ISCA_ECO8A
ID ISCA_ECO8A Reviewed; 107 AA.
AC B7M7N1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=ECIAI1_2580;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928160; CAQ99419.1; -; Genomic_DNA.
DR RefSeq; WP_000028953.1; NC_011741.1.
DR AlphaFoldDB; B7M7N1; -.
DR SMR; B7M7N1; -.
DR GeneID; 67416912; -.
DR KEGG; ecr:ECIAI1_2580; -.
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_1000145751"
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