ID   ISCA_ECOSE              Reviewed;         107 AA.
AC   B6I5A0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Iron-binding protein IscA {ECO:0000255|HAMAP-Rule:MF_01429};
DE   AltName: Full=Iron-sulfur cluster assembly protein {ECO:0000255|HAMAP-Rule:MF_01429};
GN   Name=iscA {ECO:0000255|HAMAP-Rule:MF_01429}; OrderedLocusNames=ECSE_2814;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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. {ECO:0000255|HAMAP-Rule:MF_01429}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01429};
CC       Note=Binds 2 iron ions per dimer. The dimer may bind additional iron
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01429};
CC   -!- SUBUNIT: Homodimer; may form tetramers and higher multimers.
CC       {ECO:0000255|HAMAP-Rule:MF_01429}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01429}.
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DR   EMBL; AP009240; BAG78338.1; -; Genomic_DNA.
DR   RefSeq; WP_000028953.1; NC_011415.1.
DR   AlphaFoldDB; B6I5A0; -.
DR   SMR; B6I5A0; -.
DR   EnsemblBacteria; BAG78338; BAG78338; ECSE_2814.
DR   GeneID; 67416912; -.
DR   KEGG; ecy:ECSE_2814; -.
DR   HOGENOM; CLU_069054_5_1_6; -.
DR   OMA; GYQYGMA; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProt.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Iron; Metal-binding.
FT   CHAIN           1..107
FT                   /note="Iron-binding protein IscA"
FT                   /id="PRO_1000145754"
FT   BINDING         35
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01429"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01429"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01429"
SQ   SEQUENCE   107 AA;  11556 MW;  CBA945AD547E77DD CRC64;
     MSITLSDSAA ARVNTFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDEPTP EDIVFEDKGV
     KVVVDGKSLQ FLDGTQLDFV KEGLNEGFKF TNPNVKDECG CGESFHV