RegulonDB RegulonDB 10.8: Gene Form
   

zinT gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

zinT msrQ yodB OxyR Zur terminator yodBp13 yodBp13 yodBp16 yodBp16 yodBp14 yodBp14 yodBp15 yodBp15 zinTp zinTp TSS_2282 TSS_2282

Gene      
Name: zinT    Texpresso search in the literature
Synonym(s): ECK1969, G7061, b1973, yodA
Genome position(nucleotides): 2041375 --> 2042025 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
38.25
External database links:  
ASAP:
ABE-0006546
ECHOBASE:
EB3802
OU-MICROARRAY:
b1973
PortEco:
zinT
STRING:
511145.b1973
COLOMBOS: zinT


Product      
Name: metal-binding protein ZinT
Synonym(s): YodA, ZinT, cadmium-induced cadmium binding protein
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space,cytosol
Molecular weight: 24.762
Isoelectric point: 6.351
Motif(s):
 
Type Positions Sequence
24 -> 216 HGHHSHGKPLTEVEQKAANGVFDDANVQNRTLSDWDGVWQSVYPLLQSGKLDPVFQKKADADKTKTFAEIKDYYHKGYATDIEMIGIEDGIVEFHRNNETTSCKYDYDGYKILTYKSGKKGVRYLFECKDPESKAPKYIQFSDHIIAPRKSSHFHIFMGNDSQQSLLNEMENWPTYYPYQLSSEEVVEEMMSH
1 -> 23 MAIRLYKLAVALGVFIVSAPAFS
37 -> 216 EQKAANGVFDDANVQNRTLSDWDGVWQSVYPLLQSGKLDPVFQKKADADKTKTFAEIKDYYHKGYATDIEMIGIEDGIVEFHRNNETTSCKYDYDGYKILTYKSGKKGVRYLFECKDPESKAPKYIQFSDHIIAPRKSSHFHIFMGNDSQQSLLNEMENWPTYYPYQLSSEEVVEEMMSH

 

Classification:
Multifun Terms (GenProtEC)  
  5 - cell processes --> 5.5 - adaptations
Gene Ontology Terms (GO)  
cellular_component GO:0005623 - cell
GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0046872 - metal ion binding
GO:0008270 - zinc ion binding
GO:0046870 - cadmium ion binding
biological_process GO:0006882 - cellular zinc ion homeostasis
GO:0034224 - cellular response to zinc ion starvation
GO:0070301 - cellular response to hydrogen peroxide
GO:0071276 - cellular response to cadmium ion
Note(s): Note(s): ...[more].
Evidence: [AH] Author hypothesis
[APPH] Assay of protein purified to homogeneity
Reference(s): [1] David G., et al., 2002
[2] David G., et al., 2003
[3] Gabbianelli R., et al., 2011
[4] Graham AI., et al., 2009
[5] Hantke K. 2005
[6] Kannan G., et al., 2008
External database links:  
ECOCYC:
G7061-MONOMER
ECOLIWIKI:
b1973
INTERPRO:
IPR012674
INTERPRO:
IPR015304
MODBASE:
P76344
PDB:
5XM5
PDB:
5YXC
PDB:
5AQ6
PDB:
1S7D
PDB:
1OEK
PDB:
1OEJ
PDB:
1OEE
PDB:
1TXL
PFAM:
PF09223
PRIDE:
P76344
REFSEQ:
NP_416482
SMR:
P76344
UNIPROT:
P76344


Operon      
Name: zinT         
Operon arrangement:
Transcription unit        Promoter
zinT


Transcriptional Regulation      
Display Regulation             
Activated by: Fur, OxyR, SoxS
Repressed by: Zur


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_2282 2041344 forward nd [RS-EPT-CBR] [7]
  promoter yodBp15 2042176 forward Similarity to the consensus
Read more >
[ICWHO] [8]
  promoter yodBp14 2042261 forward Similarity to the consensus
Read more >
[ICWHO] [8]
  promoter yodBp16 2042294 forward Similarity to the consensus
Read more >
[ICWHO] [8]
  promoter yodBp13 2042308 forward Similarity to the consensus
Read more >
[ICWHO] [8]


Evidence    

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

 [ICWHO] Inferred computationally without human oversight



Reference(s)    

 [1] David G., Blondeau K., Renouard M., Lewit-Bentley A., 2002, Crystallization and preliminary analysis of Escherichia coli YodA., Acta Crystallogr D Biol Crystallogr 58(Pt 7):1243-5

 [2] David G., Blondeau K., Schiltz M., Penel S., Lewit-Bentley A., 2003, YodA from Escherichia coli is a metal-binding, lipocalin-like protein., J Biol Chem 278(44):43728-35

 [3] Gabbianelli R., Scotti R., Ammendola S., Petrarca P., Nicolini L., Battistoni A., 2011, Role of ZnuABC and ZinT in Escherichia coli O157:H7 zinc acquisition and interaction with epithelial cells., BMC Microbiol 11:36

 [4] Graham AI., Hunt S., Stokes SL., Bramall N., Bunch J., Cox AG., McLeod CW., Poole RK., 2009, Severe Zinc Depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins., J Biol Chem 284(27):18377-89

 [5] Hantke K., 2005, Bacterial zinc uptake and regulators., Curr Opin Microbiol 8(2):196-202

 [6] Kannan G., Wilks JC., Fitzgerald DM., Jones BD., Bondurant SS., Slonczewski JL., 2008, Rapid acid treatment of Escherichia coli: transcriptomic response and recovery., BMC Microbiol 8:37

 [7] 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.

 [8] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78


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