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Protein

Acid stress chaperone HdeB

Gene

hdeB

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, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.UniRule annotation1 Publication

GO - Molecular functioni

  • unfolded protein binding Source: EcoCyc

GO - Biological processi

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

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciEcoCyc:EG11399-MONOMER.
ECOL316407:JW5669-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid stress chaperone HdeBUniRule annotation
Alternative name(s):
10K-L protein
Gene namesi
Name:hdeBUniRule annotation
Synonyms:yhhD, yhiC
Ordered Locus Names:b3509, JW5669
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11399. hdeB.

Subcellular locationi

  • Periplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Mutants display increased sensitivity to acid stress at pH 2 and pH 3.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 562WW → AA: Folded, but does not form homodimers at pH 7. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929UniRule annotation4 PublicationsAdd
BLAST
Chaini30 – 10879Acid stress chaperone HdeBPRO_0000021405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AET2.
PRIDEiP0AET2.

2D gel databases

SWISS-2DPAGEP0AET2.

Expressioni

Inductioni

Induced by the EvgS/EvgA two-component regulatory system. Negatively regulated by H-NS and the TorS/TorR two-component regulatory system.3 Publications

Interactioni

Subunit structurei

Homodimer at neutral pH. Dissociates into monomers at acidic pH.2 Publications

GO - Molecular functioni

  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261137. 5 interactions.
DIPiDIP-47949N.
STRINGi511145.b3509.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363Combined sources
Helixi39 – 435Combined sources
Helixi47 – 5913Combined sources
Beta strandi66 – 683Combined sources
Helixi74 – 8916Combined sources
Helixi95 – 995Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYJNMR-A/B30-108[»]
2XUVX-ray1.50A/B/C/D30-108[»]
ProteinModelPortaliP0AET2.
SMRiP0AET2. Positions 30-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AET2.

Family & Domainsi

Sequence similaritiesi

Belongs to the HdeB family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105XXV. Bacteria.
ENOG41125MZ. LUCA.
HOGENOMiHOG000125815.
KOiK19778.
OMAiMNIASLR.

Family and domain databases

Gene3Di1.10.890.10. 1 hit.
HAMAPiMF_00947. HdeB. 1 hit.
InterProiIPR028623. HdeB.
IPR010486. HNS-dep_expression_A/B.
[Graphical view]
PfamiPF06411. HdeA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AET2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNISSLRKAF IFMGAVAALS LVNAQSALAA NESAKDMTCQ EFIDLNPKAM
60 70 80 90 100
TPVAWWMLHE ETVYKGGDTV TLNETDLTQI PKVIEYCKKN PQKNLYTFKN

QASNDLPN
Length:108
Mass (Da):12,043
Last modified:December 20, 2005 - v1
Checksum:i4E80163ACFD1399F
GO

Sequence cautioni

The sequence AAB18485 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA01884 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 9065 Da from positions 30 - 108. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11109 Genomic DNA. Translation: BAA01884.1. Different initiation.
U00039 Genomic DNA. Translation: AAB18485.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76534.2.
AP009048 Genomic DNA. Translation: BAE77785.1.
PIRiS30269.
RefSeqiNP_417966.4. NC_000913.3.
WP_001298717.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76534; AAC76534; b3509.
BAE77785; BAE77785; BAE77785.
GeneIDi948026.
KEGGiecj:JW5669.
eco:b3509.
PATRICi32122476. VBIEscCol129921_3616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11109 Genomic DNA. Translation: BAA01884.1. Different initiation.
U00039 Genomic DNA. Translation: AAB18485.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76534.2.
AP009048 Genomic DNA. Translation: BAE77785.1.
PIRiS30269.
RefSeqiNP_417966.4. NC_000913.3.
WP_001298717.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MYJNMR-A/B30-108[»]
2XUVX-ray1.50A/B/C/D30-108[»]
ProteinModelPortaliP0AET2.
SMRiP0AET2. Positions 30-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261137. 5 interactions.
DIPiDIP-47949N.
STRINGi511145.b3509.

2D gel databases

SWISS-2DPAGEP0AET2.

Proteomic databases

PaxDbiP0AET2.
PRIDEiP0AET2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76534; AAC76534; b3509.
BAE77785; BAE77785; BAE77785.
GeneIDi948026.
KEGGiecj:JW5669.
eco:b3509.
PATRICi32122476. VBIEscCol129921_3616.

Organism-specific databases

EchoBASEiEB1371.
EcoGeneiEG11399. hdeB.

Phylogenomic databases

eggNOGiENOG4105XXV. Bacteria.
ENOG41125MZ. LUCA.
HOGENOMiHOG000125815.
KOiK19778.
OMAiMNIASLR.

Enzyme and pathway databases

BioCyciEcoCyc:EG11399-MONOMER.
ECOL316407:JW5669-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AET2.
PROiP0AET2.

Family and domain databases

Gene3Di1.10.890.10. 1 hit.
HAMAPiMF_00947. HdeB. 1 hit.
InterProiIPR028623. HdeB.
IPR010486. HNS-dep_expression_A/B.
[Graphical view]
PfamiPF06411. HdeA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHDEB_ECOLI
AccessioniPrimary (citable) accession number: P0AET2
Secondary accession number(s): P26605, Q2M7H1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 82 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.