(data stored in ACNUC7421 zone)

HOGENOM: STAAN_1_PE1010

ID   STAAN_1_PE1010                       STANDARD;      PRT;   292 AA.
AC   STAAN_1_PE1010; Q7A652;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=High-affinity heme uptake system protein isdE;AltName:
DE   Full=Iron-regulated surface determinant protein E;AltName:
DE   Full=Staphylococcal iron-regulated protein F;Flags: Precursor;
DE   (STAAN_1.PE1010).
GN   Name=isdE; Synonyms=sirF; OrderedLocusNames=SA0980;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAN_1.PE1010.
CC       Staphylococcus aureus subsp. aureus N315, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ISDE_STAAN
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 probable permease isdF (By similarity).
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit.
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.
CC   -!- GENE_FAMILY: HOG000059045 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7A652; -.
DR   EMBL; BA000018; BAB42229.1; -; Genomic_DNA.
DR   PIR; A89884; A89884.
DR   RefSeq; NP_374250.1; NC_002745.2.
DR   PDB; 2Q8P; X-ray; 1.95 A; A=31-289.
DR   PDB; 2Q8Q; X-ray; 2.15 A; A=31-289.
DR   PDBsum; 2Q8P; -.
DR   PDBsum; 2Q8Q; -.
DR   ProteinModelPortal; Q7A652; -.
DR   SMR; Q7A652; 32-289.
DR   STRING; Q7A652; -.
DR   TCDB; 3.A.1.14.18; ATP-binding cassette (ABC) superfamily.
DR   EnsemblBacteria; EBSTAT00000001670; EBSTAP00000001670; EBSTAG00000001670.
DR   GeneID; 1123807; -.
DR   GenomeReviews; BA000018_GR; SA0980.
DR   KEGG; sau:SA0980; -.
DR   eggNOG; COG0614; -.
DR   GeneTree; EBGT00050000023814; -.
DR   OMA; SNTEYLQ; -.
DR   ProtClustDB; CLSK2297812; -.
DR   BioCyc; SAUR158879:SA0980-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006827; P:high-affinity iron ion transport; IEA:InterPro.
DR   InterPro; IPR019957; ABC_transptr_haem-bd_IsdE.
DR   InterPro; IPR002491; ABC_transptr_periplasmic_BP.
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.
DR   HOGENOMDNA; STAAN_1.PE1010; -.
KW   hypothetical protein;
KW   3D-structure; Cell membrane; Complete proteome; Heme; Iron;
KW   Lipoprotein; Membrane; Metal-binding; Palmitate; Signal; Transport.
SQ   SEQUENCE   292 AA;  UNKNOWN MW;  UNKNOWN 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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