ID   ISCA_ECOL6              Reviewed;         107 AA.
AC   P0AAC9; P36539; P77691;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Iron-binding protein IscA;
DE   AltName: Full=Iron-sulfur cluster assembly protein;
GN   Name=iscA; OrderedLocusNames=c3053;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per dimer. The dimer may bind additional iron
CC       ions. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; may form tetramers and higher multimers.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81503.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000028953.1; NC_004431.1.
DR   AlphaFoldDB; P0AAC9; -.
DR   SMR; P0AAC9; -.
DR   STRING; 199310.c3053; -.
DR   EnsemblBacteria; AAN81503; AAN81503; c3053.
DR   GeneID; 67416912; -.
DR   KEGG; ecc:c3053; -.
DR   eggNOG; COG0316; Bacteria.
DR   HOGENOM; CLU_069054_5_1_6; -.
DR   OMA; GYQYGMA; -.
DR   Proteomes; UP000001410; 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_0000076998"
FT   BINDING         35
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   107 AA;  11556 MW;  CBA945AD547E77DD CRC64;
     MSITLSDSAA ARVNTFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDEPTP EDIVFEDKGV
     KVVVDGKSLQ FLDGTQLDFV KEGLNEGFKF TNPNVKDECG CGESFHV