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Protein

Iron-sulfur cluster assembly scaffold protein IscU

Gene

iscU

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

Functioni

A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D-state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.2 Publications

Enzyme regulationi

Carboxymethylation by iodoacetic acid blocks sulfur transfer to this protein.1 Publication

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • ferrous iron binding Source: GO_Central
  • iron-sulfur transferase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:G7324-MONOMER.
ECOL316407:JW2513-MONOMER.
MetaCyc:G7324-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-sulfur cluster assembly scaffold protein IscU
Alternative name(s):
Sulfur acceptor protein IscU
Gene namesi
Name:iscU
Synonyms:nifU, yfhN
Ordered Locus Names:b2529, JW2513
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13395. iscU.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39D → A, L or V: Stabilizes apo-protein in the S-state (structured). 2 Publications1
Mutagenesisi39D → G: No effect on equilibrium between S- and D-state (disordered). 2 Publications1
Mutagenesisi89K → A: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type. 1 Publication1
Mutagenesisi90N → A: Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. 2 Publications1
Mutagenesisi90N → D: Stabilizes apo-protein in the D-state; Fe-S cluster assembly 3-fold slower than wild-type. 2 Publications1
Mutagenesisi107S → A: Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. 2 Publications1
Mutagenesisi111E → A: Stabilizes apo-protein in the S-state; biphasic Fe-S cluster assembly 7-fold slower than wild-type. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661841 – 128Iron-sulfur cluster assembly scaffold protein IscUAdd BLAST128

Proteomic databases

EPDiP0ACD4.
PaxDbiP0ACD4.
PRIDEiP0ACD4.

Interactioni

Subunit structurei

Homodimer. Forms a heterotetramer with IscS; each subunit of the IscS dimer contacts an IscU monomer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-561646,EBI-561646
iscSP0A6B78EBI-561646,EBI-550055

Protein-protein interaction databases

BioGridi4259432. 56 interactors.
851341. 1 interactor.
DIPiDIP-48025N.
IntActiP0ACD4. 15 interactors.
STRINGi511145.b2529.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi18 – 22Combined sources5
Beta strandi25 – 27Combined sources3
Beta strandi29 – 34Combined sources6
Turni35 – 38Combined sources4
Beta strandi39 – 47Combined sources9
Beta strandi52 – 59Combined sources8
Beta strandi62 – 65Combined sources4
Helixi68 – 77Combined sources10
Helixi82 – 87Combined sources6
Helixi90 – 97Combined sources8
Turni102 – 104Combined sources3
Helixi105 – 126Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KQKNMR-A1-128[»]
2L4XNMR-A1-128[»]
ProteinModelPortaliP0ACD4.
SMRiP0ACD4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACD4.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifU family.Curated

Phylogenomic databases

eggNOGiENOG4107XTC. Bacteria.
COG0822. LUCA.
HOGENOMiHOG000069228.
InParanoidiP0ACD4.
KOiK04488.
OMAiECGDVMR.
PhylomeDBiP0ACD4.

Family and domain databases

CDDicd06664. IscU_like. 1 hit.
InterProiIPR011339. ISC_FeS_clus_asmbl_IscU.
IPR002871. NIF_FeS_clus_asmbl_NifU_N.
[Graphical view]
PfamiPF01592. NifU_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01999. iscU. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ACD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYSEKVIDH YENPRNVGSF DNNDENVGSG MVGAPACGDV MKLQIKVNDE
60 70 80 90 100
GIIEDARFKT YGCGSAIASS SLVTEWVKGK SLDEAQAIKN TDIAEELELP
110 120
PVKIHCSILA EDAIKAAIAD YKSKREAK
Length:128
Mass (Da):13,849
Last modified:November 22, 2005 - v1
Checksum:i47516021442B6535
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75582.1.
AP009048 Genomic DNA. Translation: BAA16423.1.
PIRiH65029.
RefSeqiNP_417024.1. NC_000913.3.
WP_000331707.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75582; AAC75582; b2529.
BAA16423; BAA16423; BAA16423.
GeneIDi947002.
KEGGiecj:JW2513.
eco:b2529.
PATRICi32120455. VBIEscCol129921_2630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75582.1.
AP009048 Genomic DNA. Translation: BAA16423.1.
PIRiH65029.
RefSeqiNP_417024.1. NC_000913.3.
WP_000331707.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KQKNMR-A1-128[»]
2L4XNMR-A1-128[»]
ProteinModelPortaliP0ACD4.
SMRiP0ACD4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259432. 56 interactors.
851341. 1 interactor.
DIPiDIP-48025N.
IntActiP0ACD4. 15 interactors.
STRINGi511145.b2529.

Proteomic databases

EPDiP0ACD4.
PaxDbiP0ACD4.
PRIDEiP0ACD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75582; AAC75582; b2529.
BAA16423; BAA16423; BAA16423.
GeneIDi947002.
KEGGiecj:JW2513.
eco:b2529.
PATRICi32120455. VBIEscCol129921_2630.

Organism-specific databases

EchoBASEiEB3176.
EcoGeneiEG13395. iscU.

Phylogenomic databases

eggNOGiENOG4107XTC. Bacteria.
COG0822. LUCA.
HOGENOMiHOG000069228.
InParanoidiP0ACD4.
KOiK04488.
OMAiECGDVMR.
PhylomeDBiP0ACD4.

Enzyme and pathway databases

BioCyciEcoCyc:G7324-MONOMER.
ECOL316407:JW2513-MONOMER.
MetaCyc:G7324-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ACD4.
PROiP0ACD4.

Family and domain databases

CDDicd06664. IscU_like. 1 hit.
InterProiIPR011339. ISC_FeS_clus_asmbl_IscU.
IPR002871. NIF_FeS_clus_asmbl_NifU_N.
[Graphical view]
PfamiPF01592. NifU_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01999. iscU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiISCU_ECOLI
AccessioniPrimary (citable) accession number: P0ACD4
Secondary accession number(s): P77310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [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.