fhuA

Functionⁱ

Involved in the uptake of iron in complex with ferrichrome, an 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:353030, PubMed:2066336, 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:353030, PubMed:9353297, PubMed:12427941).6 Publications

Activity regulationⁱ

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).2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	114	Ferrichrome3 Publications	1
Binding siteⁱ	133	Ferrichrome3 Publications	1
Binding siteⁱ	424	Ferrichrome1 Publication	1
Binding siteⁱ	735	Ferrichrome1 Publication	1

GO - Molecular functionⁱ

cofactor binding
Source: EcoliWiki
Inferred from physical interactionⁱ
- 12944258
iron ion binding
Source: EcoliWiki
Inferred from physical interactionⁱ
- 12944258
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 15644214
siderophore uptake transmembrane transporter activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
signaling receptor activity Source: InterPro
toxic substance binding
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 4584483
virion binding
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 4580999
- 4584483

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

ion transport Source: UniProtKB-KW
iron ion homeostasis Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Receptor
Biological process	Ion transport, Iron transport, Transport
Ligand	Iron

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10302-MONOMER MetaCyc:EG10302-MONOMER

BioCycⁱ

EcoCyc:EG10302-MONOMER
MetaCyc:EG10302-MONOMER

Protein family/group databases

TCDBⁱ	1.B.14.1.2 the outer membrane receptor (omr) family

TCDBⁱ

1.B.14.1.2 the outer membrane receptor (omr) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ferrichrome outer membrane transporter/phage receptorCurated Alternative name(s): Ferric hydroxamate receptorCurated Ferric hydroxamate uptakeCurated Ferrichrome-iron receptor1 Publication
Gene namesⁱ	Name:fhuA1 Publication Synonyms:tonA1 Publication Ordered Locus Names:b0150, JW0146
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10302 fhuA

EcoGeneⁱ

EG10302 fhuA

Subcellular locationⁱ

Cell outer membrane
4 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "Internal deletions in the FhuA receptor of Escherichia coli K-12 define domains of ligand interactions."
  Carmel G., Coulton J.W.
  J. Bacteriol. 173:4394-4403(1991) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Ref.11
  "Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane."
  Boulanger P., le Maire M., Bonhivers M., Dubois S., Desmadril M., Letellier L.
  Biochemistry 35:14216-14224(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, SUBUNIT.
- Ref.17
  "Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide."
  Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W.
  Science 282:2215-2220(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-747 IN COMPLEX WITH FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.18
  "Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes."
  Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J.P., Moras D.
  Cell 95:771-778(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 53-747 IN COMPLEX WITH FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN.
; Multi-pass membrane protein
2 Publications
Manual assertion based on experiment inⁱ
- Ref.17
  "Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide."
  Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W.
  Science 282:2215-2220(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-747 IN COMPLEX WITH FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.18
  "Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes."
  Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J.P., Moras D.
  Cell 95:771-778(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 53-747 IN COMPLEX WITH FERRICHROME, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	34 – 192	PeriplasmicAdd BLAST	159
Transmembraneⁱ	193 – 201	Beta stranded	9
Topological domainⁱ	202 – 206	Extracellular	5
Transmembraneⁱ	207 – 215	Beta stranded	9
Topological domainⁱ	216 – 222	Periplasmic	7
Transmembraneⁱ	223 – 231	Beta stranded	9
Topological domainⁱ	232 – 245	ExtracellularAdd BLAST	14
Transmembraneⁱ	246 – 255	Beta stranded	10
Topological domainⁱ	256 – 259	Periplasmic	4
Transmembraneⁱ	260 – 268	Beta stranded	9
Topological domainⁱ	269 – 312	ExtracellularAdd BLAST	44
Transmembraneⁱ	313 – 321	Beta stranded	9
Topological domainⁱ	322 – 326	Periplasmic	5
Transmembraneⁱ	327 – 335	Beta stranded	9
Topological domainⁱ	336 – 387	ExtracellularAdd BLAST	52
Transmembraneⁱ	388 – 396	Beta stranded	9
Topological domainⁱ	397 – 404	Periplasmic	8
Transmembraneⁱ	405 – 413	Beta stranded	9
Topological domainⁱ	414 – 464	ExtracellularAdd BLAST	51
Transmembraneⁱ	465 – 473	Beta stranded	9
Topological domainⁱ	474 – 477	Periplasmic	4
Transmembraneⁱ	478 – 486	Beta stranded	9
Topological domainⁱ	487 – 508	ExtracellularAdd BLAST	22
Transmembraneⁱ	509 – 517	Beta stranded	9
Topological domainⁱ	518 – 522	Periplasmic	5
Transmembraneⁱ	523 – 531	Beta stranded	9
Topological domainⁱ	532 – 551	ExtracellularAdd BLAST	20
Transmembraneⁱ	552 – 560	Beta stranded	9
Topological domainⁱ	561 – 565	Periplasmic	5
Transmembraneⁱ	566 – 574	Beta stranded	9
Topological domainⁱ	575 – 601	ExtracellularAdd BLAST	27
Transmembraneⁱ	602 – 610	Beta stranded	9
Topological domainⁱ	611 – 613	Periplasmic	3
Transmembraneⁱ	614 – 622	Beta stranded	9
Topological domainⁱ	623 – 645	ExtracellularAdd BLAST	23
Transmembraneⁱ	646 – 654	Beta stranded	9
Topological domainⁱ	655 – 661	Periplasmic	7
Transmembraneⁱ	662 – 670	Beta stranded	9
Topological domainⁱ	671 – 689	ExtracellularAdd BLAST	19
Transmembraneⁱ	690 – 698	Beta stranded	9
Topological domainⁱ	699 – 705	Periplasmic	7
Transmembraneⁱ	706 – 714	Beta stranded	9
Topological domainⁱ	715 – 737	ExtracellularAdd BLAST	23
Transmembraneⁱ	738 – 746	Beta stranded	9
Topological domainⁱ	747	Periplasmic	1

GO - Cellular componentⁱ

cell outer membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 10806384
- 15911532
integral component of membrane Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02907 2-Amino-Vinyl-Phosphate DB01814 2-Tridecanoyloxy-Pentadecanoic Acid DB02700 3-Deoxy-D-Glucosamine DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid DB02767 3-Hydroxy-Myristic Acid DB04039 3-Oxo-Pentadecanoic Acid DB02379 Beta-D-Glucose DB02724 Delta-2-Albomycin A1 DB04160 Diphosphate DB03574 Ferricrocin-Iron DB03111 Glucosamine 1-Phosphate DB02865 Glucosamine 4-Phosphate DB04526 L-Glycero-D-Manno-Heptopyranose DB03017 Lauric Acid DB08231 MYRISTIC ACID DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide DB02626 Phenylferricrocin-Iron DB04220 Rifamycin Cgp 4832

DrugBankⁱ

DB02907 2-Amino-Vinyl-Phosphate
DB01814 2-Tridecanoyloxy-Pentadecanoic Acid
DB02700 3-Deoxy-D-Glucosamine
DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid
DB02767 3-Hydroxy-Myristic Acid
DB04039 3-Oxo-Pentadecanoic Acid
DB02379 Beta-D-Glucose
DB02724 Delta-2-Albomycin A1
DB04160 Diphosphate
DB03574 Ferricrocin-Iron
DB03111 Glucosamine 1-Phosphate
DB02865 Glucosamine 4-Phosphate
DB04526 L-Glycero-D-Manno-Heptopyranose
DB03017 Lauric Acid
DB08231 MYRISTIC ACID
DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide
DB02626 Phenylferricrocin-Iron
DB04220 Rifamycin Cgp 4832

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 33	1 PublicationAdd BLAST		33
ChainⁱPRO_0000034748	34 – 747	Ferrichrome outer membrane transporter/phage receptorAdd BLAST		714

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	351 ↔ 362
Disulfide bondⁱ	725 ↔ 731

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

EPDⁱ	P06971
PaxDbⁱ	P06971
PRIDEⁱ	P06971

PTM databases

CarbonylDBⁱ	P06971

CarbonylDBⁱ

P06971

Expressionⁱ

Inductionⁱ

Induced 1.6-fold by hydroxyurea.1 Publication

Interactionⁱ

Subunit structureⁱ

Monomer (PubMed:8916906, PubMed:9856937, PubMed:9865695). Interacts with TonB (PubMed:9353297, PubMed:12427941, PubMed:18653801).6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
mcjA	Q9X2V7	2	EBI-1116714,EBI-16100378	From Escherichia coli.

With

Entry

#Exp.

IntAct

Notes

mcjA

Q9X2V7

2

EBI-1116714,EBI-16100378

From Escherichia coli.

GO - Molecular functionⁱ

protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 15644214

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259745, 139 interactors
ComplexPortalⁱ	CPX-2843 Ferrichrome outer membrane transporter complex
Database of interacting proteins More...DIPⁱ	DIP-9602N
IntActⁱ	P06971, 7 interactors
STRINGⁱ	316385.ECDH10B_0130

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	44 – 46	Combined sources	3
Helixⁱ	55 – 60	Combined sources	6
Helixⁱ	62 – 64	Combined sources	3
Beta strandⁱ	65 – 67	Combined sources	3
Turnⁱ	68 – 70	Combined sources	3
Helixⁱ	76 – 78	Combined sources	3
Beta strandⁱ	83 – 87	Combined sources	5
Helixⁱ	88 – 94	Combined sources	7
Helixⁱ	99 – 102	Combined sources	4
Turnⁱ	103 – 105	Combined sources	3
Beta strandⁱ	106 – 111	Combined sources	6
Turnⁱ	113 – 116	Combined sources	4
Beta strandⁱ	124 – 127	Combined sources	4
Helixⁱ	131 – 133	Combined sources	3
Beta strandⁱ	137 – 139	Combined sources	3
Helixⁱ	156 – 158	Combined sources	3
Beta strandⁱ	159 – 167	Combined sources	9
Helixⁱ	170 – 173	Combined sources	4
Beta strandⁱ	178 – 186	Combined sources	9
Beta strandⁱ	194 – 202	Combined sources	9
Turnⁱ	203 – 205	Combined sources	3
Beta strandⁱ	206 – 235	Combined sources	30
Beta strandⁱ	237 – 240	Combined sources	4
Beta strandⁱ	242 – 257	Combined sources	16
Beta strandⁱ	260 – 272	Combined sources	13
Turnⁱ	284 – 286	Combined sources	3
Beta strandⁱ	307 – 322	Combined sources	16
Beta strandⁱ	324 – 350	Combined sources	27
Helixⁱ	354 – 356	Combined sources	3
Helixⁱ	360 – 364	Combined sources	5
Turnⁱ	367 – 369	Combined sources	3
Helixⁱ	370 – 372	Combined sources	3
Beta strandⁱ	373 – 400	Combined sources	28
Beta strandⁱ	403 – 434	Combined sources	32
Turnⁱ	436 – 438	Combined sources	3
Beta strandⁱ	445 – 447	Combined sources	3
Turnⁱ	450 – 452	Combined sources	3
Beta strandⁱ	453 – 475	Combined sources	23
Beta strandⁱ	478 – 495	Combined sources	18
Turnⁱ	496 – 499	Combined sources	4
Beta strandⁱ	500 – 517	Combined sources	18
Beta strandⁱ	522 – 534	Combined sources	13
Beta strandⁱ	543 – 545	Combined sources	3
Beta strandⁱ	549 – 560	Combined sources	12
Beta strandⁱ	565 – 584	Combined sources	20
Beta strandⁱ	586 – 588	Combined sources	3
Beta strandⁱ	590 – 610	Combined sources	21
Beta strandⁱ	612 – 630	Combined sources	19
Turnⁱ	632 – 636	Combined sources	5
Beta strandⁱ	644 – 655	Combined sources	12
Beta strandⁱ	656 – 658	Combined sources	3
Turnⁱ	659 – 662	Combined sources	4
Beta strandⁱ	663 – 672	Combined sources	10
Beta strandⁱ	675 – 678	Combined sources	4
Beta strandⁱ	683 – 685	Combined sources	3
Beta strandⁱ	688 – 698	Combined sources	11
Helixⁱ	699 – 702	Combined sources	4
Beta strandⁱ	708 – 715	Combined sources	8
Beta strandⁱ	722 – 727	Combined sources	6
Beta strandⁱ	730 – 733	Combined sources	4
Beta strandⁱ	738 – 746	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P06971
SMRⁱ	P06971
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P06971

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	148 – 149	Ferrichrome binding3 Publications	2
Regionⁱ	277 – 279	Ferrichrome binding3 Publications	3
Regionⁱ	346 – 348	Ferrichrome binding3 Publications	3

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	40 – 47	TonB box		8
Motifⁱ	730 – 747	TonB C-terminal boxAdd BLAST		18

Domainⁱ

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:9865695, 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).4 Publications

Sequence similaritiesⁱ

Belongs to the TonB-dependent receptor family.Curated

Keywords - Domainⁱ

Signal, TonB box, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGⁱ	ENOG4105E0K Bacteria COG1629 LUCA
HOGENOMⁱ	HOG000260252
InParanoidⁱ	P06971
KEGG Orthology (KO) More...KOⁱ	K02014
PhylomeDBⁱ	P06971

Family and domain databases

Gene3Dⁱ	2.170.130.10, 1 hit 2.40.170.20, 1 hit
InterProⁱ	View protein in InterPro IPR012910 Plug_dom IPR037066 Plug_dom_sf IPR039423 TonB-dep_rcpt IPR000531 TonB-dep_rcpt_b-brl IPR010916 TonB_box_CS IPR036942 TonB_rcpt_b-brl_sf IPR010917 TonB_rcpt_CS IPR010105 TonB_sidphr_rcpt
PANTHERⁱ	PTHR32552 PTHR32552, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07715 Plug, 1 hit PF00593 TonB_dep_Rec, 1 hit
TIGRFAMsⁱ	TIGR01783 TonB-siderophor, 1 hit
PROSITEⁱ	View protein in PROSITE PS00430 TONB_DEPENDENT_REC_1, 1 hit PS01156 TONB_DEPENDENT_REC_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P06971-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP 
        60         70         80         90        100
QESAWGPAAT IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK 
       110        120        130        140        150
EALSYTPGVS VGTRGASNTY DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN 
       160        170        180        190        200
DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG LLNMVSKRPT TEPLKEVQFK 
       210        220        230        240        250
AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG SEEQRYAIAP 
       260        270        280        290        300
AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN 
       310        320        330        340        350
EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV 
       360        370        380        390        400
CSDPANAYSK QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT 
       410        420        430        440        450
GDIDHTLLTG VDFMRMRNDI NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP 
       460        470        480        490        500
ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV TLGGRYDWAD QESLNRVAGT 
       510        520        530        540        550
TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG KDGNIFAPSK 
       560        570        580        590        600
GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA 
       610        620        630        640        650
RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW 
       660        670        680        690        700
ADYTFFDGPL SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA 
       710        720        730        740 
RVGMAGSNVA LHVNNLFDRE YVASCFNTYG CFWGAERQVV ATATFRF

Length:747

Mass (Da):82,182

Last modified:November 1, 1997 - v2

Checksum:ⁱ1C2B251D1990E444

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	737	R → P in CAA29253 (PubMed:2823072).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M12486 Genomic DNA Translation: AAB61768.1 U00096 Genomic DNA Translation: AAC73261.1 AP009048 Genomic DNA Translation: BAB96726.2 U70214 Genomic DNA Translation: AAB08580.1 X05810 Genomic DNA Translation: CAA29253.1
PIRⁱ	F64738 QRECFE
NCBI Reference Sequences More...RefSeqⁱ	NP_414692.1, NC_000913.3 WP_000124438.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73261; AAC73261; b0150 BAB96726; BAB96726; BAB96726
GeneIDⁱ	944856
KEGGⁱ	ecj:JW0146 eco:b0150
PATRICⁱ	fig\|1411691.4.peg.2130

Protein	Similar proteins		Species	Score	Length	Source
P06971	TonB-dependent siderophore receptor		Shigella sp.		747	UniRef100_P06971
TonB-dependent siderophore receptor		Escherichia coli M8		747
Ferrichrome ABC transporter		ECOLX		747
Ferrichrome-iron receptor FhuA		Escherichia coli MS 145-7		747
Ferrichrome-iron receptor FhuA		Escherichia coli 1.2264		747
+44

Protein	Similar proteins		Species	Score	Length	Source
P06971	TonB-dependent siderophore receptor		Shigella sp.		747	UniRef90_P06971
TonB-dependent siderophore receptor		Escherichia coli M8		747
Ferrichrome ABC transporter		ECOLX		747
Ferrichrome-iron receptor FhuA		Escherichia coli MS 145-7		747
Ferrichrome-iron receptor FhuA		Escherichia coli 1.2264		747
+743

Protein	Similar proteins		Species	Score	Length	Source
P06971	TonB-dependent siderophore receptor		Shigella sp.		747	UniRef50_P06971
TonB-dependent siderophore receptor		Escherichia coli M8		747
Ferrichrome ABC transporter		ECOLX		747
Ferrichrome-iron receptor FhuA		Escherichia coli MS 145-7		747
Ferrichrome-iron receptor FhuA		Escherichia coli 1.2264		747
+1123

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M12486 Genomic DNA Translation: AAB61768.1 U00096 Genomic DNA Translation: AAC73261.1 AP009048 Genomic DNA Translation: BAB96726.2 U70214 Genomic DNA Translation: AAB08580.1 X05810 Genomic DNA Translation: CAA29253.1
PIRⁱ	F64738 QRECFE
RefSeqⁱ	NP_414692.1, NC_000913.3 WP_000124438.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1BY3	X-ray	2.74	A	34-747	[»]
	1BY5	X-ray	2.60	A	34-747	[»]
	1FCP	X-ray	2.70	A	52-747	[»]
	1FI1	X-ray	2.90	A	52-747	[»]
	1QFF	X-ray	2.70	A	34-747	[»]
	1QFG	X-ray	2.50	A	34-747	[»]
	1QJQ	X-ray	2.95	A	34-747	[»]
	1QKC	X-ray	3.10	A	34-747	[»]
	2FCP	X-ray	2.50	A	34-747	[»]
	2GRX	X-ray	3.30	A/B	34-747	[»]
	4CU4	X-ray	2.30	A	53-747	[»]
ProteinModelPortalⁱ	P06971
SMRⁱ	P06971
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259745, 139 interactors
ComplexPortalⁱ	CPX-2843 Ferrichrome outer membrane transporter complex
DIPⁱ	DIP-9602N
IntActⁱ	P06971, 7 interactors
STRINGⁱ	316385.ECDH10B_0130

Chemistry databases

DrugBankⁱ	DB02907 2-Amino-Vinyl-Phosphate DB01814 2-Tridecanoyloxy-Pentadecanoic Acid DB02700 3-Deoxy-D-Glucosamine DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid DB02767 3-Hydroxy-Myristic Acid DB04039 3-Oxo-Pentadecanoic Acid DB02379 Beta-D-Glucose DB02724 Delta-2-Albomycin A1 DB04160 Diphosphate DB03574 Ferricrocin-Iron DB03111 Glucosamine 1-Phosphate DB02865 Glucosamine 4-Phosphate DB04526 L-Glycero-D-Manno-Heptopyranose DB03017 Lauric Acid DB08231 MYRISTIC ACID DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide DB02626 Phenylferricrocin-Iron DB04220 Rifamycin Cgp 4832

DrugBankⁱ

DB02907 2-Amino-Vinyl-Phosphate
DB01814 2-Tridecanoyloxy-Pentadecanoic Acid
DB02700 3-Deoxy-D-Glucosamine
DB03548 3-Deoxy-D-Manno-Oct-2-Ulosonic Acid
DB02767 3-Hydroxy-Myristic Acid
DB04039 3-Oxo-Pentadecanoic Acid
DB02379 Beta-D-Glucose
DB02724 Delta-2-Albomycin A1
DB04160 Diphosphate
DB03574 Ferricrocin-Iron
DB03111 Glucosamine 1-Phosphate
DB02865 Glucosamine 4-Phosphate
DB04526 L-Glycero-D-Manno-Heptopyranose
DB03017 Lauric Acid
DB08231 MYRISTIC ACID
DB02415 N-Octyl-2-Hydroxyethyl Sulfoxide
DB02626 Phenylferricrocin-Iron
DB04220 Rifamycin Cgp 4832

Protein family/group databases

TCDBⁱ	1.B.14.1.2 the outer membrane receptor (omr) family

TCDBⁱ

1.B.14.1.2 the outer membrane receptor (omr) family

PTM databases

CarbonylDBⁱ	P06971

CarbonylDBⁱ

P06971

Proteomic databases

EPDⁱ	P06971
PaxDbⁱ	P06971
PRIDEⁱ	P06971

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73261; AAC73261; b0150 BAB96726; BAB96726; BAB96726
GeneIDⁱ	944856
KEGGⁱ	ecj:JW0146 eco:b0150
PATRICⁱ	fig\|1411691.4.peg.2130

Organism-specific databases

EchoBASEⁱ	EB0298
EcoGeneⁱ	EG10302 fhuA

Phylogenomic databases

eggNOGⁱ	ENOG4105E0K Bacteria COG1629 LUCA
HOGENOMⁱ	HOG000260252
InParanoidⁱ	P06971
KOⁱ	K02014
PhylomeDBⁱ	P06971

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10302-MONOMER MetaCyc:EG10302-MONOMER

BioCycⁱ

EcoCyc:EG10302-MONOMER
MetaCyc:EG10302-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P06971
Protein Ontology More...PROⁱ	PR:P06971

Family and domain databases

Gene3Dⁱ	2.170.130.10, 1 hit 2.40.170.20, 1 hit
InterProⁱ	View protein in InterPro IPR012910 Plug_dom IPR037066 Plug_dom_sf IPR039423 TonB-dep_rcpt IPR000531 TonB-dep_rcpt_b-brl IPR010916 TonB_box_CS IPR036942 TonB_rcpt_b-brl_sf IPR010917 TonB_rcpt_CS IPR010105 TonB_sidphr_rcpt
PANTHERⁱ	PTHR32552 PTHR32552, 1 hit
Pfamⁱ	View protein in Pfam PF07715 Plug, 1 hit PF00593 TonB_dep_Rec, 1 hit
TIGRFAMsⁱ	TIGR01783 TonB-siderophor, 1 hit
PROSITEⁱ	View protein in PROSITE PS00430 TONB_DEPENDENT_REC_1, 1 hit PS01156 TONB_DEPENDENT_REC_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FHUA_ECOLI
Accessionⁱ	P06971Primary (citable) accession number: P06971 Secondary accession number(s): P71280, P75665
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 190 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P06971 (FHUA_ECOLI)

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Ferrichrome outer membrane transporter/phage receptor

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

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GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

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Experimental Info

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ