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| Accession Number: | P07822 |
| Protein Name: | FhuD aka B0152 |
| Length: | 296 |
| Molecular Weight: | 32998.00 |
| Species: | Escherichia coli [83333] |
| Number of TMSs: | 1 |
| Location1 / Topology2 / Orientation3: | Periplasm1 |
| Substrate | iron(III) hydroxamate, elaiophylin |
Cross database links:
| RefSeq: | AP_000813.1 NP_414694.1 |
|---|---|
| Entrez Gene ID: | 947510 |
| Pfam: | PF01497 |
| BioCyc: | EcoCyc:FHUD-MONOMER ECOL168927:B0152-MONOMER |
| KEGG: | ecj:JW0148 eco:b0152 |
Gene Ontology
GO:0042597
C:periplasmic space
GO:0005381
F:iron ion transmembrane transporter activity
GO:0006827
P:high-affinity iron ion transport
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References (9)[1] “fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12.” Coulton J.W.et.al. 3301821 [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.et.al. 2823072 [3] “Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region.” Fujita N.et.al. 8202364 [4] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [6] “In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence.” Rohrback M.R.et.al. 7651325 [7] “Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides.” Tullman-Ercek D.et.al. 17218314 [8] “The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.” Clarke T.E.et.al. 10742172 [9] “X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin.” Clarke T.E.et.al. 11805094
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| Structure: | |
External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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1: MSGLPLISRR RLLTAMALSP LLWQMNTAHA AAIDPNRIVA LEWLPVELLL ALGIVPYGVA 61: DTINYRLWVS EPPLPDSVID VGLRTEPNLE LLTEMKPSFM VWSAGYGPSP EMLARIAPGR 121: GFNFSDGKQP LAMARKSLTE MADLLNLQSA AETHLAQYED FIRSMKPRFV KRGARPLLLT 181: TLIDPRHMLV FGPNSLFQEI LDEYGIPNAW QGETNFWGST AVSIDRLAAY KDVDVLCFDH 241: DNSKDMDALM ATPLWQAMPF VRAGRFQRVP AVWFYGATLS AMHFVRVLDN AIGGKA