ID   ISDE_STAAB              Reviewed;         292 AA.
AC   Q2YX92;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=SAB0997;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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; AJ938182; CAI80685.1; -; Genomic_DNA.
DR   RefSeq; WP_001220205.1; NC_007622.1.
DR   AlphaFoldDB; Q2YX92; -.
DR   SMR; Q2YX92; -.
DR   KEGG; sab:SAB0997; -.
DR   HOGENOM; CLU_038034_2_3_9; -.
DR   OMA; IWKHFNA; -.
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   3: Inferred from homology;
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_0000326207"
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"
SQ   SEQUENCE   292 AA;  33299 MW;  62F18AD3EC9B48F0 CRC64;
     MRIIKYLTIL VISVVILTSC QSSSSQESTK SGEFRIVPTT VALTMTLDKL DLPIVGKPTS
     YKTLPNRYKD VPEIGQPMEP NVEAVKKLKP THVLSVSTIK DEMQPFYKQL NMKGYFYDFD
     SLKGMQKSIT QLGDQFNRKA QAKELNDHLN SVKQKIENKA VKQKKHPKVL ILMGVPGSYL
     VATDKSYIGD LVKIAGGENV IKVKDRQYIS SNTENLLNIN PDIILRLPHG MPEEVKKMFQ
     KEFKQNDIWK HFKAVKNNHV YDLEEVPFGI TANVDADKAM TQLYDLFYKD KK