ISCA_ECOLI
ID ISCA_ECOLI Reviewed; 107 AA.
AC P0AAC8; P36539; P77691;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Iron-binding protein IscA;
DE AltName: Full=Iron-sulfur cluster assembly protein;
GN Name=iscA; Synonyms=yfhF; OrderedLocusNames=b2528, JW2512;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300516; DOI=10.1128/jb.176.3.610-619.1994;
RA Kawula T.H., Lelivelt M.J.;
RT "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and
RT bgl activation, but not proU derepression, in hns-1 mutant Escherichia
RT coli.";
RL J. Bacteriol. 176:610-619(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [6]
RP CHARACTERIZATION AS AN IRON-SULFUR CLUSTER ASSEMBLY PROTEIN.
RX PubMed=11319236; DOI=10.1074/jbc.m102902200;
RA Ollagnier-de-Choudens S., Mattioli T., Takahashi Y., Fontecave M.;
RT "Iron-sulfur cluster assembly: characterization of IscA and evidence for a
RT specific and functional complex with ferredoxin.";
RL J. Biol. Chem. 276:22604-22607(2001).
RN [7]
RP CHARACTERIZATION AS AN IRON-BINDING PROTEIN.
RX PubMed=14720122; DOI=10.1042/bj20031702;
RA Ding H., Clark R.J.;
RT "Characterization of iron binding in IscA, an ancient iron-sulphur cluster
RT assembly protein.";
RL Biochem. J. 379:433-440(2004).
RN [8]
RP MUTAGENESIS OF CYS-35; CYS-99 AND CYS-101.
RX PubMed=15247288; DOI=10.1074/jbc.m404533200;
RA Ding H., Clark R.J., Ding B.;
RT "IscA mediates iron delivery for assembly of iron-sulfur clusters in IscU
RT under the limited accessible free iron conditions.";
RL J. Biol. Chem. 279:37499-37504(2004).
RN [9]
RP TRANSFER OF IRON-SULFUR CLUSTERS.
RX PubMed=15964837; DOI=10.1074/jbc.m504344200;
RA Bonomi F., Iametti S., Ta D., Vickery L.E.;
RT "Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster
RT assembly scaffold proteins IscU and IscA.";
RL J. Biol. Chem. 280:29513-29518(2005).
RN [10]
RP ROLE OF THE THIOREDOXIN REDUCTASE SYSTEM.
RX PubMed=15985427; DOI=10.1074/jbc.m504638200;
RA Ding H., Harrison K., Lu J.;
RT "Thioredoxin reductase system mediates iron binding in IscA and iron
RT delivery for the iron-sulfur cluster assembly in IscU.";
RL J. Biol. Chem. 280:30432-30437(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-105, AND SUBUNIT.
RX PubMed=14705938; DOI=10.1021/bi035440s;
RA Bilder P.W., Ding H., Newcomer M.E.;
RT "Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel
RT protein fold.";
RL Biochemistry 43:133-139(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=15050828; DOI=10.1016/j.jmb.2004.02.027;
RA Cupp-Vickery J.R., Silberg J.J., Ta D.T., Vickery L.E.;
RT "Crystal structure of IscA, an iron-sulfur cluster assembly protein from
RT Escherichia coli.";
RL J. Mol. Biol. 338:127-137(2004).
CC -!- FUNCTION: Is able to transfer iron-sulfur clusters to apo-ferredoxin.
CC Multiple cycles of [2Fe2S] cluster formation and transfer are observed,
CC suggesting that IscA acts catalytically. Recruits intracellular free
CC iron so as to provide iron for the assembly of transient iron-sulfur
CC cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin
CC reductase system TrxA/TrxB.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per dimer. The dimer may bind additional iron
CC ions.;
CC -!- SUBUNIT: Homodimer; may form tetramers and higher multimers.
CC {ECO:0000269|PubMed:14705938, ECO:0000269|PubMed:15050828}.
CC -!- INTERACTION:
CC P0AAC8; P0A9R4: fdx; NbExp=4; IntAct=EBI-767026, EBI-767037;
CC -!- INDUCTION: Repressed by IscR.
CC -!- MISCELLANEOUS: 2 iron atoms may bind between dimers.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=U01827; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U01827; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U00096; AAC75581.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16422.1; -; Genomic_DNA.
DR PIR; G65029; G65029.
DR RefSeq; NP_417023.1; NC_000913.3.
DR RefSeq; WP_000028953.1; NZ_STEB01000011.1.
DR PDB; 1R94; X-ray; 2.30 A; A/B=1-105.
DR PDB; 1R95; X-ray; 2.65 A; A/B=1-105.
DR PDB; 1S98; X-ray; 2.30 A; A/B=1-107.
DR PDBsum; 1R94; -.
DR PDBsum; 1R95; -.
DR PDBsum; 1S98; -.
DR AlphaFoldDB; P0AAC8; -.
DR SMR; P0AAC8; -.
DR BioGRID; 4260603; 33.
DR BioGRID; 851338; 1.
DR ComplexPortal; CPX-2132; IscA complex.
DR DIP; DIP-35854N; -.
DR IntAct; P0AAC8; 5.
DR STRING; 511145.b2528; -.
DR jPOST; P0AAC8; -.
DR PaxDb; P0AAC8; -.
DR PRIDE; P0AAC8; -.
DR EnsemblBacteria; AAC75581; AAC75581; b2528.
DR EnsemblBacteria; BAA16422; BAA16422; BAA16422.
DR GeneID; 67416912; -.
DR GeneID; 946999; -.
DR KEGG; ecj:JW2512; -.
DR KEGG; eco:b2528; -.
DR PATRIC; fig|1411691.4.peg.4206; -.
DR EchoBASE; EB2053; -.
DR eggNOG; COG0316; Bacteria.
DR HOGENOM; CLU_069054_5_1_6; -.
DR InParanoid; P0AAC8; -.
DR OMA; GYQYGMA; -.
DR PhylomeDB; P0AAC8; -.
DR BioCyc; EcoCyc:EG12132-MON; -.
DR BioCyc; MetaCyc:EG12132-MON; -.
DR EvolutionaryTrace; P0AAC8; -.
DR PRO; PR:P0AAC8; -.
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:1990230; C:iron-sulfur cluster transfer complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0034986; F:iron chaperone activity; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 2.60.300.12; -; 1.
DR HAMAP; MF_01429; Fe_S_insert_IscA; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR InterPro; IPR011302; IscA_proteobacteria.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR02011; IscA; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
DR PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..107
FT /note="Iron-binding protein IscA"
FT /id="PRO_0000076997"
FT BINDING 35
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT MUTAGEN 35
FT /note="C->S: Decrease of iron binding activity."
FT /evidence="ECO:0000269|PubMed:15247288"
FT MUTAGEN 99
FT /note="C->S: Loss of iron binding activity."
FT /evidence="ECO:0000269|PubMed:15247288"
FT MUTAGEN 101
FT /note="C->S: Loss of iron binding activity."
FT /evidence="ECO:0000269|PubMed:15247288"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1R94"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1R94"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1R94"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1R95"
SQ SEQUENCE 107 AA; 11556 MW; CBA945AD547E77DD CRC64;
MSITLSDSAA ARVNTFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDEPTP EDIVFEDKGV
KVVVDGKSLQ FLDGTQLDFV KEGLNEGFKF TNPNVKDECG CGESFHV
