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Iron-regulated surface determinant protein A (Fur-regulated protein A) (Staphylococcal transferrin-binding protein A)

 ISDA_STAAU              Reviewed;         354 AA.
P0C1S5; Q9KW67;
22-AUG-2006, integrated into UniProtKB/Swiss-Prot.
22-AUG-2006, sequence version 1.
07-NOV-2018, entry version 61.
RecName: Full=Iron-regulated surface determinant protein A;
AltName: Full=Fur-regulated protein A;
AltName: Full=Staphylococcal transferrin-binding protein A;
Flags: Precursor;
Name=isdA; Synonyms=frpA, sasE, stbA;
Staphylococcus aureus.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 12598 / Cowan 1 / DSM 20372 / NCIMB 11787 / NCTC 8530;
Sakata N., Wadstrom T., Yamazaki K., Mukai T.;
"Staphylococcal cell wall-anchored surface protein.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[2]
INTERACTION WITH TRANSFERRIN, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=11952908; DOI=10.1046/j.1365-2958.2002.02850.x;
Taylor J.M., Heinrichs D.E.;
"Transferrin binding in Staphylococcus aureus: involvement of a cell
wall-anchored protein.";
Mol. Microbiol. 43:1603-1614(2002).
[3]
SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
STRAIN=RN4220;
PubMed=11830639; DOI=10.1073/pnas.032523999;
Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
"An iron-regulated sortase anchors a class of surface protein during
Staphylococcus aureus pathogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
[4]
ROLE IN IRON ACQUISITION FROM TRANSFERRIN.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=15880095;
Park R.-Y., Sun H.-Y., Choi M.-H., Bai Y.-H., Shin S.-H.;
"Staphylococcus aureus siderophore-mediated iron-acquisition system
plays a dominant and essential role in the utilization of transferrin-
bound iron.";
J. Microbiol. 43:183-190(2005).
[5]
FUNCTION, AND BIOTECHNOLOGY.
PubMed=16544250; DOI=10.1086/501471;
Clarke S.R., Brummell K.J., Horsburgh M.J., McDowell P.W.,
Mohamad S.A.S., Stapleton M.R., Acevedo J., Read R.C., Day N.P.J.,
Peacock S.J., Mond J.J., Kokai-Kun J.F., Foster S.J.;
"Identification of in vivo-expressed antigens of Staphylococcus aureus
and their use in vaccinations for protection against nasal carriage.";
J. Infect. Dis. 193:1098-1108(2006).
-!- FUNCTION: Transfers its hemin to hemin-free IsdC (apo-IsdC)
directly probably through the activation of the holo-IsdA-apo-IsdC
complex and driven by the higher affinity of apo-IsdC for the
cofactor. The reaction is reversible (By similarity). Binds
transferrin, lactoferrin, heme, hemoglobin, hemin, fetuin,
asialofetuin and protein A. Also binds fibronectin and chains B-
beta and gamma of fibrinogen, promoting clumping of S.aureus with
fibrinogen. Was also shown to adhere to plastic (By similarity).
Inactivation of isdA leads to a decrease both in the amount of
heme-iron associated with S.aureus cells and the amount of heme-
iron that enters the staphylococcal cytoplasm. This suggests that
IsdA could play a role in the removal of heme from hemoglobin. It
was also demonstrated that the IsdA-mediated iron-acquisition
system from transferrin could play only an ancillary role in the
iron uptake whereas the siderophore-mediated iron-acquisition
system from transferrin seems to play an essential or dominant
role. Overexpression of isdA enhances S.aureus growth and an isdA
inactivation mutant shows a growth defect when grown in liquid
medium containing heme as the sole iron source which suggests that
IsdA may function as a cell surface reservoir for heme. Involved
in adherence of S.aureus to human desquamated nasal epithelial
cells and is required for nasal colonization. Protects S.aureus
against the bactericidal protease activity of apolactoferrin in
vitro and confers resistance to bovine lactoferricin. Also IsdA
and/or IsdB promote resistance to hydrogen peroxide and killing by
neutrophils (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16544250}.
-!- SUBUNIT: Monomer. Interacts with IsdC (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:11952908};
Peptidoglycan-anchor {ECO:0000305|PubMed:11830639,
ECO:0000305|PubMed:11952908}. Note=Anchored to the cell wall by
sortase A. {ECO:0000305|PubMed:11830639}.
-!- INDUCTION: Repressed by fur in the presence of iron.
{ECO:0000250}.
-!- DOMAIN: The NEAT domain is responsible for binding Fe(3+) and
Fe(2+) heme and fibrinogen. The NEAT domain is an inhibitor of
apolactoferrin activity, while the C-domain confers resistance to
bovine lactoferricin (By similarity). {ECO:0000250}.
-!- BIOTECHNOLOGY: Vaccination with IsdA may prevent S.aureus nasal
carriage and reduce the prevalence of human disease. A combined
vaccine containing IsdA, IsdB, SdrD and SdrE afforded significant
protection in mice against a lethal challenge with S.aureus Newman
or any of the clinical isolates NRS252, N315, NRS248, USA100 and
USA400. The immune response elicited by the combined vaccine is
greater than the one elicited by its individual components.
{ECO:0000269|PubMed:16544250}.
-!- MISCELLANEOUS: Expressed in vivo during infection or colonization
by S.aureus.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB042826; BAA97049.1; -; Genomic_DNA.
RefSeq; WP_000160848.1; NZ_UHCO01000001.1.
ProteinModelPortal; P0C1S5; -.
SMR; P0C1S5; -.
TCDB; 9.A.39.1.2; the gram-positive bacterial hemoglobin receptor (isd) family.
TCDB; 9.A.39.1.3; the gram-positive bacterial hemoglobin receptor (isd) family.
PRO; PR:P0C1S5; -.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd06920; NEAT; 1.
InterPro; IPR019948; Gram-positive_anchor.
InterPro; IPR006635; NEAT_dom.
InterPro; IPR037250; NEAT_dom_sf.
Pfam; PF00746; Gram_pos_anchor; 1.
Pfam; PF05031; NEAT; 1.
SMART; SM00725; NEAT; 1.
SUPFAM; SSF158911; SSF158911; 1.
PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PROSITE; PS50978; NEAT; 1.
1: Evidence at protein level;
Cell wall; Heme; Iron; Metal-binding; Peptidoglycan-anchor; Secreted;
Signal.
SIGNAL 1 46
CHAIN 47 320 Iron-regulated surface determinant
protein A.
/FTId=PRO_0000046082.
PROPEP 321 354 Removed by sortase. {ECO:0000255|PROSITE-
ProRule:PRU00477,
ECO:0000305|PubMed:11830639}.
/FTId=PRO_0000046083.
DOMAIN 62 184 NEAT. {ECO:0000255|PROSITE-
ProRule:PRU00337}.
MOTIF 317 321 LPXTG sorting signal.
{ECO:0000255|PROSITE-ProRule:PRU00477}.
METAL 166 166 Iron (heme axial ligand). {ECO:0000250}.
BINDING 75 75 Heme. {ECO:0000250}.
BINDING 82 82 Heme. {ECO:0000250}.
MOD_RES 320 320 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255|PROSITE-
ProRule:PRU00477}.
SEQUENCE 354 AA; 39133 MW; 2F99C45D8E0ACB67 CRC64;
MTKHYLNSKY QSEQRSSAMK KITMGTASII LGSLVYIGAD SQQVNAATEA TNATNNQSTQ
VSQATSQPIN FQVQKDGSSE KSHMDDYMQH PGKVIKQNNK YYFQAVLNNA SFWKEYKFYN
ANNQELATTV VNDDKKADTR TINVAVEPGY KSLTTKVHIV VPQINYNHRY TTHLEFEKAI
PTLADAAKPN NVKPVQPKPA QPKTPTEQTK PVQPKVEKVK PAVTAPSKNE NRQTTKVVSS
EATKDQSQTQ SARTVKTTQT AQDQNKVQTP VKDVATAKSE SNNQAVSDNK SQQTNKVTKQ
NEVHKQGPSK DSKAKELPKT GLTSVDNFIS TVAFATLALL GSLSLLLFKR KESK


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