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Protein

Iron-sulfur cluster assembly scaffold protein IscU

Gene

iscU

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. 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 (Probable).1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3358-MONOMER.
ECOO157:Z3796-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
Ordered Locus Names:Z3796, ECs3395
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1212Missing : No longer binds IscS. 1 PublicationAdd
BLAST
Mutagenesisi1 – 66Missing : Partial loss of IscS binding. 1 Publication
Mutagenesisi5 – 51E → L: Binds IscS. 1 Publication
Mutagenesisi9 – 91D → R: Binds IscS. 1 Publication
Mutagenesisi11 – 111Y → A: Binds IscS. 1 Publication
Mutagenesisi98 – 981E → R: Binds IscS. 1 Publication
Mutagenesisi103 – 1031K → E: No longer binds IscS. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128Iron-sulfur cluster assembly scaffold protein IscUPRO_0000166185Add
BLAST

Proteomic databases

PRIDEiP0ACD6.

Interactioni

Subunit structurei

Forms a heterotetramer with IscS; each subunit of the IscS dimer contacts an IscU monomer. Certain pairs of proteins can bind simultaneously to IscS; IscS-IscU-CyaY and IscS-IscU-IscX complexes can be isolated in vitro, but others (IscS-IscU-TusA) cannot. IscU can displace TusA from IscS.1 Publication

Protein-protein interaction databases

DIPiDIP-58575N.
STRINGi155864.Z3796.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Beta strandi15 – 184Combined sources
Beta strandi25 – 339Combined sources
Turni35 – 373Combined sources
Beta strandi40 – 478Combined sources
Beta strandi49 – 513Combined sources
Beta strandi53 – 6210Combined sources
Helixi64 – 7714Combined sources
Helixi82 – 865Combined sources
Helixi90 – 978Combined sources
Helixi101 – 1044Combined sources
Helixi105 – 12319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LVLX-ray3.00A2-128[»]
ProteinModelPortaliP0ACD6.
SMRiP0ACD6. Positions 1-128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NifU family.Curated

Phylogenomic databases

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

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.

P0ACD6-1 [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
AE005174 Genomic DNA. Translation: AAG57643.1.
BA000007 Genomic DNA. Translation: BAB36818.1.
PIRiC91053.
G85897.
RefSeqiNP_311422.1. NC_002695.1.
WP_000331707.1. NZ_LPWC01000059.1.

Genome annotation databases

EnsemblBacteriaiAAG57643; AAG57643; Z3796.
BAB36818; BAB36818; BAB36818.
GeneIDi915163.
KEGGiece:Z3796.
ecs:ECs3395.
PATRICi18356222. VBIEscCol44059_3306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57643.1.
BA000007 Genomic DNA. Translation: BAB36818.1.
PIRiC91053.
G85897.
RefSeqiNP_311422.1. NC_002695.1.
WP_000331707.1. NZ_LPWC01000059.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LVLX-ray3.00A2-128[»]
ProteinModelPortaliP0ACD6.
SMRiP0ACD6. Positions 1-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58575N.
STRINGi155864.Z3796.

Proteomic databases

PRIDEiP0ACD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57643; AAG57643; Z3796.
BAB36818; BAB36818; BAB36818.
GeneIDi915163.
KEGGiece:Z3796.
ecs:ECs3395.
PATRICi18356222. VBIEscCol44059_3306.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3358-MONOMER.
ECOO157:Z3796-MONOMER.

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_ECO57
AccessioniPrimary (citable) accession number: P0ACD6
Secondary accession number(s): P77310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: September 7, 2016
This is version 71 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.