ISCA_ECOK1
ID ISCA_ECOK1 Reviewed; 107 AA.
AC A1AE65;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Ecok1_24610;
GN ORFNames=APECO1_3997;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01955.1; -; Genomic_DNA.
DR RefSeq; WP_000028953.1; NC_008563.1.
DR AlphaFoldDB; A1AE65; -.
DR SMR; A1AE65; -.
DR EnsemblBacteria; ABJ01955; ABJ01955; APECO1_3997.
DR GeneID; 67416912; -.
DR KEGG; ecv:APECO1_3997; -.
DR HOGENOM; CLU_069054_5_1_6; -.
DR OMA; GYQYGMA; -.
DR Proteomes; UP000008216; 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_1000024372"
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
