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Protein

Iron(3+)-hydroxamate-binding protein FhuD

Gene

fhuD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron

Enzyme and pathway databases

BioCyciEcoCyc:FHUD-MONOMER.
ECOL316407:JW0148-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

Complete GO annotation...

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

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. 340 interactors.
IntActiP07822. 2 interactors.
STRINGi511145.b0152.

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

Contains 1 Fe/B12 periplasmic-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105J76. Bacteria.
COG0614. LUCA.
HOGENOMiHOG000285075.
InParanoidiP07822.
KOiK02016.
OMAiVLCFDHG.
PhylomeDBiP07822.

Family and domain databases

InterProiIPR002491. ABC_transptr_periplasmic_BD.
IPR008091. Ferrichrome-bd.
[Graphical view]
PfamiPF01497. Peripla_BP_2. 1 hit.
[Graphical view]
PRINTSiPR01715. FERRIBNDNGPP.
PROSITEiPS50983. FE_B12_PBP. 1 hit.
[Graphical view]

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.
PATRICi32115413. VBIEscCol129921_0158.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi4263041. 340 interactors.
IntActiP07822. 2 interactors.
STRINGi511145.b0152.

Protein family/group databases

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

Proteomic databases

PaxDbiP07822.
PRIDEiP07822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73263; AAC73263; b0152.
BAB96728; BAB96728; BAB96728.
GeneIDi947510.
KEGGiecj:JW0148.
eco:b0152.
PATRICi32115413. VBIEscCol129921_0158.

Organism-specific databases

EchoBASEiEB0301.
EcoGeneiEG10305. fhuD.

Phylogenomic databases

eggNOGiENOG4105J76. Bacteria.
COG0614. LUCA.
HOGENOMiHOG000285075.
InParanoidiP07822.
KOiK02016.
OMAiVLCFDHG.
PhylomeDBiP07822.

Enzyme and pathway databases

BioCyciEcoCyc:FHUD-MONOMER.
ECOL316407:JW0148-MONOMER.
MetaCyc:FHUD-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07822.
PROiP07822.

Family and domain databases

InterProiIPR002491. ABC_transptr_periplasmic_BD.
IPR008091. Ferrichrome-bd.
[Graphical view]
PfamiPF01497. Peripla_BP_2. 1 hit.
[Graphical view]
PRINTSiPR01715. FERRIBNDNGPP.
PROSITEiPS50983. FE_B12_PBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFHUD_ECOLI
AccessioniPrimary (citable) accession number: P07822
Secondary accession number(s): P77711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 154 of the entry and version 3 of the sequence. [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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.