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Protein

Fe(2+) transporter FeoB

Gene

feoB

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

Functioni

Transporter of a GTP-driven Fe2+ uptake system, probably couples GTP-binding to channel opening and Fe2+ uptake (PubMed:12446835, PubMed:19629046). A guanine nucleotide-binding protein (G proteins) in which the guanine nucleotide binding site alternates between an active, GTP-bound state and an inactive, GDP-bound state. This protein has fast intrinsic GDP release, mediated by the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads to conformational changes and channel closing (PubMed:19629046). A GDP release mechanism involving a conformational change of the G5 loop (and thus the removal of the nucleotide-binding and stabilizing interactions) would significantly reduce the affinity for GDP, and conceivably be sufficient for catalysing nucleotide release (PubMed:25374115).6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 17GTP 1PROSITE-ProRule annotation1 Publication8
Nucleotide bindingi35 – 39GTP 2PROSITE-ProRule annotation5
Nucleotide bindingi56 – 59GTP 3PROSITE-ProRule annotation4
Nucleotide bindingi120 – 123GTPPROSITE-ProRule annotation1 Publication1 Publication4
Nucleotide bindingi149 – 151GTPPROSITE-ProRule annotationCurated2 Publications3

GO - Molecular functioni

  • ferrous iron transmembrane transporter activity Source: EcoCyc
  • GTPase activity Source: GO_Central
  • GTP binding Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • ferrous iron transport Source: EcoCyc
  • iron ion homeostasis Source: UniProtKB-KW

Keywordsi

Biological processIon transport, Iron transport, Transport
LigandGTP-binding, Iron, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:FEOB-MONOMER.
MetaCyc:FEOB-MONOMER.

Protein family/group databases

TCDBi9.A.8.1.1. the ferrous iron uptake (feob) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Fe(2+) transporter FeoBCurated
Alternative name(s):
Ferrous iron transport protein B
Gene namesi
Name:feoB
Ordered Locus Names:b3409, JW3372
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12102. feoB.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 281Cytoplasmic1 PublicationAdd BLAST281
Transmembranei282 – 302HelicalSequence analysisAdd BLAST21
Topological domaini303 – 308PeriplasmicCurated6
Transmembranei309 – 329HelicalSequence analysisAdd BLAST21
Topological domaini330 – 343CytoplasmicCuratedAdd BLAST14
Transmembranei344 – 366HelicalSequence analysisAdd BLAST23
Topological domaini367 – 382PeriplasmicCuratedAdd BLAST16
Transmembranei383 – 403HelicalSequence analysisAdd BLAST21
Topological domaini404 – 426CytoplasmicCuratedAdd BLAST23
Transmembranei427 – 447HelicalSequence analysisAdd BLAST21
Topological domaini448 – 452PeriplasmicCurated5
Transmembranei453 – 473HelicalSequence analysisAdd BLAST21
Topological domaini474 – 517CytoplasmicCuratedAdd BLAST44
Transmembranei518 – 538HelicalSequence analysisAdd BLAST21
Topological domaini539 – 663PeriplasmicCuratedAdd BLAST125
Transmembranei664 – 684HelicalSequence analysisAdd BLAST21
Topological domaini685 – 690CytoplasmicCurated6
Transmembranei691 – 711HelicalSequence analysisAdd BLAST21
Topological domaini712 – 721PeriplasmicCurated10
Transmembranei722 – 742HelicalSequence analysisAdd BLAST21
Topological domaini743 – 773Cytoplasmic1 PublicationAdd BLAST31

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Poor uptake of Fe2+.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94D → N: No effect. 1 Publication1
Mutagenesisi123D → N: Loss of guanine nucleotide-binding specificity and Fe(2+) uptake. 1 Publication1
Mutagenesisi150 – 158STRGRGIEA → ATDTKNVQFV: 10-fold reduced affinity for GDP, corresponds to the G5 loop of human GNAI1, a slow GDP-releasing protein, in construct of residues 1-270. 1 Publication9
Mutagenesisi150S → A: Dramatically reduced GDP release-rate, 5-fold increase in affinity for GDP, in construct of residues 1-270. GTP hydrolysis rate 1.5-fold higher than wild-type. 2 Publications1
Mutagenesisi151T → A: GTP hydrolysis rate 4-fold slower than wild-type, releases GDP very quickly. 1 Publication1
Mutagenesisi152R → A: GTP hydrolysis rate 1.3-fold slower than wild-type. 1 Publication1
Mutagenesisi153G → A: GTP hydrolysis rate 1.8-fold slower than wild-type. 1 Publication1
Mutagenesisi154R → A: Dramatically reduced GDP release-rate, in construct of residues 1-270. GTP hydrolysis rate 2.7-fold slower than wild-type. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002108211 – 773Fe(2+) transporter FeoBAdd BLAST773

Proteomic databases

PaxDbiP33650.
PRIDEiP33650.

Expressioni

Inductioni

Iron uptake is repressed by the global regulator Fur in presence of Fe2+ (PubMed:12446835). Induced by hydroxyurea (PubMed:20005847).2 Publications

Interactioni

Subunit structurei

The isolated N-terminal domain (residues 1-274) forms trimers (PubMed:19629046, Ref. 10,PubMed:25374115).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-7131497,EBI-7131497

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261727. 22 interactors.
DIPiDIP-9591N.
MINTiMINT-7914741.
STRINGi511145.b3409.

Structurei

Secondary structure

1773
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi16 – 24Combined sources9
Beta strandi28 – 32Combined sources5
Beta strandi36 – 46Combined sources11
Beta strandi51 – 56Combined sources6
Beta strandi66 – 68Combined sources3
Helixi72 – 83Combined sources12
Beta strandi87 – 94Combined sources8
Helixi95 – 97Combined sources3
Helixi98 – 111Combined sources14
Beta strandi115 – 120Combined sources6
Helixi122 – 127Combined sources6
Beta strandi130 – 132Combined sources3
Helixi134 – 141Combined sources8
Beta strandi145 – 147Combined sources3
Helixi151 – 153Combined sources3
Helixi154 – 164Combined sources11
Helixi179 – 191Combined sources13
Helixi198 – 210Combined sources13
Helixi213 – 218Combined sources6
Helixi220 – 225Combined sources6
Helixi226 – 236Combined sources11
Helixi240 – 259Combined sources20
Beta strandi260 – 262Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HYRX-ray2.20A/B/C1-270[»]
3HYTX-ray2.74A/B/C1-270[»]
3I8SX-ray1.80A/B/C1-274[»]
3I8XX-ray2.25A/B/C1-274[»]
3I92X-ray3.00A/B/C1-274[»]
4Q00X-ray2.10A/B/C1-261[»]
4Q5IX-ray2.80A/B/C/D/E/F1-270[»]
4R98X-ray2.22A/B1-270[»]
ProteinModelPortaliP33650.
SMRiP33650.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33650.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 169FeoB-type GPROSITE-ProRule annotationAdd BLAST167

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 274NFeoB, GTPase protein domain, binds GTP but not ATP5 PublicationsAdd BLAST274

Domaini

Contains a guanine-nucleotide-specific nucleotide-binding site (about residues 1-276) that shows slow GTP hydrolysis (PubMed:12446835, PubMed:23104801). When a non-hydrolyzable GTP analog binds to the trimeric N-terminal domain, it induces a structural shift which opens a pore (PubMed:19629046).3 Publications

Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family. [View classification]PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CE1. Bacteria.
COG0370. LUCA.
HOGENOMiHOG000054023.
InParanoidiP33650.
KOiK04759.
OMAiLVMEMPD.
PhylomeDBiP33650.

Family and domain databases

CDDicd01879. FeoB. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiView protein in InterPro
IPR003373. Fe2_transport_prot-B.
IPR011640. Fe2_transport_prot_B_C.
IPR030389. G_FEOB_dom.
IPR011642. Gate_dom.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF07664. FeoB_C. 1 hit.
PF02421. FeoB_N. 1 hit.
PF07670. Gate. 2 hits.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00437. feoB. 1 hit.
PROSITEiView protein in PROSITE
PS51711. G_FEOB. 1 hit.

Sequencei

Sequence statusi: Complete.

P33650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLTIGLIG NPNSGKTTLF NQLTGSRQRV GNWAGVTVER KEGQFSTTDH
60 70 80 90 100
QVTLVDLPGT YSLTTISSQT SLDEQIACHY ILSGDADLLI NVVDASNLER
110 120 130 140 150
NLYLTLQLLE LGIPCIVALN MLDIAEKQNI RIEIDALSAR LGCPVIPLVS
160 170 180 190 200
TRGRGIEALK LAIDRYKANE NVELVHYAQP LLNEADSLAK VMPSDIPLKQ
210 220 230 240 250
RRWLGLQMLE GDIYSRAYAG EASQHLDAAL ARLRNEMDDP ALHIADARYQ
260 270 280 290 300
CIAAICDVVS NTLTAEPSRF TTAVDKIVLN RFLGLPIFLF VMYLMFLLAI
310 320 330 340 350
NIGGALQPLF DVGSVALFVH GIQWIGYTLH FPDWLTIFLA QGLGGGINTV
360 370 380 390 400
LPLVPQIGMM YLFLSFLEDS GYMARAAFVM DRLMQALGLP GKSFVPLIVG
410 420 430 440 450
FGCNVPSVMG ARTLDAPRER LMTIMMAPFM SCGARLAIFA VFAAAFFGQN
460 470 480 490 500
GALAVFSLYM LGIVMAVLTG LMLKYTIMRG EATPFVMELP VYHVPHVKSL
510 520 530 540 550
IIQTWQRLKG FVLRAGKVII IVSIFLSAFN SFSLSGKIVD NINDSALASV
560 570 580 590 600
SRVITPVFKP IGVHEDNWQA TVGLFTGAMA KEVVVGTLNT LYTAENIQDE
610 620 630 640 650
EFNPAEFNLG EELFSAIDET WQSLKDTFSL SVLMNPIEAS KGDGEMGTGA
660 670 680 690 700
MGVMDQKFGS AAAAYSYLIF VLLYVPCISV MGAIARESSR GWMGFSILWG
710 720 730 740 750
LNIAYSLATL FYQVASYSQH PTYSLVCILA VILFNIVVIG LLRRARSRVD
760 770
IELLATRKSV SSCCAASTTG DCH
Length:773
Mass (Da):84,474
Last modified:February 1, 1994 - v1
Checksum:i1150A14B131AB9AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71063 Genomic DNA. Translation: CAA50387.1.
U18997 Genomic DNA. Translation: AAA58207.1.
U00096 Genomic DNA. Translation: AAC76434.1.
AP009048 Genomic DNA. Translation: BAE77882.1.
AY625107 Genomic DNA. Translation: AAT42461.1.
PIRiA36932.
RefSeqiNP_417868.1. NC_000913.3.
WP_000737039.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76434; AAC76434; b3409.
BAE77882; BAE77882; BAE77882.
GeneIDi947919.
KEGGiecj:JW3372.
eco:b3409.
PATRICi32122254. VBIEscCol129921_3504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71063 Genomic DNA. Translation: CAA50387.1.
U18997 Genomic DNA. Translation: AAA58207.1.
U00096 Genomic DNA. Translation: AAC76434.1.
AP009048 Genomic DNA. Translation: BAE77882.1.
AY625107 Genomic DNA. Translation: AAT42461.1.
PIRiA36932.
RefSeqiNP_417868.1. NC_000913.3.
WP_000737039.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HYRX-ray2.20A/B/C1-270[»]
3HYTX-ray2.74A/B/C1-270[»]
3I8SX-ray1.80A/B/C1-274[»]
3I8XX-ray2.25A/B/C1-274[»]
3I92X-ray3.00A/B/C1-274[»]
4Q00X-ray2.10A/B/C1-261[»]
4Q5IX-ray2.80A/B/C/D/E/F1-270[»]
4R98X-ray2.22A/B1-270[»]
ProteinModelPortaliP33650.
SMRiP33650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261727. 22 interactors.
DIPiDIP-9591N.
MINTiMINT-7914741.
STRINGi511145.b3409.

Protein family/group databases

TCDBi9.A.8.1.1. the ferrous iron uptake (feob) family.

Proteomic databases

PaxDbiP33650.
PRIDEiP33650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76434; AAC76434; b3409.
BAE77882; BAE77882; BAE77882.
GeneIDi947919.
KEGGiecj:JW3372.
eco:b3409.
PATRICi32122254. VBIEscCol129921_3504.

Organism-specific databases

EchoBASEiEB2026.
EcoGeneiEG12102. feoB.

Phylogenomic databases

eggNOGiENOG4105CE1. Bacteria.
COG0370. LUCA.
HOGENOMiHOG000054023.
InParanoidiP33650.
KOiK04759.
OMAiLVMEMPD.
PhylomeDBiP33650.

Enzyme and pathway databases

BioCyciEcoCyc:FEOB-MONOMER.
MetaCyc:FEOB-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP33650.
PROiP33650.

Family and domain databases

CDDicd01879. FeoB. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiView protein in InterPro
IPR003373. Fe2_transport_prot-B.
IPR011640. Fe2_transport_prot_B_C.
IPR030389. G_FEOB_dom.
IPR011642. Gate_dom.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF07664. FeoB_C. 1 hit.
PF02421. FeoB_N. 1 hit.
PF07670. Gate. 2 hits.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00437. feoB. 1 hit.
PROSITEiView protein in PROSITE
PS51711. G_FEOB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFEOB_ECOLI
AccessioniPrimary (citable) accession number: P33650
Secondary accession number(s): Q2M774, Q6IU42
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 15, 2017
This is version 130 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.