P06971 · FHUA_ECOLI
- ProteinFerrichrome outer membrane transporter/phage receptor
- GenefhuA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids747 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane (PubMed:1089064, PubMed:2066336).
In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1 (PubMed:1089064, PubMed:2066336, PubMed:353030, PubMed:8617231).
The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system (PubMed:12427941, PubMed:353030, PubMed:9353297).
In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1 (PubMed:1089064, PubMed:2066336, PubMed:353030, PubMed:8617231).
The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system (PubMed:12427941, PubMed:353030, PubMed:9353297).
Activity regulation
Binding of ferrichrome or colicin M enhances the interaction between FhuA and TonB (PubMed:9353297).
TonB activates FhuA through interaction with the beta-barrel (PubMed:12427941).
TonB activates FhuA through interaction with the beta-barrel (PubMed:12427941).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 114 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 133 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 148-149 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: FY | ||||||
Binding site | 277-279 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: YGW | ||||||
Binding site | 346-348 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: YGY | ||||||
Binding site | 424 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Site | 566 | Interaction with phage T5 RBP-pb5 | ||||
Sequence: P | ||||||
Binding site | 735 | ferrichrome (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Cellular Component | membrane | |
Cellular Component | transmembrane transporter complex | |
Molecular Function | iron ion binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | siderophore uptake transmembrane transporter activity | |
Molecular Function | signaling receptor activity | |
Molecular Function | toxic substance binding | |
Molecular Function | virion binding | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | siderophore transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFerrichrome outer membrane transporter/phage receptor
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP06971
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 34-192 | Periplasmic | ||||
Sequence: AVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTE | ||||||
Transmembrane | 193-201 | Beta stranded | ||||
Sequence: PLKEVQFKA | ||||||
Topological domain | 202-206 | Extracellular | ||||
Sequence: GTDSL | ||||||
Transmembrane | 207-215 | Beta stranded | ||||
Sequence: FQTGFDFSD | ||||||
Topological domain | 216-222 | Periplasmic | ||||
Sequence: SLDDDGV | ||||||
Transmembrane | 223-231 | Beta stranded | ||||
Sequence: YSYRLTGLA | ||||||
Topological domain | 232-245 | Extracellular | ||||
Sequence: RSANAQQKGSEEQR | ||||||
Transmembrane | 246-255 | Beta stranded | ||||
Sequence: YAIAPAFTWR | ||||||
Topological domain | 256-259 | Periplasmic | ||||
Sequence: PDDK | ||||||
Transmembrane | 260-268 | Beta stranded | ||||
Sequence: TNFTFLSYF | ||||||
Topological domain | 269-312 | Extracellular | ||||
Sequence: QNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNE | ||||||
Transmembrane | 313-321 | Beta stranded | ||||
Sequence: KMVGYSFDH | ||||||
Topological domain | 322-326 | Periplasmic | ||||
Sequence: EFNDT | ||||||
Transmembrane | 327-335 | Beta stranded | ||||
Sequence: FTVRQNLRF | ||||||
Topological domain | 336-387 | Extracellular | ||||
Sequence: AENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQN | ||||||
Transmembrane | 388-396 | Beta stranded | ||||
Sequence: FSVDTQLQS | ||||||
Topological domain | 397-404 | Periplasmic | ||||
Sequence: KFATGDID | ||||||
Transmembrane | 405-413 | Beta stranded | ||||
Sequence: HTLLTGVDF | ||||||
Topological domain | 414-464 | Extracellular | ||||
Sequence: MRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQ | ||||||
Transmembrane | 465-473 | Beta stranded | ||||
Sequence: TGVYVQDQA | ||||||
Topological domain | 474-477 | Periplasmic | ||||
Sequence: QWDK | ||||||
Transmembrane | 478-486 | Beta stranded | ||||
Sequence: VLVTLGGRY | ||||||
Topological domain | 487-508 | Extracellular | ||||
Sequence: DWADQESLNRVAGTTDKRDDKQ | ||||||
Transmembrane | 509-517 | Beta stranded | ||||
Sequence: FTWRGGVNY | ||||||
Topological domain | 518-522 | Periplasmic | ||||
Sequence: LFDNG | ||||||
Transmembrane | 523-531 | Beta stranded | ||||
Sequence: VTPYFSYSE | ||||||
Topological domain | 532-551 | Extracellular | ||||
Sequence: SFEPSSQVGKDGNIFAPSKG | ||||||
Transmembrane | 552-560 | Beta stranded | ||||
Sequence: KQYEVGVKY | ||||||
Topological domain | 561-565 | Periplasmic | ||||
Sequence: VPEDR | ||||||
Transmembrane | 566-574 | Beta stranded | ||||
Sequence: PIVVTGAVY | ||||||
Topological domain | 575-601 | Extracellular | ||||
Sequence: NLTKTNNLMADPEGSFFSVEGGEIRAR | ||||||
Transmembrane | 602-610 | Beta stranded | ||||
Sequence: GVEIEAKAA | ||||||
Topological domain | 611-613 | Periplasmic | ||||
Sequence: LSA | ||||||
Transmembrane | 614-622 | Beta stranded | ||||
Sequence: SVNVVGSYT | ||||||
Topological domain | 623-645 | Extracellular | ||||
Sequence: YTDAEYTTDTTYKGNTPAQVPKH | ||||||
Transmembrane | 646-654 | Beta stranded | ||||
Sequence: MASLWADYT | ||||||
Topological domain | 655-661 | Periplasmic | ||||
Sequence: FFDGPLS | ||||||
Transmembrane | 662-670 | Beta stranded | ||||
Sequence: GLTLGTGGR | ||||||
Topological domain | 671-689 | Extracellular | ||||
Sequence: YTGSSYGDPANSFKVGSYT | ||||||
Transmembrane | 690-698 | Beta stranded | ||||
Sequence: VVDALVRYD | ||||||
Topological domain | 699-705 | Periplasmic | ||||
Sequence: LARVGMA | ||||||
Transmembrane | 706-714 | Beta stranded | ||||
Sequence: GSNVALHVN | ||||||
Topological domain | 715-737 | Extracellular | ||||
Sequence: NLFDREYVASCFNTYGCFWGAER | ||||||
Transmembrane | 738-746 | Beta stranded | ||||
Sequence: QVVATATFR | ||||||
Topological domain | 747 | Periplasmic | ||||
Sequence: F |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MARSKTAQPKHSLRKIAVVVATAVSGMSVYAQA | ||||||
Chain | PRO_0000034748 | 34-747 | Ferrichrome outer membrane transporter/phage receptor | |||
Sequence: AVEPKEDTITVTAAPAPQESAWGPAATIAARQSATGTKTDTPIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSKRPTTEPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF | ||||||
Disulfide bond | 351↔362 | |||||
Sequence: CSDPANAYSKQC | ||||||
Disulfide bond | 725↔731 | |||||
Sequence: CFNTYGC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Induced 1.6-fold by hydroxyurea.
Interaction
Subunit
Monomer (PubMed:36215462, PubMed:36779755, PubMed:8916906, PubMed:9856937, PubMed:9865695).
Interacts with TonB (PubMed:12427941, PubMed:18653801, PubMed:9353297).
Interacts with Escherichia phage T5 receptor-binding protein pb5 (RBP-pb5); this interaction is necessary for the entry of the viral genome into the host cell (PubMed:36215462, PubMed:36779755).
Interacts with TonB (PubMed:12427941, PubMed:18653801, PubMed:9353297).
Interacts with Escherichia phage T5 receptor-binding protein pb5 (RBP-pb5); this interaction is necessary for the entry of the viral genome into the host cell (PubMed:36215462, PubMed:36779755).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P06971 | mcjA Q9X2V7 | 2 | EBI-1116714, EBI-16100378 | |
BINARY | P06971 | tonB P02929 | 4 | EBI-1116714, EBI-6399993 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 40-47 | TonB box | ||||
Sequence: DTITVTAA | ||||||
Domain | 75-187 | TBDR plug | ||||
Sequence: PIQKVPQSISVVTAEEMALHQPKSVKEALSYTPGVSVGTRGASNTYDHLIIRGFAAEGQSQNNYLNGLKLQGNFYNDAVIDPYMLERAEIMRGPVSVLYGKSSPGGLLNMVSK | ||||||
Domain | 192-747 | TBDR beta-barrel | ||||
Sequence: EPLKEVQFKAGTDSLFQTGFDFSDSLDDDGVYSYRLTGLARSANAQQKGSEEQRYAIAPAFTWRPDDKTNFTFLSYFQNEPETGYYGWLPKEGTVEPLPNGKRLPTDFNEGAKNNTYSRNEKMVGYSFDHEFNDTFTVRQNLRFAENKTSQNSVYGYGVCSDPANAYSKQCAALAPADKGHYLARKYVVDDEKLQNFSVDTQLQSKFATGDIDHTLLTGVDFMRMRNDINAWFGYDDSVPLLNLYNPVNTDFDFNAKDPANSGPYRILNKQKQTGVYVQDQAQWDKVLVTLGGRYDWADQESLNRVAGTTDKRDDKQFTWRGGVNYLFDNGVTPYFSYSESFEPSSQVGKDGNIFAPSKGKQYEVGVKYVPEDRPIVVTGAVYNLTKTNNLMADPEGSFFSVEGGEIRARGVEIEAKAALSASVNVVGSYTYTDAEYTTDTTYKGNTPAQVPKHMASLWADYTFFDGPLSGLTLGTGGRYTGSSYGDPANSFKVGSYTVVDALVRYDLARVGMAGSNVALHVNNLFDREYVASCFNTYGCFWGAERQVVATATFRF | ||||||
Motif | 730-747 | TonB C-terminal box | ||||
Sequence: GCFWGAERQVVATATFRF |
Domain
Has two distinct conformations in the presence and absence of ferrichrome. The globular N-terminal domain acts a plug that closes the channel formed by the beta-barrel. Binding of ferrichrome at the cell surface induces a conformational change in FhuA, but does not open the channel. Structural changes are propagated and amplified across the plug, and may facilitate binding of FhuA to TonB (PubMed:9353297, PubMed:9865695).
TonB binding promotes conformational changes in outer surface-exposed loops of FhuA (PubMed:18653801).
Phage T5 is a TonB-independent ligand, and its binding to FhuA results in the formation of high conductance ion channels (PubMed:8617231, PubMed:9353297).
TonB binding promotes conformational changes in outer surface-exposed loops of FhuA (PubMed:18653801).
Phage T5 is a TonB-independent ligand, and its binding to FhuA results in the formation of high conductance ion channels (PubMed:8617231, PubMed:9353297).
Sequence similarities
Belongs to the TonB-dependent receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length747
- Mass (Da)82,182
- Last updated1997-11-01 v2
- Checksum1C2B251D1990E444
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 737 | in Ref. 6; CAA29253 | ||||
Sequence: R → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M12486 EMBL· GenBank· DDBJ | AAB61768.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73261.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAB96726.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
U70214 EMBL· GenBank· DDBJ | AAB08580.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X05810 EMBL· GenBank· DDBJ | CAA29253.1 EMBL· GenBank· DDBJ | Genomic DNA |