Iron(3+)-hydroxamate-binding protein FhuD precursor

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P07822 (FHUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Iron(3+)-hydroxamate-binding protein FhuD

Alternative name(s):
Ferric hydroxamate uptake protein D
Ferrichrome-binding periplasmic protein
Iron(III)-hydroxamate-binding protein FhuD

Gene names

Name:	fhuD
Ordered Locus Names:	b0152, JW0148

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	The complex is composed of an ATP-binding protein (FhuC), two transmembrane proteins (FhuB) and a solute-binding protein (FhuD).
Subcellular location	Periplasm.
Post-translational modification	Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Can also be exported by the Sec system.
Sequence similarities	Belongs to the bacterial solute-binding protein 8 family. Contains 1 Fe/B12 periplasmic-binding domain.

Ontologies

Keywords
Biological process	Ion transport Iron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Iron
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ion transport Inferred from electronic annotation. Source: UniProtKB-KW iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

Tat-type signal

Chain

31 – 296

266

Iron(3+)-hydroxamate-binding protein FhuD

PRO_0000031824

Regions

Domain

37 – 296

260

Fe/B12 periplasmic-binding

Experimental info

Sequence conflict

L → V in CAA29255. Ref.1

Sequence conflict

154

H → D Ref.2

Sequence conflict

154

H → D Ref.3

Secondary structure

296

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07822 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 4687A34771397D9F
Show »

FASTA

296

32,998

        10         20         30         40         50         60 
MSGLPLISRR RLLTAMALSP LLWQMNTAHA AAIDPNRIVA LEWLPVELLL ALGIVPYGVA 

        70         80         90        100        110        120 
DTINYRLWVS EPPLPDSVID VGLRTEPNLE LLTEMKPSFM VWSAGYGPSP EMLARIAPGR 

       130        140        150        160        170        180 
GFNFSDGKQP LAMARKSLTE MADLLNLQSA AETHLAQYED FIRSMKPRFV KRGARPLLLT 

       190        200        210        220        230        240 
TLIDPRHMLV FGPNSLFQEI LDEYGIPNAW QGETNFWGST AVSIDRLAAY KDVDVLCFDH 

       250        260        270        280        290 
DNSKDMDALM ATPLWQAMPF VRAGRFQRVP AVWFYGATLS AMHFVRVLDN AIGGKA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12." Coulton J.W., Mason P., Allatt D.D. J. Bacteriol. 169:3844-3849(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins." Burkhardt R., Braun V. Mol. Gen. Genet. 209:49-55(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 154. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence." Rohrback M.R., Paul S., Koster W. Mol. Gen. Genet. 248:33-42(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-39.
[8]	"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G. J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract] Cited for: EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
[9]	"The structure of the ferric siderophore binding protein FhuD complexed with gallichrome." Clarke T.E., Ku S.-Y., Dougan D.R., Vogel H.J., Tari L.W. Nat. Struct. Biol. 7:287-291(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-296 IN COMPLEX WITH GALLICHROME.
[10]	"X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin." Clarke T.E., Braun V., Winkelmann G., Tari L.W., Vogel H.J. J. Biol. Chem. 277:13966-13972(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-296 IN COMPLEX WITH COPROGEN; DESFERRIOXAMINE AND ALBOMYCIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

QRECFD. H64738.

RefSeq

NP_414694.1. NC_000913.2.
YP_488455.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EFD	X-ray	1.90	N	33-296	[»]
1ESZ	X-ray	2.00	A	31-296	[»]
1K2V	X-ray	1.97	N	31-296	[»]
1K7S	X-ray	2.60	N	33-296	[»]

ProteinModelPortal

P07822.

SMR

P07822. Positions 32-293.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07822. 2 interactions.

STRING

511145.b0152.

Protein family/group databases

TCDB

3.A.1.14.3. ATP-binding cassette (ABC) superfamily.

Proteomic databases

PRIDE

P07822.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73263; AAC73263; b0152.
BAB96728; BAB96728; BAB96728.

GeneID

12934047.
947510.

KEGG

ecj:Y75_p0149.
eco:b0152.

PATRIC

32115413. VBIEscCol129921_0158.

Organism-specific databases

EchoBASE

EB0301.

EcoGene

EG10305. fhuD.

Phylogenomic databases

eggNOG

COG0614.

HOGENOM

HOG000285075.

K02016.

OMA

YGVADIP.

ProtClustDB

PRK10576.

Enzyme and pathway databases

BioCyc

EcoCyc:FHUD-MONOMER.
ECOL316407:JW0148-MONOMER.

Gene expression databases

Genevestigator

P07822.

Family and domain databases

InterPro

IPR002491. ABC_transptr_periplasmic_BD.
IPR008091. Ferrichrome-bd.
[Graphical view]

Pfam

PF01497. Peripla_BP_2. 1 hit.
[Graphical view]

PRINTS

PR01715. FERRIBNDNGPP.

PROSITE

PS50983. FE_B12_PBP. 1 hit.
PS51318. TAT. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07822.

Entry information

Entry name

FHUD_ECOLI

Accession

Primary (citable) accession number: P07822
Secondary accession number(s): P77711

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents