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Protein

Acid stress chaperone HdeA

Gene

hdeA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.4 Publications

GO - Molecular functioni

  • chaperone binding Source: EcoCyc

GO - Biological processi

  • cellular response to acidic pH Source: EcoCyc
  • cellular response to stress Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciEcoCyc:EG11398-MONOMER.
ECOL316407:JW3478-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid stress chaperone HdeAUniRule annotation
Alternative name(s):
10K-S protein
Gene namesi
Name:hdeAUniRule annotation
Synonyms:yhhC, yhiB
Ordered Locus Names:b3510, JW3478
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11398. hdeA.

Subcellular locationi

  • Periplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121UniRule annotation4 PublicationsAdd
BLAST
Chaini22 – 11089Acid stress chaperone HdeAPRO_0000021404Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 872 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AES9.
PRIDEiP0AES9.

2D gel databases

SWISS-2DPAGEP0AES9.

Expressioni

Inductioni

Activated by a low pH-induced dimer-to-monomer transition.

Interactioni

Subunit structurei

Homodimer at neutral pH. Dissociates into monomer at pH 4. Changes from a highly ordered form at pH above 3.1 to a highly disordered form at pH below 2.5 that is essential for its chaperone activity.1 Publication

GO - Molecular functioni

  • chaperone binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262518. 3 interactions.
DIPiDIP-47945N.
STRINGi511145.b3510.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363Combined sources
Helixi39 – 435Combined sources
Helixi47 – 493Combined sources
Helixi50 – 6213Combined sources
Helixi66 – 683Combined sources
Helixi73 – 8816Combined sources
Turni89 – 924Combined sources
Helixi95 – 1039Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG8X-ray2.20A/B/C22-110[»]
1DJ8X-ray2.00A/B/C/D/E/F22-110[»]
ProteinModelPortaliP0AES9.
SMRiP0AES9. Positions 30-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AES9.

Family & Domainsi

Sequence similaritiesi

Belongs to the HdeA family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41060V2. Bacteria.
ENOG41128BT. LUCA.
HOGENOMiHOG000125826.
KOiK19777.
OMAiVESEWEK.
OrthoDBiEOG6Q2SQ4.

Family and domain databases

Gene3Di1.10.890.10. 1 hit.
HAMAPiMF_00946. HdeA.
InterProiIPR024972. HdeA.
IPR010486. HNS-dep_expression_A/B.
[Graphical view]
PfamiPF06411. HdeA. 1 hit.
[Graphical view]
PIRSFiPIRSF009564. HNS-dep_expression_A. 1 hit.
ProDomiPD065392. HNS-dep_expression_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47752. SSF47752. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AES9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLGVILG GLLLLPVVSN AADAQKAADN KKPVNSWTCE DFLAVDESFQ
60 70 80 90 100
PTAVGFAEAL NNKDKPEDAV LDVQGIATVT PAIVQACTQD KQANFKDKVK
110
GEWDKIKKDM
Length:110
Mass (Da):11,858
Last modified:December 20, 2005 - v1
Checksum:i063262C4863FA2E9
GO

Mass spectrometryi

Molecular mass is 9742 Da from positions 22 - 110. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11109 Genomic DNA. Translation: BAA01883.1.
U00039 Genomic DNA. Translation: AAB18486.1.
U00096 Genomic DNA. Translation: AAC76535.1.
AP009048 Genomic DNA. Translation: BAE77784.1.
PIRiS30268.
RefSeqiNP_417967.1. NC_000913.3.
WP_000756550.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76535; AAC76535; b3510.
BAE77784; BAE77784; BAE77784.
GeneIDi948025.
KEGGiecj:JW3478.
eco:b3510.
PATRICi32122478. VBIEscCol129921_3617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11109 Genomic DNA. Translation: BAA01883.1.
U00039 Genomic DNA. Translation: AAB18486.1.
U00096 Genomic DNA. Translation: AAC76535.1.
AP009048 Genomic DNA. Translation: BAE77784.1.
PIRiS30268.
RefSeqiNP_417967.1. NC_000913.3.
WP_000756550.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG8X-ray2.20A/B/C22-110[»]
1DJ8X-ray2.00A/B/C/D/E/F22-110[»]
ProteinModelPortaliP0AES9.
SMRiP0AES9. Positions 30-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262518. 3 interactions.
DIPiDIP-47945N.
STRINGi511145.b3510.

2D gel databases

SWISS-2DPAGEP0AES9.

Proteomic databases

PaxDbiP0AES9.
PRIDEiP0AES9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76535; AAC76535; b3510.
BAE77784; BAE77784; BAE77784.
GeneIDi948025.
KEGGiecj:JW3478.
eco:b3510.
PATRICi32122478. VBIEscCol129921_3617.

Organism-specific databases

EchoBASEiEB1370.
EcoGeneiEG11398. hdeA.

Phylogenomic databases

eggNOGiENOG41060V2. Bacteria.
ENOG41128BT. LUCA.
HOGENOMiHOG000125826.
KOiK19777.
OMAiVESEWEK.
OrthoDBiEOG6Q2SQ4.

Enzyme and pathway databases

BioCyciEcoCyc:EG11398-MONOMER.
ECOL316407:JW3478-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AES9.
PROiP0AES9.

Family and domain databases

Gene3Di1.10.890.10. 1 hit.
HAMAPiMF_00946. HdeA.
InterProiIPR024972. HdeA.
IPR010486. HNS-dep_expression_A/B.
[Graphical view]
PfamiPF06411. HdeA. 1 hit.
[Graphical view]
PIRSFiPIRSF009564. HNS-dep_expression_A. 1 hit.
ProDomiPD065392. HNS-dep_expression_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47752. SSF47752. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant."
    Yoshida T., Ueguchi C., Yamada H., Mizuno T.
    Mol. Gen. Genet. 237:113-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-40.
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Physical map location of a set of Escherichia coli genes (hde) whose expression is affected by the nucleoid protein H-NS."
    Yoshida T., Ueguchi C., Mizuno T.
    J. Bacteriol. 175:7747-7748(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
  6. Cited for: PROTEIN SEQUENCE OF 22-41.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-33.
    Strain: K12 / EMG2.
  8. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-31.
    Strain: K12.
  9. "Gas-phase concentration, purification, and identification of whole proteins from complex mixtures."
    Reid G.E., Shang H., Hogan J.M., Lee G.U., McLuckey S.A.
    J. Am. Chem. Soc. 124:7353-7362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: ATCC 15597.
  10. "Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation."
    Hong W., Jiao W., Hu J., Zhang J., Liu C., Fu X., Shen D., Xia B., Chang Z.
    J. Biol. Chem. 280:27029-27034(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHAPERONE-LIKE PROTEIN.
  11. "Escherichia coli HdeB is an acid stress chaperone."
    Kern R., Malki A., Abdallah J., Tagourti J., Richarme G.
    J. Bacteriol. 189:603-610(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  12. "Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB."
    Malki A., Le H.-T., Milles S., Kern R., Caldas T., Abdallah J., Richarme G.
    J. Biol. Chem. 283:13679-13687(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROTEIN SOLUBILIZATION AT NEUTRAL PH.
  13. "A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance."
    Zhang M., Lin S., Song X., Liu J., Fu Y., Ge X., Fu X., Chang Z., Chen P.R.
    Nat. Chem. Biol. 7:671-677(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DISULFIDE BOND.
  15. "HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria."
    Gajiwala K.S., Burley S.K.
    J. Mol. Biol. 295:605-612(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND, SUBUNIT.

Entry informationi

Entry nameiHDEA_ECOLI
AccessioniPrimary (citable) accession number: P0AES9
Secondary accession number(s): P26604, Q2M7H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 16, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In vitro, HdeA is more efficient than HdeB at pH 2 and HdeB is more efficient than HdeA at pH 3. In vivo, both are required for optimal protection against acid stress at either pH 3 or pH 2 (PubMed:17085547).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.