ISCA_CROS8
ID ISCA_CROS8 Reviewed; 107 AA.
AC A7MGY0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=ESA_00724;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76001.1; -; Genomic_DNA.
DR RefSeq; WP_004385926.1; NC_009778.1.
DR AlphaFoldDB; A7MGY0; -.
DR SMR; A7MGY0; -.
DR EnsemblBacteria; ABU76001; ABU76001; ESA_00724.
DR GeneID; 45714563; -.
DR GeneID; 56729611; -.
DR GeneID; 60762369; -.
DR KEGG; esa:ESA_00724; -.
DR HOGENOM; CLU_069054_5_1_6; -.
DR OMA; GYQYGMA; -.
DR OrthoDB; 1891602at2; -.
DR Proteomes; UP000000260; 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_1000024374"
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; 11473 MW; 1BAC33D2F1CE234B CRC64;
MSITLSDTAA ARVNAFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDAPQP EDTVFEDKGV
KVVVDGKSLQ FLNGTQLDFV KEGLNEGFKF TNPNVKDECG CGESFNV