ID   ISCA_ECO27              Reviewed;         107 AA.
AC   B7UGX4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, 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=E2348C_2811;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS10359.1; -; Genomic_DNA.
DR   RefSeq; WP_000028953.1; NC_011601.1.
DR   AlphaFoldDB; B7UGX4; -.
DR   SMR; B7UGX4; -.
DR   EnsemblBacteria; CAS10359; CAS10359; E2348C_2811.
DR   GeneID; 67416912; -.
DR   KEGG; ecg:E2348C_2811; -.
DR   HOGENOM; CLU_069054_5_1_6; -.
DR   OMA; GYQYGMA; -.
DR   Proteomes; UP000008205; 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_1000184884"
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