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Protein

Iron(3+)-hydroxamate-binding protein FhuD

Gene

fhuD

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

Functioni

Part of the ABC transporter complex FhuCDB involved in iron3+-hydroxamate import. Binds the iron3+-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron3+-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin.4 Publications

GO - Biological processi

Keywordsi

Biological processIon transport, Iron transport, Transport
LigandIron

Enzyme and pathway databases

BioCyciEcoCyc:FHUD-MONOMER
MetaCyc:FHUD-MONOMER

Protein family/group databases

TCDBi3.A.1.14.3 the atp-binding cassette (abc) superfamily

Names & Taxonomyi

Protein namesi
Recommended name:
Iron(3+)-hydroxamate-binding protein FhuDCurated
Alternative name(s):
Ferric hydroxamate uptake protein DCurated
Ferrichrome-binding periplasmic proteinCurated
Iron(III)-hydroxamate-binding protein FhuDCurated
Gene namesi
Name:fhuD
Ordered Locus Names:b0152, JW0148
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10305 fhuD

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68W → L: Decreases binding of coprogen. Does not bind aerobactin and ferrichrome. Increases resistance to albomycin. 1 Publication1

Chemistry databases

DrugBankiDB01747 Coprogen
DB02724 Delta-2-Albomycin A1
DB03436 Gallichrome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Tat-type signalAdd BLAST30
ChainiPRO_000003182431 – 296Iron(3+)-hydroxamate-binding protein FhuDAdd BLAST266

Post-translational modificationi

Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system.1 Publication

Proteomic databases

PaxDbiP07822
PRIDEiP07822

Expressioni

Inductioni

Induced 1.3-fold by hydroxyurea.1 Publication

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (FhuC), two transmembrane proteins (FhuB) and a solute-binding protein (FhuD) (Probable). FhuD interacts with FhuB (PubMed:8522527, PubMed:9426146).Curated2 Publications

Protein-protein interaction databases

BioGridi4263041, 342 interactors
IntActiP07822, 2 interactors
STRINGi316385.ECDH10B_0132

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 42Combined sources6
Helixi43 – 51Combined sources9
Beta strandi57 – 60Combined sources4
Helixi62 – 68Combined sources7
Beta strandi78 – 80Combined sources3
Beta strandi84 – 87Combined sources4
Helixi89 – 95Combined sources7
Beta strandi98 – 103Combined sources6
Beta strandi106 – 108Combined sources3
Helixi110 – 116Combined sources7
Beta strandi119 – 122Combined sources4
Beta strandi126 – 128Combined sources3
Helixi130 – 145Combined sources16
Helixi148 – 165Combined sources18
Helixi166 – 169Combined sources4
Beta strandi170 – 172Combined sources3
Beta strandi177 – 184Combined sources8
Beta strandi187 – 191Combined sources5
Helixi198 – 203Combined sources6
Beta strandi218 – 222Combined sources5
Helixi224 – 229Combined sources6
Beta strandi234 – 238Combined sources5
Helixi243 – 250Combined sources8
Helixi253 – 257Combined sources5
Helixi259 – 262Combined sources4
Beta strandi266 – 269Combined sources4
Helixi278 – 292Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFDX-ray1.90N31-296[»]
1ESZX-ray2.00A31-296[»]
1K2VX-ray1.97N31-296[»]
1K7SX-ray2.60N33-296[»]
ProteinModelPortaliP07822
SMRiP07822
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07822

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 296Fe/B12 periplasmic-bindingPROSITE-ProRule annotationAdd BLAST260

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105J76 Bacteria
COG0614 LUCA
HOGENOMiHOG000285075
InParanoidiP07822
KOiK02016
OMAiGIWMFGG
PhylomeDBiP07822

Family and domain databases

InterProiView protein in InterPro
IPR002491 ABC_transptr_periplasmic_BD
IPR008091 Ferrichrome-bd
PfamiView protein in Pfam
PF01497 Peripla_BP_2, 1 hit
PRINTSiPR01715 FERRIBNDNGPP
PROSITEiView protein in PROSITE
PS50983 FE_B12_PBP, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07822-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLPLISRR RLLTAMALSP LLWQMNTAHA AAIDPNRIVA LEWLPVELLL
60 70 80 90 100
ALGIVPYGVA DTINYRLWVS EPPLPDSVID VGLRTEPNLE LLTEMKPSFM
110 120 130 140 150
VWSAGYGPSP EMLARIAPGR GFNFSDGKQP LAMARKSLTE MADLLNLQSA
160 170 180 190 200
AETHLAQYED FIRSMKPRFV KRGARPLLLT TLIDPRHMLV FGPNSLFQEI
210 220 230 240 250
LDEYGIPNAW QGETNFWGST AVSIDRLAAY KDVDVLCFDH DNSKDMDALM
260 270 280 290
ATPLWQAMPF VRAGRFQRVP AVWFYGATLS AMHFVRVLDN AIGGKA
Length:296
Mass (Da):32,998
Last modified:November 1, 1997 - v3
Checksum:i4687A34771397D9F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48L → V in CAA29255 (PubMed:3301821).Curated1
Sequence conflicti154H → D in AAB61770 (PubMed:3301821).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05810 Genomic DNA Translation: CAA29255.1
M12486 Genomic DNA Translation: AAB61770.1
U70214 Genomic DNA Translation: AAB08582.1
U00096 Genomic DNA Translation: AAC73263.1
AP009048 Genomic DNA Translation: BAB96728.2
PIRiH64738 QRECFD
RefSeqiNP_414694.1, NC_000913.3
WP_001310529.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73263; AAC73263; b0152
BAB96728; BAB96728; BAB96728
GeneIDi947510
KEGGiecj:JW0148
eco:b0152
PATRICifig|1411691.4.peg.2128

Similar proteinsi

Entry informationi

Entry nameiFHUD_ECOLI
AccessioniPrimary (citable) accession number: P07822
Secondary accession number(s): P77711
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 161 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health