ISDE_STAAN
ID ISDE_STAAN Reviewed; 292 AA.
AC Q7A652;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SA0980;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-289 IN COMPLEX WITH HEME, AND
RP COFACTOR.
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:17666394};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:17666394};
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; BA000018; BAB42229.1; -; Genomic_DNA.
DR PIR; A89884; A89884.
DR RefSeq; WP_001220199.1; NC_002745.2.
DR PDB; 2Q8P; X-ray; 1.95 A; A=32-289.
DR PDB; 2Q8Q; X-ray; 2.15 A; A=32-289.
DR PDBsum; 2Q8P; -.
DR PDBsum; 2Q8Q; -.
DR AlphaFoldDB; Q7A652; -.
DR SMR; Q7A652; -.
DR TCDB; 3.A.1.14.17; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; BAB42229; BAB42229; BAB42229.
DR KEGG; sau:SA0980; -.
DR HOGENOM; CLU_038034_2_3_9; -.
DR OMA; IWKHFNA; -.
DR EvolutionaryTrace; Q7A652; -.
DR Proteomes; UP000000751; 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 3D-structure; Cell membrane; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; 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_0000326214"
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:0000269|PubMed:17666394"
FT BINDING 42
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:17666394"
FT BINDING 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:17666394"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:17666394"
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 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 STRAND 36..38
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 139..162
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2Q8P"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2Q8P"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2Q8P"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2Q8P"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:2Q8P"
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
