Catecholate siderophore receptor Fiu

Details

Name
Catecholate siderophore receptor Fiu
Synonyms
  • Ferric iron uptake protein
  • TonB-dependent receptor Fiu
  • ybiL
Gene Name
fiu
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0052197|Catecholate siderophore receptor Fiu
MENNRNFPARQFHSLTFFAGLCIGITPVAQALAAEGQTNADDTLVVEASTPSLYAPQQSA
DPKFSRPVADTTRTMTVISEQVIKDQGATNLTDALKNVPGVGAFFAGENGNSTTGDAIYM
RGADTSNSIYIDGIRDIGSVSRDTFNTEQVEVIKGPSGTDYGRSAPTGSINMISKQPRND
SGIDASASIGSAWFRRGTLDVNQVIGDTTAVRLNVMGEKTHDAGRDKVKNERYGVAPSVA
FGLGTANRLYLNYLHVTQHNTPDGGIPTIGLPGYSAPSAGTAALNHSGKVDTHNFYGTDS
DYDDSTTDTATMRFEHDINDNTTIRNTTRWSRVKQDYLMTAIMGGASNITQPTSDVNSWT
WSRTANTKDVSNKILTNQTNLTSTFYTGSIGHDVSTGVEFTRETQTNYGVNPVTLPAVNI
YHPDSSIHPGGLTRNGANANGQTDTFAIYAFDTLQITRDFELNGGIRLDNYHTEYDSATA
CGGSGRGAITCPTGVAKGSPVTTVDTAKSGNLMNWKAGALYHLTENGNVYINYAVSQQPP
GGNNFALAQSGSGNSANRTDFKPQKANTSEIGTKWQVLDKRLLLTAALFRTDIENEVEQN
DDGTYSQYGKKRVEGYEISVAGNITPAWQVIGGYTQQKATIKNGKDVAQDGSSSLPYTPE
HAFTLWSQYQATDDISVGAGARYIGSMHKGSDGAVGTPAFTEGYWVADAKLGYRVNRNLD
FQLNVYNLFDTDYVASINKSGYRYHPGEPRTFLLTANMHF
Number of residues
760
Molecular Weight
81959.515
Theoretical pI
Not Available
GO Classification
Functions
siderophore uptake transmembrane transporter activity / signaling receptor activity
Processes
iron ion homeostasis / microcin transport / siderophore transport
Components
cell outer membrane / integral component of membrane
General Function
Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.
Specific Function
Siderophore uptake transmembrane transporter activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell outer membrane
Gene sequence
>lcl|BSEQ0052198|Catecholate siderophore receptor Fiu (fiu)
ATGGAAAACAATCGCAATTTCCCTGCCAGACAATTTCATTCGCTCACGTTCTTTGCCGGT
CTTTGTATTGGCATCACGCCTGTGGCTCAGGCACTCGCCGCCGAAGGGCAAACTAACGCG
GATGACACGCTGGTTGTCGAAGCATCAACGCCTTCGCTTTATGCGCCACAACAATCTGCC
GATCCGAAATTCTCGCGTCCGGTAGCGGATACTACCCGCACGATGACGGTAATTTCTGAA
CAAGTGATTAAAGATCAGGGCGCAACCAACCTTACCGACGCGCTCAAAAACGTCCCCGGC
GTGGGTGCGTTTTTTGCGGGTGAGAACGGTAACTCCACCACTGGCGACGCCATTTATATG
CGTGGTGCCGATACCTCTAACAGTATTTATATTGATGGCATTCGCGATATCGGCAGCGTC
TCGCGCGACACCTTCAATACCGAGCAGGTCGAAGTGATTAAAGGGCCGTCCGGCACCGAC
TACGGGCGCAGCGCACCGACAGGCTCGATCAATATGATCAGCAAGCAGCCGCGCAATGAT
TCCGGCATTGACGCCTCCGCCAGTATTGGCAGCGCCTGGTTCCGCCGCGGCACGCTGGAC
GTCAATCAGGTCATTGGTGATACCACCGCGGTGCGCCTGAATGTAATGGGCGAAAAAACG
CACGATGCCGGACGCGACAAAGTCAAAAATGAGCGTTACGGCGTCGCCCCTTCTGTCGCT
TTTGGCCTTGGTACAGCGAATCGTTTGTATCTTAATTATCTGCATGTCACCCAGCACAAC
ACGCCAGACGGCGGCATTCCGACCATCGGTTTGCCGGGCTATTCTGCCCCATCTGCGGGA
ACGGCGGCCCTGAATCATTCCGGAAAAGTTGATACTCATAACTTTTACGGCACGGATTCC
GATTACGACGATTCGACCACCGACACCGCCACCATGCGTTTTGAGCACGACATCAACGAT
AACACCACCATTCGCAATACTACCCGTTGGTCGCGCGTAAAGCAGGATTACCTGATGACG
GCGATTATGGGCGGGGCGTCGAATATTACTCAGCCCACCAGCGATGTGAATAGCTGGACC
TGGTCACGCACGGCGAATACCAAAGATGTGAGTAATAAAATTCTCACCAACCAGACCAAC
CTGACCTCGACGTTCTATACCGGTTCTATCGGTCATGATGTCAGTACCGGCGTGGAATTT
ACCCGTGAAACGCAGACTAACTACGGCGTTAATCCGGTGACGTTACCCGCGGTAAATATT
TATCATCCTGACAGCAGCATTCATCCCGGCGGCCTGACGCGCAACGGCGCAAACGCCAAT
GGTCAGACGGATACCTTCGCAATTTACGCCTTTGATACGCTGCAAATCACCCGTGATTTT
GAGCTGAACGGCGGGATCCGTCTGGATAATTATCATACTGAATATGACAGTGCCACCGCC
TGCGGCGGCAGCGGACGCGGTGCCATCACCTGCCCAACTGGTGTGGCAAAAGGTTCTCCG
GTCACCACCGTCGACACCGCCAAGTCGGGCAATCTGATGAACTGGAAAGCCGGGGCGCTG
TATCACCTGACGGAAAACGGCAATGTCTATATTAACTATGCCGTTTCCCAGCAGCCTCCG
GGCGGCAACAACTTCGCCCTTGCGCAGTCTGGCAGCGGTAACAGTGCCAACCGCACCGAT
TTTAAACCGCAAAAAGCCAACACCAGCGAGATTGGCACCAAATGGCAGGTTCTGGATAAA
CGTCTGTTGCTCACCGCCGCGCTGTTCCGCACTGATATCGAAAATGAAGTTGAGCAAAAT
GATGACGGAACTTACTCGCAATACGGTAAGAAACGCGTCGAAGGCTATGAGATATCCGTG
GCCGGGAATATCACTCCCGCGTGGCAGGTGATTGGCGGCTATACCCAGCAAAAAGCAACC
ATCAAAAACGGCAAAGATGTTGCCCAGGATGGTTCCTCATCGCTGCCGTATACCCCGGAG
CACGCCTTCACCTTATGGAGCCAATATCAGGCAACCGACGATATCTCTGTTGGCGCGGGC
GCACGCTATATCGGCAGTATGCATAAAGGTTCAGACGGCGCGGTGGGAACGCCAGCGTTT
ACCGAAGGTTACTGGGTCGCCGATGCCAAACTGGGGTATCGAGTTAATCGCAATCTCGAC
TTCCAGCTAAACGTTTACAACCTGTTTGATACCGATTACGTCGCCTCAATCAACAAGAGC
GGCTACCGTTATCACCCGGGCGAGCCAAGAACCTTCTTGCTCACAGCCAATATGCATTTC
TGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP75780
UniProtKB Entry NameFIU_ECOLI
General References
  1. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Curtis NA, Eisenstadt RL, East SJ, Cornford RJ, Walker LA, White AJ: Iron-regulated outer membrane proteins of Escherichia coli K-12 and mechanism of action of catechol-substituted cephalosporins. Antimicrob Agents Chemother. 1988 Dec;32(12):1879-86. doi: 10.1128/aac.32.12.1879. [Article]
  5. Hantke K: Dihydroxybenzoylserine--a siderophore for E. coli. FEMS Microbiol Lett. 1990 Jan 15;55(1-2):5-8. doi: 10.1016/0378-1097(90)90158-m. [Article]
  6. Nikaido H, Rosenberg EY: Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups. J Bacteriol. 1990 Mar;172(3):1361-7. doi: 10.1128/jb.172.3.1361-1367.1990. [Article]
  7. Niehaus F, Hantke K, Unden G: Iron content and FNR-dependent gene regulation in Escherichia coli. FEMS Microbiol Lett. 1991 Dec 1;68(3):319-23. doi: 10.1016/0378-1097(91)90376-l. [Article]
  8. Newman DL, Shapiro JA: Differential fiu-lacZ fusion regulation linked to Escherichia coli colony development. Mol Microbiol. 1999 Jul;33(1):18-32. doi: 10.1046/j.1365-2958.1999.01423.x. [Article]
  9. Molloy MP, Herbert BR, Slade MB, Rabilloud T, Nouwens AS, Williams KL, Gooley AA: Proteomic analysis of the Escherichia coli outer membrane. Eur J Biochem. 2000 May;267(10):2871-81. doi: 10.1046/j.1432-1327.2000.01296.x. [Article]
  10. Patzer SI, Baquero MR, Bravo D, Moreno F, Hantke K: The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN. Microbiology. 2003 Sep;149(Pt 9):2557-70. doi: 10.1099/mic.0.26396-0. [Article]
  11. Destoumieux-Garzon D, Peduzzi J, Thomas X, Djediat C, Rebuffat S: Parasitism of iron-siderophore receptors of Escherichia coli by the siderophore-peptide microcin E492m and its unmodified counterpart. Biometals. 2006 Apr;19(2):181-91. doi: 10.1007/s10534-005-4452-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB14879Cefiderocolapproved, investigationalnosubstrateDetails