ID ISDE_STAAW Reviewed; 292 AA.
AC Q7A150;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 54.
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=MW1015;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-
RT acquired MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- FUNCTION: Involved in heme (porphyrin) scavenging. Binds Fe(2+)
CC and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions
CC as a high-affinity heme binding protein and probably has a role in
CC relaying heme-iron from cell wall-anchored isd proteins receptors
CC to the putative probable IsdF (By similarity).
CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
CC -!- INDUCTION: Repressed by fur in the presence of iron (By
CC similarity).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8
CC family.
CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain.
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DR EMBL; BA000033; BAB94880.1; -; Genomic_DNA.
DR RefSeq; NP_645832.1; NC_003923.1.
DR ProteinModelPortal; Q7A150; -.
DR SMR; Q7A150; 32-289.
DR STRING; 196620.MW1015; -.
DR EnsemblBacteria; BAB94880; BAB94880; BAB94880.
DR GeneID; 1003127; -.
DR KEGG; sam:MW1015; -.
DR PATRIC; 19568610; VBIStaAur44266_1064.
DR eggNOG; COG0614; -.
DR HOGENOM; HOG000059045; -.
DR KO; K02016; -.
DR OMA; MFDEEFK; -.
DR ProtClustDB; CLSK2297812; -.
DR BioCyc; SAUR196620:GJ9Z-1039-MONOMER; -.
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; Complete proteome; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Signal; Transport.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 292 High-affinity heme uptake system protein
FT IsdE.
FT /FTId=PRO_0000326213.
FT DOMAIN 35 291 Fe/B12 periplasmic-binding.
FT METAL 78 78 Iron (heme axial ligand) (By similarity).
FT METAL 229 229 Iron (heme axial ligand) (By similarity).
FT BINDING 41 41 Heme; via amide nitrogen (By similarity).
FT BINDING 42 42 Heme; via amide nitrogen (By similarity).
FT BINDING 60 60 Heme (By similarity).
FT BINDING 61 61 Heme; via amide nitrogen (By similarity).
FT LIPID 20 20 N-palmitoyl cysteine (Potential).
FT LIPID 20 20 S-diacylglycerol cysteine (Potential).
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
//
