HDEA_ECOLI
ID HDEA_ECOLI Reviewed; 110 AA.
AC P0AES9; P26604; Q2M7H2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acid stress chaperone HdeA {ECO:0000255|HAMAP-Rule:MF_00946};
DE AltName: Full=10K-S protein;
DE Flags: Precursor;
GN Name=hdeA {ECO:0000255|HAMAP-Rule:MF_00946}; Synonyms=yhhC, yhiB;
GN OrderedLocusNames=b3510, JW3478;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-40.
RC STRAIN=K12;
RX PubMed=8455549; DOI=10.1007/bf00282791;
RA Yoshida T., Ueguchi C., Yamada H., Mizuno T.;
RT "Function of the Escherichia coli nucleoid protein, H-NS: molecular
RT analysis of a subset of proteins whose expression is enhanced in a hns
RT deletion mutant.";
RL Mol. Gen. Genet. 237:113-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP GENE NAME.
RX PubMed=8244952; DOI=10.1128/jb.175.23.7747-7748.1993;
RA Yoshida T., Ueguchi C., Mizuno T.;
RT "Physical map location of a set of Escherichia coli genes (hde) whose
RT expression is affected by the nucleoid protein H-NS.";
RL J. Bacteriol. 175:7747-7748(1993).
RN [6]
RP PROTEIN SEQUENCE OF 22-41.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 22-33.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 22-31.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [9]
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 15597;
RX PubMed=12071744; DOI=10.1021/ja025966k;
RA Reid G.E., Shang H., Hogan J.M., Lee G.U., McLuckey S.A.;
RT "Gas-phase concentration, purification, and identification of whole
RT proteins from complex mixtures.";
RL J. Am. Chem. Soc. 124:7353-7362(2002).
RN [10]
RP FUNCTION AS A CHAPERONE-LIKE PROTEIN.
RX PubMed=15911614; DOI=10.1074/jbc.m503934200;
RA Hong W., Jiao W., Hu J., Zhang J., Liu C., Fu X., Shen D., Xia B.,
RA Chang Z.;
RT "Periplasmic protein HdeA exhibits chaperone-like activity exclusively
RT within stomach pH range by transforming into disordered conformation.";
RL J. Biol. Chem. 280:27029-27034(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17085547; DOI=10.1128/jb.01522-06;
RA Kern R., Malki A., Abdallah J., Tagourti J., Richarme G.;
RT "Escherichia coli HdeB is an acid stress chaperone.";
RL J. Bacteriol. 189:603-610(2007).
RN [12]
RP FUNCTION IN PROTEIN SOLUBILIZATION AT NEUTRAL PH.
RX PubMed=18359765; DOI=10.1074/jbc.m800869200;
RA Malki A., Le H.-T., Milles S., Kern R., Caldas T., Abdallah J.,
RA Richarme G.;
RT "Solubilization of protein aggregates by the acid stress chaperones HdeA
RT and HdeB.";
RL J. Biol. Chem. 283:13679-13687(2008).
RN [13]
RP FUNCTION.
RX PubMed=21892184; DOI=10.1038/nchembio.644;
RA Zhang M., Lin S., Song X., Liu J., Fu Y., Ge X., Fu X., Chang Z.,
RA Chen P.R.;
RT "A genetically incorporated crosslinker reveals chaperone cooperation in
RT acid resistance.";
RL Nat. Chem. Biol. 7:671-677(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=9731767; DOI=10.1038/1796;
RA Yang F., Gustafson K.R., Boyd M.R., Wlodawer A.;
RT "Crystal structure of Escherichia coli HdeA.";
RL Nat. Struct. Biol. 5:763-764(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND, AND SUBUNIT.
RX PubMed=10623550; DOI=10.1006/jmbi.1999.3347;
RA Gajiwala K.S., Burley S.K.;
RT "HDEA, a periplasmic protein that supports acid resistance in pathogenic
RT enteric bacteria.";
RL J. Mol. Biol. 295:605-612(2000).
CC -!- FUNCTION: Required for optimal acid stress protection. Exhibits a
CC chaperone-like activity only at pH below 3 by suppressing non-
CC specifically the aggregation of denaturated periplasmic proteins.
CC Important for survival of enteric bacteria in the acidic environment of
CC the host stomach. Also promotes the solubilization at neutral pH of
CC proteins that had aggregated in their presence at acidic pHs. May
CC cooperate with other periplasmic chaperones such as DegP and SurA.
CC {ECO:0000269|PubMed:15911614, ECO:0000269|PubMed:17085547,
CC ECO:0000269|PubMed:18359765, ECO:0000269|PubMed:21892184}.
CC -!- SUBUNIT: Homodimer at neutral pH. Dissociates into monomer at pH 4.
CC Changes from a highly ordered form at pH above 3.1 to a highly
CC disordered form at pH below 2.5 that is essential for its chaperone
CC activity. {ECO:0000269|PubMed:10623550}.
CC -!- INTERACTION:
CC P0AES9; P0AES9: hdeA; NbExp=2; IntAct=EBI-15826386, EBI-15826386;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00946,
CC ECO:0000269|PubMed:17085547}.
CC -!- INDUCTION: Activated by a low pH-induced dimer-to-monomer transition.
CC -!- MASS SPECTROMETRY: Mass=9742; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12071744};
CC -!- MISCELLANEOUS: In vitro, HdeA is more efficient than HdeB at pH 2 and
CC HdeB is more efficient than HdeA at pH 3. In vivo, both are required
CC for optimal protection against acid stress at either pH 3 or pH 2
CC (PubMed:17085547). {ECO:0000305|PubMed:17085547}.
CC -!- SIMILARITY: Belongs to the HdeA family. {ECO:0000255|HAMAP-
CC Rule:MF_00946}.
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DR EMBL; D11109; BAA01883.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18486.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76535.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77784.1; -; Genomic_DNA.
DR PIR; S30268; S30268.
DR RefSeq; NP_417967.1; NC_000913.3.
DR RefSeq; WP_000756550.1; NZ_SSZK01000042.1.
DR PDB; 1BG8; X-ray; 2.20 A; A/B/C=22-110.
DR PDB; 1DJ8; X-ray; 2.00 A; A/B/C/D/E/F=22-110.
DR PDBsum; 1BG8; -.
DR PDBsum; 1DJ8; -.
DR AlphaFoldDB; P0AES9; -.
DR BMRB; P0AES9; -.
DR SMR; P0AES9; -.
DR BioGRID; 4262518; 8.
DR DIP; DIP-47945N; -.
DR STRING; 511145.b3510; -.
DR SWISS-2DPAGE; P0AES9; -.
DR jPOST; P0AES9; -.
DR PaxDb; P0AES9; -.
DR PRIDE; P0AES9; -.
DR EnsemblBacteria; AAC76535; AAC76535; b3510.
DR EnsemblBacteria; BAE77784; BAE77784; BAE77784.
DR GeneID; 66672606; -.
DR GeneID; 948025; -.
DR KEGG; ecj:JW3478; -.
DR KEGG; eco:b3510; -.
DR PATRIC; fig|511145.12.peg.3617; -.
DR EchoBASE; EB1370; -.
DR eggNOG; ENOG5032Y4G; Bacteria.
DR HOGENOM; CLU_170142_1_0_6; -.
DR OMA; ACTENKK; -.
DR BioCyc; EcoCyc:EG11398-MON; -.
DR EvolutionaryTrace; P0AES9; -.
DR PRO; PR:P0AES9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071468; P:cellular response to acidic pH; IMP:EcoCyc.
DR GO; GO:1990451; P:cellular stress response to acidic pH; IEA:UniProtKB-UniRule.
DR DisProt; DP02548; -.
DR Gene3D; 1.10.890.10; -; 1.
DR HAMAP; MF_00946; HdeA; 1.
DR InterPro; IPR024972; HdeA.
DR InterPro; IPR038303; HdeA/HdeB_sf.
DR InterPro; IPR036831; HdeA_sf.
DR InterPro; IPR010486; HNS-dep_expression_A/B.
DR Pfam; PF06411; HdeA; 1.
DR PIRSF; PIRSF009564; HNS-dep_expression_A; 1.
DR SUPFAM; SSF47752; SSF47752; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Disulfide bond;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00946,
FT ECO:0000269|PubMed:8455549, ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9868784, ECO:0000269|Ref.6"
FT CHAIN 22..110
FT /note="Acid stress chaperone HdeA"
FT /id="PRO_0000021404"
FT DISULFID 39..87
FT /evidence="ECO:0000269|PubMed:10623550,
FT ECO:0000269|PubMed:9731767"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:1DJ8"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1DJ8"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:1DJ8"
SQ SEQUENCE 110 AA; 11858 MW; 063262C4863FA2E9 CRC64;
MKKVLGVILG GLLLLPVVSN AADAQKAADN KKPVNSWTCE DFLAVDESFQ PTAVGFAEAL
NNKDKPEDAV LDVQGIATVT PAIVQACTQD KQANFKDKVK GEWDKIKKDM
