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Protein

Iron(3+)-hydroxamate import system permease protein FhuB

Gene

fhuB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex FhuCDB involved in iron3+-hydroxamate import. Responsible for the translocation of the substrate across the membrane.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron

Enzyme and pathway databases

BioCyciEcoCyc:FHUB-MONOMER.
ECOL316407:JW0149-MONOMER.
MetaCyc:FHUB-MONOMER.

Protein family/group databases

TCDBi3.A.1.14.3. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron(3+)-hydroxamate import system permease protein FhuBCurated
Alternative name(s):
Ferric hydroxamate uptake protein BCurated
Ferrichrome transport system permease protein FhuBCurated
Ferrichrome uptake protein FhuBCurated
Iron(III)-hydroxamate import system permease protein FhuBCurated
Gene namesi
Name:fhuB
Ordered Locus Names:b0153, JW0149
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10303. fhuB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521HelicalSequence analysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST
Transmembranei118 – 13821HelicalSequence analysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence analysisAdd
BLAST
Transmembranei197 – 21721HelicalSequence analysisAdd
BLAST
Transmembranei240 – 26021HelicalSequence analysisAdd
BLAST
Transmembranei277 – 29721HelicalSequence analysisAdd
BLAST
Transmembranei303 – 32321HelicalSequence analysisAdd
BLAST
Transmembranei348 – 36821HelicalSequence analysisAdd
BLAST
Transmembranei391 – 41121HelicalSequence analysisAdd
BLAST
Transmembranei424 – 44421HelicalSequence analysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST
Transmembranei479 – 49921HelicalSequence analysisAdd
BLAST
Transmembranei528 – 54821HelicalSequence analysisAdd
BLAST
Transmembranei567 – 58721HelicalSequence analysisAdd
BLAST
Transmembranei607 – 62721HelicalSequence analysisAdd
BLAST
Transmembranei635 – 65521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Iron(3+)-hydroxamate import system permease protein FhuBPRO_0000060028Add
BLAST

Proteomic databases

PaxDbiP06972.
PRIDEiP06972.

Expressioni

Inductioni

Induced 2.1-fold by hydroxyurea.1 Publication

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (FhuC), two transmembrane proteins (FhuB) and a solute-binding protein (FhuD) (Probable). FhuB interacts with FhuC and FhuD (PubMed:1551849, PubMed:8522527, PubMed:9426146).Curated3 Publications

Protein-protein interaction databases

BioGridi4259735. 143 interactions.
DIPiDIP-9603N.
IntActiP06972. 1 interaction.
MINTiMINT-1304500.
STRINGi511145.b0153.

Structurei

3D structure databases

ProteinModelPortaliP06972.
SMRiP06972. Positions 59-323, 356-657.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

FhuD interacts with a periplasmic and a transmembrane/cytoplasmic region of FhuB. The transmembrane region may be part of a pore through which a portion of FhuD inserts into the cytoplasmic membrane during transport.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105S6R. Bacteria.
COG0609. LUCA.
HOGENOMiHOG000260186.
InParanoidiP06972.
KOiK02015.
OMAiWMSGSTY.
OrthoDBiEOG61ZTDC.

Family and domain databases

Gene3Di1.10.3470.10. 2 hits.
InterProiIPR029022. ABC_BtuC-like.
IPR000522. ABC_transptr_permAse.
[Graphical view]
PANTHERiPTHR30472. PTHR30472. 1 hit.
PfamiPF01032. FecCD. 2 hits.
[Graphical view]
SUPFAMiSSF81345. SSF81345. 2 hits.

Sequencei

Sequence statusi: Complete.

P06972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRIALFPA LLLALLVIVA TALTWMNFSQ ALPRSQWAQA AWSPDIDVIE
60 70 80 90 100
QMIFHYSLLP RLAISLLVGA GLGLVGVLFQ QVLRNPLAEP TTLGVATGAQ
110 120 130 140 150
LGITVTTLWA IPGAMASQFA AQAGACVVGL IVFGVAWGKR LSPVTLILAG
160 170 180 190 200
LVVSLYCGAI NQLLVIFHHD QLQSMFLWST GTLTQTDWGG VERLWPQLLG
210 220 230 240 250
GVMLTLLLLR PLTLMGLDDG VARNLGLALS LARLAALSLA IVISALLVNA
260 270 280 290 300
VGIIGFIGLF APLLAKMLGA RRLLPRLMLA SLIGALILWL SDQIILWLTR
310 320 330 340 350
VWMEVSTGSV TALIGAPLLL WLLPRLRSIS APDMKVNDRV AAERQHVLAF
360 370 380 390 400
ALAGGVLLLM AVVVALSFGR DAHGWTWASG ALLEDLMPWR WPRIMAALFA
410 420 430 440 450
GVMLAVAGCI IQRLTGNPMA SPEVLGISSG AAFGVVLMLF LVPGNAFGWL
460 470 480 490 500
LPAGSLGAAV TLLIIMIAAG RGGFSPHRML LAGMALSTAF TMLLMMLQAS
510 520 530 540 550
GDPRMAQVLT WISGSTYNAT DAQVWRTGIV MVILLAITPL CRRWLTILPL
560 570 580 590 600
GGDTARAVGM ALTPTRIALL LLAACLTATA TMTIGPLSFV GLMAPHIARM
610 620 630 640 650
MGFRRTMPHI VISALVGGLL LVFADWCGRM VLFPFQIPAG LLSTFIGAPY
660
FIYLLRKQSR
Length:660
Mass (Da):70,423
Last modified:November 1, 1997 - v2
Checksum:i427313E7B421B0BC
GO

Sequence cautioni

The sequence CAA27853.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → V in CAA29256 (PubMed:2823072).Curated
Sequence conflicti311 – 3111T → I in CAA27852 (PubMed:3020380).Curated
Sequence conflicti311 – 3111T → I in CAA27853 (PubMed:3020380).Curated
Sequence conflicti364 – 3641Missing in CAA27852 (PubMed:3020380).Curated
Sequence conflicti364 – 3641Missing in CAA27853 (PubMed:3020380).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04319 Genomic DNA. Translation: CAA27852.1.
X04319 Genomic DNA. Translation: CAA27853.1. Different initiation.
U70214 Genomic DNA. Translation: AAB08583.1.
U00096 Genomic DNA. Translation: AAC73264.1.
AP009048 Genomic DNA. Translation: BAB96729.2.
X05810 Genomic DNA. Translation: CAA29256.1.
PIRiA64739.
RefSeqiNP_414695.1. NC_000913.3.
WP_000044072.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73264; AAC73264; b0153.
BAB96729; BAB96729; BAB96729.
GeneIDi946890.
KEGGiecj:JW0149.
eco:b0153.
PATRICi32115415. VBIEscCol129921_0159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04319 Genomic DNA. Translation: CAA27852.1.
X04319 Genomic DNA. Translation: CAA27853.1. Different initiation.
U70214 Genomic DNA. Translation: AAB08583.1.
U00096 Genomic DNA. Translation: AAC73264.1.
AP009048 Genomic DNA. Translation: BAB96729.2.
X05810 Genomic DNA. Translation: CAA29256.1.
PIRiA64739.
RefSeqiNP_414695.1. NC_000913.3.
WP_000044072.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP06972.
SMRiP06972. Positions 59-323, 356-657.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259735. 143 interactions.
DIPiDIP-9603N.
IntActiP06972. 1 interaction.
MINTiMINT-1304500.
STRINGi511145.b0153.

Protein family/group databases

TCDBi3.A.1.14.3. the atp-binding cassette (abc) superfamily.

Proteomic databases

PaxDbiP06972.
PRIDEiP06972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73264; AAC73264; b0153.
BAB96729; BAB96729; BAB96729.
GeneIDi946890.
KEGGiecj:JW0149.
eco:b0153.
PATRICi32115415. VBIEscCol129921_0159.

Organism-specific databases

EchoBASEiEB0299.
EcoGeneiEG10303. fhuB.

Phylogenomic databases

eggNOGiENOG4105S6R. Bacteria.
COG0609. LUCA.
HOGENOMiHOG000260186.
InParanoidiP06972.
KOiK02015.
OMAiWMSGSTY.
OrthoDBiEOG61ZTDC.

Enzyme and pathway databases

BioCyciEcoCyc:FHUB-MONOMER.
ECOL316407:JW0149-MONOMER.
MetaCyc:FHUB-MONOMER.

Miscellaneous databases

PROiP06972.

Family and domain databases

Gene3Di1.10.3470.10. 2 hits.
InterProiIPR029022. ABC_BtuC-like.
IPR000522. ABC_transptr_permAse.
[Graphical view]
PANTHERiPTHR30472. PTHR30472. 1 hit.
PfamiPF01032. FecCD. 2 hits.
[Graphical view]
SUPFAMiSSF81345. SSF81345. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Iron hydroxamate transport of Escherichia coli: nucleotide sequence of the fhuB gene and identification of the protein."
    Koester W., Braun V.
    Mol. Gen. Genet. 204:435-442(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 311 AND 364.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins."
    Burkhardt R., Braun V.
    Mol. Gen. Genet. 209:49-55(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
  7. "Iron(III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants."
    Schultz-Hauser G., Koester W., Schwarz H., Braun V.
    J. Bacteriol. 174:2305-2311(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IRON(3+)-HYDROXAMATE TRANSPORT, INTERACTION WITH FHUC.
    Strain: K12.
  8. "Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB."
    Rohrbach M.R., Braun V., Koester W.
    J. Bacteriol. 177:7186-7193(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHUD.
  9. "ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping."
    Mademidis A., Killmann H., Kraas W., Flechsler I., Jung G., Braun V.
    Mol. Microbiol. 26:1109-1123(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHUD, DOMAIN.
  10. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYDROXYUREA.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiFHUB_ECOLI
AccessioniPrimary (citable) accession number: P06972
Secondary accession number(s): P77372
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.