ID   ISCA_ECOBW              Reviewed;         107 AA.
AC   C4ZXA3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BWG_2292;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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; CP001396; ACR63084.1; -; Genomic_DNA.
DR   RefSeq; WP_000028953.1; NC_012759.1.
DR   AlphaFoldDB; C4ZXA3; -.
DR   SMR; C4ZXA3; -.
DR   GeneID; 67416912; -.
DR   KEGG; ebw:BWG_2292; -.
DR   HOGENOM; CLU_069054_5_1_6; -.
DR   OMA; GYQYGMA; -.
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_1000215271"
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