YAAA_ECOLI
ID YAAA_ECOLI Reviewed; 258 AA.
AC P0A8I3; P11288;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Peroxide stress resistance protein YaaA {ECO:0000305};
DE AltName: Full=UPF0246 protein YaaA {ECO:0000305};
GN Name=yaaA; OrderedLocusNames=b0006, JW0005;
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;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 133-258.
RX PubMed=6316258; DOI=10.1093/nar/11.21.7331;
RA Parsot C., Cossart P., Saint-Girons I., Cohen G.N.;
RT "Nucleotide sequence of thrC and of the transcription termination region of
RT the threonine operon in Escherichia coli K12.";
RL Nucleic Acids Res. 11:7331-7345(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 138-258.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21378183; DOI=10.1128/jb.00001-11;
RA Liu Y., Bauer S.C., Imlay J.A.;
RT "The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen
RT peroxide toxicity by diminishing the amount of intracellular unincorporated
RT iron.";
RL J. Bacteriol. 193:2186-2196(2011).
RN [8] {ECO:0007744|PDB:5CAJ}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-258.
RA Prahlad J., Wilson M.A.;
RT "Crystal structure of E. coli YaaA, a member of the DUF328/UPF0246
RT family.";
RL Submitted (JUN-2015) to the PDB data bank.
CC -!- FUNCTION: Involved in the cellular response to hydrogen peroxide
CC (H(2)O(2)) stress. During H(2)O(2) stress, prevents oxidative damage to
CC both DNA and proteins by diminishing the amount of unincorporated iron
CC within the cell. {ECO:0000269|PubMed:21378183}.
CC -!- INDUCTION: Induced by H(2)O(2), via OxyR.
CC {ECO:0000269|PubMed:21378183}.
CC -!- DISRUPTION PHENOTYPE: In a catalase/peroxidase-deficient (Hpx(-))
CC background, yaaA deletion mutants grow poorly and form filaments in
CC aerobic medium. Mutants show higher levels of DNA damage and
CC polypeptide damage during H(2)O(2) stress. They also have an unusually
CC high level of intracellular unincorporated iron.
CC {ECO:0000269|PubMed:21378183}.
CC -!- SIMILARITY: Belongs to the UPF0246 family. {ECO:0000255|HAMAP-
CC Rule:MF_00652}.
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DR EMBL; U00096; AAC73117.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96584.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97304.1; -; Genomic_DNA.
DR PIR; S40534; Q3ECTC.
DR RefSeq; NP_414547.1; NC_000913.3.
DR RefSeq; WP_000906197.1; NZ_LN832404.1.
DR PDB; 5CAJ; X-ray; 1.65 A; A/B=2-258.
DR PDBsum; 5CAJ; -.
DR AlphaFoldDB; P0A8I3; -.
DR SMR; P0A8I3; -.
DR BioGRID; 4261937; 18.
DR BioGRID; 849152; 1.
DR DIP; DIP-35783N; -.
DR IntAct; P0A8I3; 6.
DR STRING; 511145.b0006; -.
DR jPOST; P0A8I3; -.
DR PaxDb; P0A8I3; -.
DR PRIDE; P0A8I3; -.
DR EnsemblBacteria; AAC73117; AAC73117; b0006.
DR EnsemblBacteria; BAB96584; BAB96584; BAB96584.
DR GeneID; 58461419; -.
DR GeneID; 944749; -.
DR KEGG; ecj:JW0005; -.
DR KEGG; eco:b0006; -.
DR PATRIC; fig|1411691.4.peg.2277; -.
DR EchoBASE; EB0011; -.
DR eggNOG; COG3022; Bacteria.
DR HOGENOM; CLU_061989_0_0_6; -.
DR InParanoid; P0A8I3; -.
DR OMA; WKNGQYK; -.
DR PhylomeDB; P0A8I3; -.
DR BioCyc; EcoCyc:EG10011-MON; -.
DR PRO; PR:P0A8I3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000217; F:DNA secondary structure binding; IDA:EcoCyc.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:EcoCyc.
DR HAMAP; MF_00652; UPF0246; 1.
DR InterPro; IPR005583; YaaA.
DR PANTHER; PTHR30283; PTHR30283; 1.
DR Pfam; PF03883; H2O2_YaaD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Stress response.
FT CHAIN 1..258
FT /note="Peroxide stress resistance protein YaaA"
FT /id="PRO_0000203983"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:5CAJ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5CAJ"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:5CAJ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5CAJ"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5CAJ"
SQ SEQUENCE 258 AA; 29586 MW; 050257199733C8F6 CRC64;
MLILISPAKT LDYQSPLTTT RYTLPELLDN SQQLIHEARK LTPPQISTLM RISDKLAGIN
AARFHDWQPD FTPANARQAI LAFKGDVYTG LQAETFSEDD FDFAQQHLRM LSGLYGVLRP
LDLMQPYRLE MGIRLENARG KDLYQFWGDI ITNKLNEALA AQGDNVVINL ASDEYFKSVK
PKKLNAEIIK PVFLDEKNGK FKIISFYAKK ARGLMSRFII ENRLTKPEQL TGFNSEGYFF
DEDSSSNGEL VFKRYEQR
