ID ISDE_STAAR Reviewed; 292 AA.
AC Q6GHV3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
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=SAR1106;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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DR EMBL; BX571856; CAG40108.1; -; Genomic_DNA.
DR RefSeq; WP_001220201.1; NC_002952.2.
DR AlphaFoldDB; Q6GHV3; -.
DR SMR; Q6GHV3; -.
DR KEGG; sar:SAR1106; -.
DR HOGENOM; CLU_038034_2_3_9; -.
DR Proteomes; UP000000596; 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 Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR InterPro; IPR019957; ABC_transptr_haem-bd_IsdE.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR NCBIfam; TIGR03659; IsdE; 1.
DR PANTHER; PTHR30535:SF36; HIGH-AFFINITY HEME UPTAKE SYSTEM PROTEIN ISDE; 1.
DR PANTHER; PTHR30535; VITAMIN B12-BINDING PROTEIN; 1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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_0000326209"
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; 33261 MW; 603301DE748758F3 CRC64;
MRIIKYLTIL VISVVILTSC QSSSSQESTK SGEFRIVPTT VALTMTLDKL DLPIVGKPTS
YKTLPNRYKD VPEIGQPMEP NVEAVKKLKP THVLSVSTIK DEMQPFYKQL NMKGYFYDFD
SLKGMQKSIT QLGDQFNRKA QAKELNDHLN SVKQKIENKA AKQKKHPKVL ILMGVPGSYL
VATDKSYIGD LVKIAGGENV IKVKDRQYIS SNTENLLNIN PDIILRLPHG MSEEVKKMFQ
KEFKQNDIWK HFKAVKNNHV YDLEEVPFGI TANVDADKAM TQLYDLFYKD KK
//
