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Protein

Hemolysin expression-modulating protein Hha

Gene

hha

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

Functioni

Down-regulates hemolysin (hly) expression in complex with H-NS (PubMed:1956303, PubMed:10778755, PubMed:11790731, PubMed:21600204). Stimulates transposition events in vivo (PubMed:8145648). Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex (PubMed:23543115). Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS (PubMed:23543115). Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR (PubMed:19909729). Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes (PubMed:18545668).9 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei25 – 251Interacts with H-NS
Sitei48 – 481Interacts with H-NS

GO - Biological processi

  • regulation of gene expression Source: EcoCyc
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG10439-MONOMER.
ECOL316407:JW0449-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemolysin expression-modulating protein Hha
Gene namesi
Name:hha
Ordered Locus Names:b0460, JW0449
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10439. hha.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Deletion results in a large increase in the production of extracellular and intracellular hemolysin (PubMed:1956303). At low osmolarity minor changes in overall translation, at 0.4 M NaCl expression of about 25 proteins altered, including decreased OmpA, crr and AhpC (in strain 5K, not a K12 derivative) (PubMed:10322001). At 0.3 M NaCl in strain W3110 up-regulation of 113 genes and down-regulation of 8 genes was observed; a double cnu-hha deletion up-regulated 134 and down-regulated 5 genes, most of which are thought to have been acquired horizontally and are also up-regulated in double hns-stpA deletions (PubMed:23543115). However there are only 12 genes that were commonly up-regulated in the hha and cnu-hha deletions (PubMed:23543115). Represses the production of persister cells (PubMed:19909729). Deletion of hha and tomB (ybaJ), in the presence of a conjugative plasmid (R1drd19), decreases biofilm formation, cell aggregation and increases motility via flagella and motility gene expression (PubMed:16317765).5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → N: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi16 – 161R → C: Derepression of the hly operon, impaired H-NS binding. 1 Publication
Mutagenesisi22 – 221D → N: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi25 – 251E → Q: Affects H-NS binding ability. Decrease in the ability to repress the expression of the hly operon. 1 Publication
Mutagenesisi29 – 291E → Q: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi34 – 341E → Q: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi37 – 371D → N: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi39 – 391E → Q: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi44 – 7229Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd
BLAST
Mutagenesisi48 – 481D → E or R: Abolishes the interaction with H-NS. 1 Publication
Mutagenesisi48 – 481D → N: Abolishes the interaction with H-NS. Loss of the ability to repress the expression of the hly operon. 1 Publication
Mutagenesisi50 – 501R → H: Derepression of the hly operon, impaired H-NS binding. 1 Publication
Mutagenesisi58 – 7215Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd
BLAST
Mutagenesisi61 – 611D → N: Does not affect H-NS binding ability. 1 Publication
Mutagenesisi64 – 641P → L or S: Derepression of the hly operon, impaired H-NS binding. 1 Publication
Mutagenesisi72 – 721R → RHHHHHH: Derepression of the hly operon, impaired H-NS binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7272Hemolysin expression-modulating protein HhaPRO_0000201727Add
BLAST

Proteomic databases

PaxDbiP0ACE3.
PRIDEiP0ACE3.

Expressioni

Inductioni

Expression is autoregulated (Probable). Induced during biofilm formation (PubMed:14727089, PubMed:18545668).Curated2 Publications

Interactioni

Subunit structurei

Forms a heterotrimeric complex with the H-NS dimer in the absence of DNA.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hnsP0ACF85EBI-1122578,EBI-544934

Protein-protein interaction databases

BioGridi4262034. 9 interactions.
DIPiDIP-9897N.
IntActiP0ACE3. 2 interactions.
MINTiMINT-8175118.
STRINGi511145.b0460.

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Helixi21 – 3414Combined sources
Helixi37 – 5519Combined sources
Beta strandi56 – 583Combined sources
Helixi65 – 706Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW2NMR-A1-72[»]
2MW2NMR-A1-72[»]
ProteinModelPortaliP0ACE3.
SMRiP0ACE3. Positions 1-72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACE3.

Family & Domainsi

Domaini

Histidine-tagging (His-tagging) at the N-terminus does not impair interaction with H-NS, whereas His-tagging at the C-terminus does impair interaction (PubMed:11790731).1 Publication

Sequence similaritiesi

Belongs to the Hha/YmoA/Cnu family.2 Publications

Phylogenomic databases

eggNOGiENOG4105KF5. Bacteria.
ENOG4111U15. LUCA.
HOGENOMiHOG000219358.
KOiK05839.
OMAiRRCQSID.

Family and domain databases

Gene3Di1.20.1280.40. 1 hit.
InterProiIPR007985. Hemolysn_expr_modulating_HHA.
[Graphical view]
PfamiPF05321. HHA. 1 hit.
[Graphical view]
SUPFAMiSSF68989. SSF68989. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ACE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKPLTKTD YLMRLRRCQT IDTLERVIEK NKYELSDNEL AVFYSAADHR
60 70
LAELTMNKLY DKIPSSVWKF IR
Length:72
Mass (Da):8,628
Last modified:November 22, 2005 - v1
Checksum:iA77211B87CF0134A
GO

Sequence cautioni

The sequence AAB40215 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57977 Genomic DNA. Translation: CAA41043.1.
U82664 Genomic DNA. Translation: AAB40215.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73562.1.
AP009048 Genomic DNA. Translation: BAE76239.1.
PIRiC64776.
RefSeqiNP_414993.1. NC_000913.3.
WP_001291435.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73562; AAC73562; b0460.
BAE76239; BAE76239; BAE76239.
GeneIDi945098.
KEGGiecj:JW0449.
eco:b0460.
PATRICi32116073. VBIEscCol129921_0478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57977 Genomic DNA. Translation: CAA41043.1.
U82664 Genomic DNA. Translation: AAB40215.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73562.1.
AP009048 Genomic DNA. Translation: BAE76239.1.
PIRiC64776.
RefSeqiNP_414993.1. NC_000913.3.
WP_001291435.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW2NMR-A1-72[»]
2MW2NMR-A1-72[»]
ProteinModelPortaliP0ACE3.
SMRiP0ACE3. Positions 1-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262034. 9 interactions.
DIPiDIP-9897N.
IntActiP0ACE3. 2 interactions.
MINTiMINT-8175118.
STRINGi511145.b0460.

Proteomic databases

PaxDbiP0ACE3.
PRIDEiP0ACE3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73562; AAC73562; b0460.
BAE76239; BAE76239; BAE76239.
GeneIDi945098.
KEGGiecj:JW0449.
eco:b0460.
PATRICi32116073. VBIEscCol129921_0478.

Organism-specific databases

EchoBASEiEB0434.
EcoGeneiEG10439. hha.

Phylogenomic databases

eggNOGiENOG4105KF5. Bacteria.
ENOG4111U15. LUCA.
HOGENOMiHOG000219358.
KOiK05839.
OMAiRRCQSID.

Enzyme and pathway databases

BioCyciEcoCyc:EG10439-MONOMER.
ECOL316407:JW0449-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ACE3.
PROiP0ACE3.

Family and domain databases

Gene3Di1.20.1280.40. 1 hit.
InterProiIPR007985. Hemolysn_expr_modulating_HHA.
[Graphical view]
PfamiPF05321. HHA. 1 hit.
[Graphical view]
SUPFAMiSSF68989. SSF68989. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHHA_ECOLI
AccessioniPrimary (citable) accession number: P0ACE3
Secondary accession number(s): P23870, P77120, Q2MBW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: September 7, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Hha and TomB may form a toxin-antitoxin (TA) module (PubMed:18545668).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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.