(data stored in ACNUC7421 zone)

HOGENOM: STAAN_1_PE1007

ID   STAAN_1_PE1007                       STANDARD;      PRT;   350 AA.
AC   STAAN_1_PE1007; Q7A655;
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=Iron-regulated surface determinant protein A;AltName:
DE   Full=Fur-regulated protein A;AltName: Full=Staphylococcal
DE   transferrin-binding protein A;Flags: Precursor; (STAAN_1.PE1007).
GN   Name=isdA; Synonyms=frpA, stbA; OrderedLocusNames=SA0977;
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.PE1007.
CC       Staphylococcus aureus subsp. aureus N315, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ISDA_STAAN
CC   -!- FUNCTION: Transfers its hemin to hemin-free isdC (apo-isdC)
CC       directly probably through the activated holo-isdA-apo-isdC complex
CC       and driven by the higher affinity of apo-isdC for the cofactor.
CC       The reaction is reversible. Binds transferrin, lactoferrin, heme,
CC       hemoglobin, hemin, fetuin, asialofetuin and protein A. Also binds
CC       fibronectin and chains B-beta and gamma of fibrinogen. Could play
CC       a role in the removal of heme from hemoglobin. The isdA-mediated
CC       iron-acquisition system from transferrin could play only an
CC       ancillary role in the iron uptake whereas the siderophore-mediated
CC       iron-acquisition system from transferrin seems to play an
CC       essential or dominant role. May function as a reservoir for heme.
CC       Involved in adherence of S.aureus to human desquamated nasal
CC       epithelial cells and is required for nasal colonization. Protects
CC       S.aureus against the bactericidal protease activity of
CC       apolactoferrin in vitro and confers resistance to bovine
CC       lactoferricin. Also isdA and/or isdB promote resistance to
CC       hydrogen peroxide and killing by neutrophils (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with isdC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor
CC       (Probable).
CC   -!- INDUCTION: Repressed by fur in the presence of iron (By
CC       similarity).
CC   -!- DOMAIN: The NEAT domain is responsible for binding Fe(3+) and
CC       Fe(2+) heme and fibrinogen. The NEAT domain is an inhibitor of
CC       apolactoferrin activity, while the C-domain confers resistance to
CC       bovine lactoferricin (By similarity).
CC   -!- BIOTECHNOLOGY: A combined vaccine containing isdA, isdB, sdrD and
CC       sdrE afforded significative protection in mice against a lethal
CC       challenge with S.aureus Newman or any of the clinical isolates
CC       NRS252, N315, NRS248, USA100 and USA400. The immune response
CC       elicited by the combined vaccine is greater than the one elicited
CC       by its individual components.
CC   -!- SIMILARITY: Contains 1 NEAT domain.
CC   -!- GENE_FAMILY: HOG000107381 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7A655; -.
DR   EMBL; BA000018; BAB42226.1; -; Genomic_DNA.
DR   PIR; F89883; F89883.
DR   RefSeq; NP_374247.1; NC_002745.2.
DR   ProteinModelPortal; Q7A655; -.
DR   SMR; Q7A655; 62-184.
DR   STRING; Q7A655; -.
DR   EnsemblBacteria; EBSTAT00000001624; EBSTAP00000001624; EBSTAG00000001624.
DR   GeneID; 1123804; -.
DR   GenomeReviews; BA000018_GR; SA0977.
DR   KEGG; sau:SA0977; -.
DR   eggNOG; COG5386; -.
DR   GeneTree; EBGT00050000023708; -.
DR   OMA; NDDKKAD; -.
DR   ProtClustDB; CLSK885153; -.
DR   BioCyc; SAUR158879:SA0977-MON; -.
DR   GO; GO:0009986; C:cell surface; IEA:InterPro.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019948; Gram-positive_anchor.
DR   InterPro; IPR019931; LPXTG-motif_cell_wall_anchor.
DR   InterPro; IPR006635; NEA_transpt.
DR   InterPro; IPR001899; Surface_protein_Gram_pos_cocci.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF05031; NEAT; 1.
DR   SMART; SM00725; NEAT; 1.
DR   TIGRFAMs; TIGR01167; LPXTG_anchor; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS50978; NEAT; 1.
DR   HOGENOMDNA; STAAN_1.PE1007; -.
KW   cell surface protein;
KW   Cell wall; Complete proteome; Heme; Iron; Metal-binding;
KW   Peptidoglycan-anchor; Secreted; Signal.
SQ   SEQUENCE   350 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTKHYLNSKY QSEQRSSAMK KITMGTASII LGSLVYIGAD SQQVNAATEA TNATNNQSTQ
     VSQATSQPIN FQVQKDGSSE KSHMDDYMQH PGKVIKQNNK YYFQTVLNNA SFWKEYKFYN
     ANNQELATTV VNDNKKADTR TINVAVEPGY KSLTTKVHIV VPQINYNHRY TTHLEFEKAI
     PTLADAAKPN NVKPVQPKPA QPKTPTEQTK PVQPKVEKVK PTVTTTSKVE DNHSTKVVST
     DTTKDQTKTQ TAHTVKTAQT AQEQNKVQTP VKDVATAKSE SNNQAVSDNK SQQTNKVTKH
     NETPKQASKA KELPKTGLTS VDNFISTVAF ATLALLGSLS LLLFKRKESK
//

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