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ISDE_STAAE
ID   ISDE_STAAE              Reviewed;         292 AA.
AC   A6QG34;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=NWMN_1044;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   BINDING TO HEME-IRON, IRON-REGULATED EXPRESSION, AND SUBCELLULAR LOCATION.
RX   PubMed=12574635; DOI=10.1126/science.1081147;
RA   Mazmanian S.K., Skaar E.P., Gaspar A.H., Humayun M., Gornicki P.,
RA   Jelenska J., Joachmiak A., Missiakas D.M., Schneewind O.;
RT   "Passage of heme-iron across the envelope of Staphylococcus aureus.";
RL   Science 299:906-909(2003).
RN   [3]
RP   FUNCTION, MUTAGENESIS OF MET-78 AND HIS-229, AND DISRUPTION PHENOTYPE.
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. {ECO:0000269|PubMed:17666394}.
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.
CC   -!- DISRUPTION PHENOTYPE: Mutant is still able to grow on hemin as a sole
CC       source of iron but slower. {ECO:0000269|PubMed:17666394}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.
CC       {ECO:0000305}.
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DR   EMBL; AP009351; BAF67316.1; -; Genomic_DNA.
DR   RefSeq; WP_001220199.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QG34; -.
DR   SMR; A6QG34; -.
DR   EnsemblBacteria; BAF67316; BAF67316; NWMN_1044.
DR   KEGG; sae:NWMN_1044; -.
DR   HOGENOM; CLU_038034_2_3_9; -.
DR   OMA; IWKHFNA; -.
DR   Proteomes; UP000006386; 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   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_0000326216"
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"
FT   MUTAGEN         78
FT                   /note="M->A: Reduction in heme-binding activity. No effect
FT                   on S.aures growth on hemin."
FT                   /evidence="ECO:0000269|PubMed:17666394"
FT   MUTAGEN         229
FT                   /note="H->A: Reduction in heme-binding activity. Abolishes
FT                   S.aureus growth on hemin."
FT                   /evidence="ECO:0000269|PubMed:17666394"
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
 
 
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