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Accession Number: | P06971 |
Protein Name: | FhuA aka TONA aka B0150 |
Length: | 747 |
Molecular Weight: | 82182.00 |
Species: | Escherichia coli [83333] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: | Cell outer membrane1 / Multi-pass membrane protein2 |
Substrate | ferrichrome, rifamycin SV, elaiophylin |
Cross database links:
DIP: | DIP-9602N |
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RefSeq: | AP_000811.1 NP_414692.1 |
Entrez Gene ID: | 944856 |
Pfam: | PF07715 PF00593 |
BioCyc: | EcoCyc:EG10302-MONOMER ECOL168927:B0150-MONOMER |
KEGG: | ecj:JW0146 eco:b0150 |
Gene Ontology
GO:0009279
C:cell outer membrane
GO:0016021
C:integral to membrane
GO:0005886
C:plasma membrane
GO:0048037
F:cofactor binding
GO:0005506
F:iron ion binding
GO:0004872
F:receptor activity
GO:0015343
F:siderophore-iron transmembrane transporter ...
GO:0015643
F:toxin binding
GO:0046790
F:virion binding
GO:0009597
P:detection of virus
GO:0046718
P:entry of virus into host cell
GO:0006826
P:iron ion transport
GO:0015891
P:siderophore transport
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References (10)[1] “Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12.” Coulton J.W.et.al. 3079747 [2] “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 [3] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [5] “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 [6] “Energy-coupled transport through the outer membrane of Escherichia coli small deletions in the gating loop convert the FhuA transport protein into a diffusion channel.” Braun V.et.al. 7515827 [7] “FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.” Bonhivers M.et.al. 8617231 [8] “Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide.” Ferguson A.D.et.al. 9856937 [9] “Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes.” Locher K.P.et.al. 9865695 [10] “Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA.” Ferguson A.D.et.al. 10850805
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Structure: | |
[...more] |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP QESAWGPAAT 61: IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK EALSYTPGVS VGTRGASNTY 121: DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG 181: LLNMVSKRPT TEPLKEVQFK AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG 241: SEEQRYAIAP AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN 301: EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV CSDPANAYSK 361: QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT GDIDHTLLTG VDFMRMRNDI 421: NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV 481: TLGGRYDWAD QESLNRVAGT TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG 541: KDGNIFAPSK GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA 601: RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW ADYTFFDGPL 661: SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA RVGMAGSNVA LHVNNLFDRE 721: YVASCFNTYG CFWGAERQVV ATATFRF