RegulonDB RegulonDB 11.1: Gene Form
   

fhuD gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fhuA fhuB hemL fhuD fhuC terminator TSS_291 TSS_291 TSS_290 TSS_290 TSS_289 TSS_289

Gene      
Name: fhuD    Texpresso search in the literature
Synonym(s): ECK0151, EG10305, b0152
Genome position(nucleotides): 170575 --> 171465
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 54.66
External database links:  
ASAP:
 ABE-0000524
CGSC:
 11184
ECHOBASE:
 EB0301
ECOLIHUB:
 fhuD
OU-MICROARRAY:
 b0152
STRING:
 511145.b0152
COLOMBOS: fhuD


Product      
Name: iron(III) hydroxamate ABC transporter periplasmic binding protein
Synonym(s): FhuD
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane,periplasmic space
Molecular weight: 32.998
Isoelectric point: 6.364
Motif(s):
 
Type Positions Sequence Comment
1 -> 30 MSGLPLISRRRLLTAMALSPLLWQMNTAHA UniProt: Tat-type signal.
27 -> 141 TAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEM
31 -> 296 AAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGKA UniProt: Iron(3+)-hydroxamate-binding protein FhuD.
37 -> 296 RIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGKA UniProt: Fe/B12 periplasmic-binding.
38 -> 270 IVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMKPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVP

 
Classification:
Multifun Terms (GenProtEC)  
  5 - cell processes --> 5.5 - adaptations --> 5.5.7 - Fe aquisition
  4 - transport --> 4.3 - Primary Active Transporters --> 4.3.A - Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters --> 4.3.A.1 - The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases --> 4.3.A.1.p - ABC superfamily, periplasmic binding component
Gene Ontology Terms (GO)  
cellular_component GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
molecular_function GO:0005515 - protein binding
biological_process GO:0098711 - iron ion import across plasma membrane
GO:0006811 - ion transport
GO:0055072 - iron ion homeostasis
GO:0015687 - ferric-hydroxamate import into cell
Note(s): Note(s): ...[more].
Reference(s): [1] Chu BC., et al., 2011
[2] Koster W. 1991
[3] Koster W., et al., 1990
[4] Krewulak KD., et al., 2005
[5] Rohrback MR., et al., 1995
External database links:  
ALPHAFOLD:
 P07822
ECOCYC:
 FHUD-MONOMER
ECOLIWIKI:
 b0152
INTERPRO:
 IPR002491
MODBASE:
 P07822
PDB:
 1K2V
PDB:
 1ESZ
PDB:
 1EFD
PDB:
 1K7S
PFAM:
 PF01497
PRIDE:
 P07822
PRODB:
 PRO_000022612
PROSITE:
 PS50983
REFSEQ:
 NP_414694
SMR:
 P07822
UNIPROT:
 P07822


Operon      
Name: fhuACDB         
Operon arrangement:
Transcription unit        Promoter
fhuACDB


Transcriptional Regulation      
Display Regulation             
Repressed by: Fur


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_289 169733 forward nd [RS-EPT-CBR] [6]
  promoter TSS_290 173420 forward nd [RS-EPT-CBR] [6]
  promoter TSS_291 173769 reverse nd [RS-EPT-CBR] [6]


Evidence    

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


Reference(s)    

 [1] Chu BC., Vogel HJ., 2011, A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport., Biol Chem 392(1-2):39-52

 [2] Koster W., 1991, Iron(III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli., Biol Met 4(1):23-32

 [3] Koster W., Braun V., 1990, Iron (III) hydroxamate transport into Escherichia coli. Substrate binding to the periplasmic FhuD protein., J Biol Chem 265(35):21407-10

 [4] Krewulak KD., Shepherd CM., Vogel HJ., 2005, Molecular dynamics simulations of the periplasmic ferric-hydroxamate binding protein FhuD., Biometals 18(4):375-86

 [5] Rohrback MR., Paul S., Koster W., 1995, In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence., Mol Gen Genet 248(1):33-42

 [6] 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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