945904; -.
DR KEGG; ecj:JW1327; -.
DR KEGG; eco:b1333; -.
DR PATRIC; fig|1411691.4.peg.944; -.
DR EchoBASE; EB1227; -.
DR eggNOG; COG0589; Bacteria.
DR HOGENOM; CLU_049301_1_2_6; -.
DR InParanoid; P0AAC0; -.
DR OMA; MAKYQNM; -.
DR PhylomeDB; P0AAC0; -.
DR BioCyc; EcoCyc:EG11246-MON; -.
DR PRO; PR:P0AAC0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:EcoCyc.
DR GO; GO:0034644; P:cellular response to UV; IMP:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR DisProt; DP00991; -.
DR InterPro; IPR006016; UspA.
DR Pfam; PF00582; Usp; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9600841"
FT CHAIN 2..316
FT /note="Universal stress protein E"
FT /id="PRO_0000147417"
FT CONFLICT 55
FT /note="Missing (in Ref. 4; AAA87982)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..73
FT /note="AMRQGVISQRTAWIH -> RYASGRHQPAYSLDP (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5CB0"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 54..82
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:5CB0"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 215..236
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:5CB0"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5CB0"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5CB0"
SQ SEQUENCE 316 AA; 35707 MW; F5F416848D452378 CRC64;
MAMYQNMLVV IDPNQDDQPA LRRAVYLHQR IGGKIKAFLP IYDFSYEMTT LLSPDERTAM
RQGVISQRTA WIHEQAKYYL NAGVPIEIKV VWHNRPFEAI IQEVISGGHD LVLKMAHQHD
RLEAVIFTPT DWHLLRKCPS PVWMVKDQPW PEGGKALVAV NLASEEPYHN ALNEKLVKET
IELAEQVNHT EVHLVGAYPV TPINIAIELP EFDPSVYNDA IRGQHLLAMK ALRQKFGINE
NMTHVEKGLP EEVIPDLAEH LQAGIVVLGT VGRTGISAAF LGNTAEQVID HLRCDLLVIK
PDQYQTPVEL DDEEDD
