ISDE_STAA8
ID ISDE_STAA8 Reviewed; 292 AA.
AC Q2FZE6; Q8KQR3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
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=SAOUHSC_01085;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], REGULATION BY FUR, AND IRON-REGULATED
RP EXPRESSION.
RX PubMed=11952908; DOI=10.1046/j.1365-2958.2002.02850.x;
RA Taylor J.M., Heinrichs D.E.;
RT "Transferrin binding in Staphylococcus aureus: involvement of a cell wall-
RT anchored protein.";
RL Mol. Microbiol. 43:1603-1614(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION.
RX PubMed=15240116; DOI=10.1016/j.bbrc.2004.06.025;
RA Mack J., Vermeiren C.L., Heinrichs D.E., Stillman M.J.;
RT "In vivo heme scavenging by Staphylococcus aureus IsdC and IsdE proteins.";
RL Biochem. Biophys. Res. Commun. 320:781-788(2004).
RN [4]
RP MASS SPECTROMETRY, COFACTOR, AND MUTAGENESIS OF TYR-61; TYR-187; HIS-229
RP AND TYR-261.
RX PubMed=17929943; DOI=10.1021/bi7009585;
RA Pluym M., Vermeiren C.L., Mack J., Heinrichs D.E., Stillman M.J.;
RT "Heme binding properties of Staphylococcus aureus IsdE.";
RL Biochemistry 46:12777-12787(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:15240116}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:17929943};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:17929943};
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 -!- MASS SPECTROMETRY: Mass=31112; Method=Electrospray; Note=The measured
CC mass is that of heme-free IsdE.;
CC Evidence={ECO:0000269|PubMed:17929943};
CC -!- MASS SPECTROMETRY: Mass=31728; Method=Electrospray; Note=The measured
CC mass is that of IsdE with a single heme bound.;
CC Evidence={ECO:0000269|PubMed:17929943};
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD30200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY061874; AAL33765.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30200.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001220199.1; NZ_LS483365.1.
DR RefSeq; YP_499630.1; NC_007795.1.
DR AlphaFoldDB; Q2FZE6; -.
DR SMR; Q2FZE6; -.
DR STRING; 1280.SAXN108_1128; -.
DR EnsemblBacteria; ABD30200; ABD30200; SAOUHSC_01085.
DR GeneID; 3919246; -.
DR KEGG; sao:SAOUHSC_01085; -.
DR PATRIC; fig|93061.5.peg.994; -.
DR eggNOG; COG0614; Bacteria.
DR HOGENOM; CLU_038034_2_3_9; -.
DR Proteomes; UP000008816; 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 Reference proteome; 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_0000326215"
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 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 61
FT /note="Y->A: No effect on heme-binding."
FT /evidence="ECO:0000269|PubMed:17929943"
FT MUTAGEN 187
FT /note="Y->A: No effect on heme-binding."
FT /evidence="ECO:0000269|PubMed:17929943"
FT MUTAGEN 229
FT /note="H->A: Only binds to Fe(2+) heme."
FT /evidence="ECO:0000269|PubMed:17929943"
FT MUTAGEN 261
FT /note="Y->A: No effect on heme-binding."
FT /evidence="ECO:0000269|PubMed:17929943"
FT CONFLICT 232
FT /note="P -> S (in Ref. 1; AAL33765)"
FT /evidence="ECO:0000305"
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
