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Protein

Hemolysin expression-modulating protein Hha

Gene

hha

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei25Interacts with H-NS1
Sitei48Interacts with H-NS1

GO - Biological processi

  • regulation of gene expression Source: EcoCyc
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionRepressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG10439-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10439 hha

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

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)DescriptionActionsGraphical viewLength
Mutagenesisi10D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi16R → C: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi22D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi25E → Q: Affects H-NS binding ability. Decrease in the ability to repress the expression of the hly operon. 1 Publication1
Mutagenesisi29E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi34E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi37D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi39E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi44 – 72Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd BLAST29
Mutagenesisi48D → E or R: Abolishes the interaction with H-NS. 1 Publication1
Mutagenesisi48D → N: Abolishes the interaction with H-NS. Loss of the ability to repress the expression of the hly operon. 1 Publication1
Mutagenesisi50R → H: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi58 – 72Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd BLAST15
Mutagenesisi61D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi64P → L or S: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi72R → RHHHHHH: Derepression of the hly operon, impaired H-NS binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017271 – 72Hemolysin expression-modulating protein HhaAdd BLAST72

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 interactors
ComplexPortaliCPX-1979 H-NS-Hha complex
DIPiDIP-9897N
IntActiP0ACE3, 2 interactors
MINTiP0ACE3
STRINGi316385.ECDH10B_0416

Structurei

Secondary structure

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 16Combined sources9
Helixi21 – 34Combined sources14
Helixi37 – 55Combined sources19
Beta strandi56 – 58Combined sources3
Helixi65 – 70Combined sources6

3D structure databases

ProteinModelPortaliP0ACE3
SMRiP0ACE3
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
InterProiView protein in InterPro
IPR007985 Hemolysn_expr_modulating_HHA
IPR036666 HHA_sf
PfamiView protein in Pfam
PF05321 HHA, 1 hit
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
PATRICifig|511145.12.peg.478

Entry informationi

Entry nameiHHA_ECOLI
AccessioniPrimary (citable) accession number: P0ACE3
Secondary accession number(s): P23870, P77120, Q2MBW7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 20, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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