ISDE_STAAE
ID ISDE_STAAE Reviewed; 292 AA.
AC A6QG34;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=High-affinity heme uptake system protein IsdE;
DE AltName: Full=Iron-regulated surface determinant protein E;
DE AltName: Full=Staphylococcal iron-regulated protein F;
DE Flags: Precursor;
GN Name=isdE; Synonyms=sirF; OrderedLocusNames=NWMN_1044;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP BINDING TO HEME-IRON, IRON-REGULATED EXPRESSION, AND SUBCELLULAR LOCATION.
RX PubMed=12574635; DOI=10.1126/science.1081147;
RA Mazmanian S.K., Skaar E.P., Gaspar A.H., Humayun M., Gornicki P.,
RA Jelenska J., Joachmiak A., Missiakas D.M., Schneewind O.;
RT "Passage of heme-iron across the envelope of Staphylococcus aureus.";
RL Science 299:906-909(2003).
RN [3]
RP FUNCTION, MUTAGENESIS OF MET-78 AND HIS-229, AND DISRUPTION PHENOTYPE.
RX PubMed=17666394; DOI=10.1074/jbc.m704602200;
RA Grigg J.C., Vermeiren C.L., Heinrichs D.E., Murphy M.E.P.;
RT "Heme coordination by Staphylococcus aureus IsdE.";
RL J. Biol. Chem. 282:28815-28822(2007).
CC -!- FUNCTION: Involved in heme (porphyrin) scavenging. Binds Fe(2+) and
CC Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a
CC high-affinity heme binding protein and probably has a role in relaying
CC heme-iron from cell wall-anchored isd proteins receptors to the
CC probable permease IsdF. {ECO:0000269|PubMed:17666394}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Repressed by fur in the presence of iron.
CC -!- DISRUPTION PHENOTYPE: Mutant is still able to grow on hemin as a sole
CC source of iron but slower. {ECO:0000269|PubMed:17666394}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009351; BAF67316.1; -; Genomic_DNA.
DR RefSeq; WP_001220199.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QG34; -.
DR SMR; A6QG34; -.
DR EnsemblBacteria; BAF67316; BAF67316; NWMN_1044.
DR KEGG; sae:NWMN_1044; -.
DR HOGENOM; CLU_038034_2_3_9; -.
DR OMA; IWKHFNA; -.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015886; P:heme transport; IEA:InterPro.
DR InterPro; IPR019957; ABC_transptr_haem-bd_IsdE.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR TIGRFAMs; TIGR03659; IsdE; 1.
DR PROSITE; PS50983; FE_B12_PBP; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..292
FT /note="High-affinity heme uptake system protein IsdE"
FT /id="PRO_0000326216"
FT DOMAIN 35..291
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00344"
FT BINDING 41
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 78
FT /note="M->A: Reduction in heme-binding activity. No effect
FT on S.aures growth on hemin."
FT /evidence="ECO:0000269|PubMed:17666394"
FT MUTAGEN 229
FT /note="H->A: Reduction in heme-binding activity. Abolishes
FT S.aureus growth on hemin."
FT /evidence="ECO:0000269|PubMed:17666394"
SQ SEQUENCE 292 AA; 33271 MW; 62E301DE778458F0 CRC64;
MRIIKYLTIL VISVVILTSC QSSSSQESTK SGEFRIVPTT VALTMTLDKL DLPIVGKPTS
YKTLPNRYKD VPEIGQPMEP NVEAVKKLKP THVLSVSTIK DEMQPFYKQL NMKGYFYDFD
SLKGMQKSIT QLGDQFNRKA QAKELNDHLN SVKQKIENKA AKQKKHPKVL ILMGVPGSYL
VATDKSYIGD LVKIAGGENV IKVKDRQYIS SNTENLLNIN PDIILRLPHG MPEEVKKMFQ
KEFKQNDIWK HFKAVKNNHV YDLEEVPFGI TANVDADKAM TQLYDLFYKD KK