ISCA_SALPC
ID ISCA_SALPC Reviewed; 107 AA.
AC C0PYK9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=SPC_1110;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(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; CP000857; ACN45276.1; -; Genomic_DNA.
DR RefSeq; WP_000028952.1; NC_012125.1.
DR AlphaFoldDB; C0PYK9; -.
DR SMR; C0PYK9; -.
DR EnsemblBacteria; ACN45276; ACN45276; SPC_1110.
DR GeneID; 66756972; -.
DR KEGG; sei:SPC_1110; -.
DR HOGENOM; CLU_069054_5_1_6; -.
DR OMA; GYQYGMA; -.
DR Proteomes; UP000001599; 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_1000184887"
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; 11504 MW; 6EA519AD456F635B CRC64;
MSITLSDSAA ARVNTFLANR GKGFGLRLGV RTSGCSGMAY VLEFVDEPTA EDTVFEDKGV
KVVVDGKSLQ FLDGTQLDFV KEGLNEGFKF SNPNVKDECG CGESFHV
