RegulonDB RegulonDB 11.0: Gene Form
   

hipA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

yneO hipA ydeT hipB yneL IHF HipB HipAB HipB HipAB HipB HipAB HipB HipAB hipBp hipBp TSS_1836 TSS_1836

Gene      
Name: hipA    Texpresso search in the literature
Synonym(s): ECK1500, EG10443, b1507
Genome position(nucleotides): 1590854 <-- 1592176
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
48.07
External database links:  
ASAP:
ABE-0005022
ECHOBASE:
EB0438
ECOLIHUB:
hipA
OU-MICROARRAY:
b1507
STRING:
511145.b1507
COLOMBOS: hipA


Product      
Name: serine/threonine-protein kinase toxin HipA
Synonym(s): HipA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 49.276
Isoelectric point: 8.419
Motif(s):
 
Type Positions Sequence Comment
7 -> 103 WMNNQRVGELTKLANGAHTFKYAPEWLASRYARPLSLSLPLQRGNITSDAVFNFFDNLLPDSPIVRDRIVKRYHAKSRQPFDLLSEIGRDSVGAVTL
22 -> 22 G UniProt: Loss of toxicity, does not confer high persistence. Single mutation has decreased affinity for HipB-operator. Loss of toxicity, high levels of persister cells and cold sensitivity, decreased affinity for HipB; in hipA7; when associated with A-291..
40 -> 40 P UniProt: In Ref. 1; AAA56878..
86 -> 86 P UniProt: High levels of persister cells formed which survive better than wild-type in ampicillin or ciprofloxacin, decreased affinity for HipB-operator..
88 -> 88 D UniProt: Loss of toxicity, still confers high levels of persister cells. Decreased affinity for HipB-operator..

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
  2 - information transfer --> 2.3 - protein related --> 2.3.3 - posttranslational modification
  3 - regulation --> 3.1 - type of regulation --> 3.1.3 - posttranscriptional --> 3.1.3.2 - covalent modification, demodification, maturation
Gene Ontology Terms (GO)  
cellular_component GO:0110001 - toxin-antitoxin complex
GO:0005829 - cytosol
GO:0032993 - protein-DNA complex
molecular_function GO:0106310 - protein serine kinase activity
GO:0004712 - protein serine/threonine/tyrosine kinase activity
GO:0003677 - DNA binding
GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0016301 - kinase activity
GO:0004674 - protein serine/threonine kinase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0000287 - magnesium ion binding
GO:0043565 - sequence-specific DNA binding
GO:0000976 - transcription cis-regulatory region binding
GO:0001217 - DNA-binding transcription repressor activity
biological_process GO:0006355 - regulation of transcription, DNA-templated
GO:0045892 - negative regulation of transcription, DNA-templated
GO:0016310 - phosphorylation
GO:0046677 - response to antibiotic
GO:0040008 - regulation of growth
GO:0022611 - dormancy process
GO:0044010 - single-species biofilm formation
GO:0043086 - negative regulation of catalytic activity
GO:0036289 - peptidyl-serine autophosphorylation
Note(s): Note(s): ...[more].
Reference(s): [1] Bruel N., et al., 2012
[2] Kelsey R. 2015
[3] Keren I., et al., 2012
[4] Lewis K. 2012
[5] Li C., et al., 2013
[6] Liu S., et al., 2017
[7] Riber L., et al., 2018
[8] Wu N., et al., 2015
External database links:  
ALPHAFOLD:
P23874
DIP:
DIP-9898N
ECOCYC:
EG10443-MONOMER
ECOLIWIKI:
b1507
INTERPRO:
IPR012893
INTERPRO:
IPR017508
PDB:
2WIU
PDB:
3DNT
PDB:
5K98
PDB:
4YG7
PDB:
3TPV
PDB:
3TPT
PDB:
3TPE
PDB:
3TPD
PDB:
3DNU
PDB:
3DNV
PDB:
3FBR
PDB:
3HZI
PDB:
3TPB
PFAM:
PF07804
PFAM:
PF13657
PRIDE:
P23874
PRODB:
PRO_000022889
REFSEQ:
NP_416024
SMR:
P23874
UNIPROT:
P23874


Operon      
Name: hipBA         
Operon arrangement:
Transcription unit        Promoter
hipBA


Transcriptional Regulation      
Display Regulation             
Activated by: IHF
Repressed by: HipAB, HipB


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_1836 1592159 reverse nd [RS-EPT-CBR] [9]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Bruel N., Castanie-Cornet MP., Cirinesi AM., Koningstein G., Georgopoulos C., Luirink J., Genevaux P., 2012, Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones., J Biol Chem 287(53):44435-46

 [2] Kelsey R., 2015, Infection: HipA and multidrug tolerance in urinary tract infection., Nat Rev Urol 12(9):474

 [3] Keren I., Mulcahy LR., Lewis K., 2012, Persister eradication: lessons from the world of natural products., Methods Enzymol 517:387-406

 [4] Lewis K., 2012, Persister cells: molecular mechanisms related to antibiotic tolerance., Handb Exp Pharmacol (211):121-33

 [5] Li C., Wang Y., Chen G., 2013, Interaction investigations of HipA binding to HipB dimer and HipB dimer + DNA complex: a molecular dynamics simulation study., J Mol Recognit 26(11):556-67

 [6] Liu S., Wu N., Zhang S., Yuan Y., Zhang W., Zhang Y., 2017, Variable Persister Gene Interactions with (p)ppGpp for Persister Formation in Escherichia coli., Front Microbiol 8:1795

 [7] Riber L., Koch BM., Kruse LR., Germain E., Lobner-Olesen A., 2018, HipA-Mediated Phosphorylation of SeqA Does not Affect Replication Initiation in Escherichia coli., Front Microbiol 9:2637

 [8] Wu N., He L., Cui P., Wang W., Yuan Y., Liu S., Xu T., Zhang S., Wu J., Zhang W., Zhang Y., 2015, Ranking of persister genes in the same Escherichia coli genetic background demonstrates varying importance of individual persister genes in tolerance to different antibiotics., Front Microbiol 6:1003

 [9] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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