ISCU_ECOLI
ID ISCU_ECOLI Reviewed; 128 AA.
AC P0ACD4; P77310;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU;
DE AltName: Full=Sulfur acceptor protein IscU;
GN Name=iscU; Synonyms=nifU, yfhN; OrderedLocusNames=b2529, JW2513;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A SULFUR ACCEPTOR, INTERACTION WITH ISCS, ACTIVITY REGULATION,
RP AND SUBUNIT.
RX PubMed=11577100; DOI=10.1074/jbc.m106907200;
RA Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E.;
RT "Transfer of sulfur from IscS to IscU during Fe/S cluster assembly.";
RL J. Biol. Chem. 276:44521-44526(2001).
RN [5]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-39; LYS-89; ASN-90; SER-107 AND
RP GLU-111.
RX PubMed=22203963; DOI=10.1073/pnas.1114372109;
RA Kim J.H., Tonelli M., Markley J.L.;
RT "Disordered form of the scaffold protein IscU is the substrate for iron-
RT sulfur cluster assembly on cysteine desulfurase.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:454-459(2012).
RN [6]
RP STRUCTURE BY NMR OF APO-PROTEIN, AND MUTAGENESIS OF ASP-39; ASN-90; SER-107
RP AND GLU-111.
RX PubMed=22734684; DOI=10.1021/bi300579p;
RA Kim J.H., Tonelli M., Kim T., Markley J.L.;
RT "Three-dimensional structure and determinants of stability of the iron-
RT sulfur cluster scaffold protein IscU from Escherichia coli.";
RL Biochemistry 51:5557-5563(2012).
CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters. Exists as 2
CC interconverting forms, a structured (S) and disordered (D) form. The D-
CC state is the preferred substrate for IscS. Converts to the S-state when
CC an Fe-S cluster is assembled, which helps it dissociate from IscS to
CC transfer the Fe-S to an acceptor. It is likely that Fe-S cluster
CC coordination is flexible as the role of this complex is to build and
CC then hand off Fe-S clusters. {ECO:0000269|PubMed:11577100,
CC ECO:0000269|PubMed:22203963}.
CC -!- ACTIVITY REGULATION: Carboxymethylation by iodoacetic acid blocks
CC sulfur transfer to this protein. {ECO:0000269|PubMed:11577100}.
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscS; each subunit of
CC the IscS dimer contacts an IscU monomer. {ECO:0000269|PubMed:11577100,
CC ECO:0000269|PubMed:22203963}.
CC -!- INTERACTION:
CC P0ACD4; P0A6B7: iscS; NbExp=12; IntAct=EBI-561646, EBI-550055;
CC P0ACD4; P0ACD4: iscU; NbExp=5; IntAct=EBI-561646, EBI-561646;
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; U00096; AAC75582.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16423.1; -; Genomic_DNA.
DR PIR; H65029; H65029.
DR RefSeq; NP_417024.1; NC_000913.3.
DR RefSeq; WP_000331707.1; NZ_STEB01000011.1.
DR PDB; 2KQK; NMR; -; A=1-128.
DR PDB; 2L4X; NMR; -; A=1-128.
DR PDBsum; 2KQK; -.
DR PDBsum; 2L4X; -.
DR AlphaFoldDB; P0ACD4; -.
DR BMRB; P0ACD4; -.
DR SASBDB; P0ACD4; -.
DR SMR; P0ACD4; -.
DR BioGRID; 4259432; 63.
DR BioGRID; 851341; 5.
DR ComplexPortal; CPX-2141; iscS-iscU iron-sulfur cluster assembly complex.
DR DIP; DIP-48025N; -.
DR IntAct; P0ACD4; 17.
DR STRING; 511145.b2529; -.
DR jPOST; P0ACD4; -.
DR PaxDb; P0ACD4; -.
DR PRIDE; P0ACD4; -.
DR EnsemblBacteria; AAC75582; AAC75582; b2529.
DR EnsemblBacteria; BAA16423; BAA16423; BAA16423.
DR GeneID; 67416913; -.
DR GeneID; 947002; -.
DR KEGG; ecj:JW2513; -.
DR KEGG; eco:b2529; -.
DR PATRIC; fig|1411691.4.peg.4205; -.
DR EchoBASE; EB3176; -.
DR eggNOG; COG0822; Bacteria.
DR HOGENOM; CLU_079283_5_0_6; -.
DR InParanoid; P0ACD4; -.
DR OMA; YKNPRNY; -.
DR PhylomeDB; P0ACD4; -.
DR BioCyc; EcoCyc:G7324-MON; -.
DR BioCyc; MetaCyc:G7324-MON; -.
DR EvolutionaryTrace; P0ACD4; -.
DR PRO; PR:P0ACD4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990330; C:IscS-IscU complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0019448; P:L-cysteine catabolic process; IC:ComplexPortal.
DR CDD; cd06664; IscU_like; 1.
DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR PANTHER; PTHR10093; PTHR10093; 1.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR01999; iscU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..128
FT /note="Iron-sulfur cluster assembly scaffold protein IscU"
FT /id="PRO_0000166184"
FT MUTAGEN 39
FT /note="D->A,L,V: Stabilizes apo-protein in the S-state
FT (structured)."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT MUTAGEN 39
FT /note="D->G: No effect on equilibrium between S- and D-
FT state (disordered)."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT MUTAGEN 89
FT /note="K->A: Stabilizes apo-protein in the D-state; Fe-S
FT cluster assembly 3-fold slower than wild-type."
FT /evidence="ECO:0000269|PubMed:22203963"
FT MUTAGEN 90
FT /note="N->A: Stabilizes apo-protein in the S-state;
FT biphasic Fe-S cluster assembly 7-fold slower than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT MUTAGEN 90
FT /note="N->D: Stabilizes apo-protein in the D-state; Fe-S
FT cluster assembly 3-fold slower than wild-type."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT MUTAGEN 107
FT /note="S->A: Stabilizes apo-protein in the S-state;
FT biphasic Fe-S cluster assembly 7-fold slower than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT MUTAGEN 111
FT /note="E->A: Stabilizes apo-protein in the S-state;
FT biphasic Fe-S cluster assembly 7-fold slower than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:22203963,
FT ECO:0000269|PubMed:22734684"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2KQK"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2L4X"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2L4X"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2KQK"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2KQK"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:2KQK"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2KQK"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2KQK"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:2KQK"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2KQK"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2KQK"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2L4X"
FT HELIX 105..126
FT /evidence="ECO:0007829|PDB:2KQK"
SQ SEQUENCE 128 AA; 13849 MW; 47516021442B6535 CRC64;
MAYSEKVIDH YENPRNVGSF DNNDENVGSG MVGAPACGDV MKLQIKVNDE GIIEDARFKT
YGCGSAIASS SLVTEWVKGK SLDEAQAIKN TDIAEELELP PVKIHCSILA EDAIKAAIAD
YKSKREAK
