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Q2FZE9

- ISDA_STAA8

UniProt

Q2FZE9 - ISDA_STAA8

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Protein

Iron-regulated surface determinant protein A

Gene

isdA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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. 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. May function as a 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751Heme1 Publication
Binding sitei82 – 821Heme1 Publication
Metal bindingi166 – 1661Iron (heme axial ligand)

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-1040-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-regulated surface determinant protein A
Alternative name(s):
Fur-regulated protein A
Staphylococcal transferrin-binding protein A
Gene namesi
Name:isdA
Synonyms:frpA, stbA
Ordered Locus Names:SAOUHSC_01081
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816: Chromosome

Subcellular locationi

Secretedcell wall 1 Publication; Peptidoglycan-anchor 1 Publication

GO - Cellular componenti

  1. cell wall Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831H → A: Does not affect heme-binding. 1 Publication
Mutagenesisi87 – 871Y → A: Decreases heme-binding. 1 Publication
Mutagenesisi101 – 1011Y → A: Does not affect heme-binding. 1 Publication
Mutagenesisi102 – 1021Y → A: Does not affect heme-binding. 1 Publication
Mutagenesisi150 – 1501Y → A: Does not affect heme-binding. 1 Publication
Mutagenesisi166 – 1661Y → A: Almost abolishes heme-binding. 1 Publication
Mutagenesisi170 – 1701Y → A: Strongly decreases heme-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4646By similarityAdd
BLAST
Chaini47 – 316270Iron-regulated surface determinant protein APRO_0000247966Add
BLAST
Propeptidei317 – 35034Removed by sortase APROSITE-ProRule annotationPRO_0000247967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

Keywords - PTMi

Peptidoglycan-anchor

Expressioni

Inductioni

Repressed by fur in the presence of iron.

Interactioni

Subunit structurei

Monomer. Interacts with IsdC (By similarity).By similarity

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01081.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 695Combined sources
Beta strandi71 – 755Combined sources
Beta strandi78 – 814Combined sources
Helixi83 – 875Combined sources
Beta strandi90 – 978Combined sources
Beta strandi100 – 10910Combined sources
Helixi110 – 1123Combined sources
Beta strandi113 – 1197Combined sources
Beta strandi128 – 1347Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi152 – 16110Combined sources
Helixi162 – 1643Combined sources
Beta strandi166 – 17813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ITEX-ray1.60A/B62-184[»]
2ITFX-ray1.90A/B/C/D62-184[»]
ProteinModelPortaliQ2FZE9.
SMRiQ2FZE9. Positions 63-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2FZE9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 184123NEATPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi313 – 3175LPXTG sorting signalPROSITE-ProRule annotation

Domaini

The NEAT domain is responsible for binding Fe3+ and Fe2+ heme and fibrinogen. The NEAT domain is an inhibitor of apolactoferrin activity, while the C-domain confers resistance to bovine lactoferricin (By similarity).By similarity

Sequence similaritiesi

Contains 1 NEAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5386.
HOGENOMiHOG000107381.
KOiK14193.
OMAiVNDDKKA.
OrthoDBiEOG68SVXG.

Family and domain databases

InterProiIPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
IPR006635. NEAT_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF05031. NEAT. 1 hit.
[Graphical view]
SMARTiSM00725. NEAT. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
PS50978. NEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2FZE9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKHYLNSKY QSEQRSSAMK KITMGTASII LGSLVYIGAD SQQVNAATEA
60 70 80 90 100
TNATNNQSTQ VSQATSQPIN FQVQKDGSSE KSHMDDYMQH PGKVIKQNNK
110 120 130 140 150
YYFQTVLNNA SFWKEYKFYN ANNQELATTV VNDNKKADTR TINVAVEPGY
160 170 180 190 200
KSLTTKVHIV VPQINYNHRY TTHLEFEKAI PTLADAAKPN NVKPVQPKPA
210 220 230 240 250
QPKTPTEQTK PVQPKVEKVK PTVTTTSKVE DNHSTKVVST DTTKDQTKTQ
260 270 280 290 300
TAHTVKTAQT AQEQNKVQTP VKDVATAKSE SNNQAVSDNK SQQTNKVTKH
310 320 330 340 350
NETPKQASKA KELPKTGLTS VDNFISTVAF ATLALLGSLS LLLFKRKESK
Length:350
Mass (Da):38,746
Last modified:March 21, 2006 - v1
Checksum:i14882D25C0EA3CA6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051T → A in AAL33768. (PubMed:11952908)Curated
Sequence conflicti134 – 1341N → D in AAL33768. (PubMed:11952908)Curated
Sequence conflicti222 – 2221T → A in AAL33768. (PubMed:11952908)Curated
Sequence conflicti225 – 2262TT → AP in AAL33768. (PubMed:11952908)Curated
Sequence conflicti229 – 2346VEDNHS → NENRQT in AAL33768. (PubMed:11952908)Curated
Sequence conflicti240 – 2423TDT → SEA in AAL33768. (PubMed:11952908)Curated
Sequence conflicti247 – 2482TK → SQ in AAL33768. (PubMed:11952908)Curated
Sequence conflicti251 – 2533TAH → SAR in AAL33768. (PubMed:11952908)Curated
Sequence conflicti258 – 2581A → T in AAL33768. (PubMed:11952908)Curated
Sequence conflicti263 – 2631E → D in AAL33768. (PubMed:11952908)Curated
Sequence conflicti300 – 3001H → Q in AAL33768. (PubMed:11952908)Curated
Sequence conflicti303 – 3042TP → VH AA sequence (PubMed:11952908)Curated
Sequence conflicti307 – 3071A → GPSKD AA sequence (PubMed:11952908)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061874 Genomic DNA. Translation: AAL33768.1.
CP000253 Genomic DNA. Translation: ABD30197.1.
RefSeqiYP_499627.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30197; ABD30197; SAOUHSC_01081.
GeneIDi3919243.
KEGGisao:SAOUHSC_01081.
PATRICi19579665. VBIStaAur99865_0991.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061874 Genomic DNA. Translation: AAL33768.1 .
CP000253 Genomic DNA. Translation: ABD30197.1 .
RefSeqi YP_499627.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ITE X-ray 1.60 A/B 62-184 [» ]
2ITF X-ray 1.90 A/B/C/D 62-184 [» ]
ProteinModelPortali Q2FZE9.
SMRi Q2FZE9. Positions 63-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 93061.SAOUHSC_01081.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD30197 ; ABD30197 ; SAOUHSC_01081 .
GeneIDi 3919243.
KEGGi sao:SAOUHSC_01081.
PATRICi 19579665. VBIStaAur99865_0991.

Phylogenomic databases

eggNOGi COG5386.
HOGENOMi HOG000107381.
KOi K14193.
OMAi VNDDKKA.
OrthoDBi EOG68SVXG.

Enzyme and pathway databases

BioCyci SAUR93061:GIWJ-1040-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q2FZE9.
PROi Q2FZE9.

Family and domain databases

InterProi IPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
IPR006635. NEAT_dom.
[Graphical view ]
Pfami PF00746. Gram_pos_anchor. 1 hit.
PF05031. NEAT. 1 hit.
[Graphical view ]
SMARTi SM00725. NEAT. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01167. LPXTG_anchor. 1 hit.
PROSITEi PS50847. GRAM_POS_ANCHORING. 1 hit.
PS50978. NEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transferrin binding in Staphylococcus aureus: involvement of a cell wall-anchored protein."
    Taylor J.M., Heinrichs D.E.
    Mol. Microbiol. 43:1603-1614(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-60, INTERACTION WITH TRANSFERRIN, SUBCELLULAR LOCATION.
  2. "The Staphylococcus aureus NCTC 8325 genome."
    Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
    (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 8325.
  3. "Conservation, surface exposure, and in vivo expression of the Frp family of iron-regulated cell wall proteins in Staphylococcus aureus."
    Morrissey J.A., Cockayne A., Hammacott J., Bishop K., Denman-Johnson A., Hill P.J., Williams P.
    Infect. Immun. 70:2399-2407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-56, NON-SPECIFIC BINDING TO TRANSFERRIN AND PROTEIN A, BINDING TO PLASTIC, REGULATION BY FUR.
  4. "IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesin."
    Clarke S.R., Wiltshire M.D., Foster S.J.
    Mol. Microbiol. 51:1509-1519(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEMIN; FETUIN; HEMOGLOBIN; TRANSFERRIN; FIBRONECTIN AND FIBRINOGEN, IRON-REGULATED EXPRESSION, ROLE OF THE NEAT DOMAIN.
  5. "Characterization of the heme binding properties of Staphylococcus aureus IsdA."
    Vermeiren C.L., Pluym M., Mack J., Heinrichs D.E., Stillman M.J.
    Biochemistry 45:12867-12875(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Heme binding in the NEAT domains of IsdA and IsdC of Staphylococcus aureus."
    Pluym M., Muryoi N., Heinrichs D.E., Stillman M.J.
    J. Inorg. Biochem. 102:480-488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF THE NEAT DOMAIN.
  7. "Haem recognition by a Staphylococcus aureus NEAT domain."
    Grigg J.C., Vermeiren C.L., Heinrichs D.E., Murphy M.E.P.
    Mol. Microbiol. 63:139-149(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 62-184 OF APOPROTEIN AND IN COMPLEX WITH HEME, ROLE IN IRON ACQUISITION, DOMAIN, MUTAGENESIS OF HIS-83; TYR-87; TYR-101; TYR-102; TYR-150; TYR-166 AND TYR-170.

Entry informationi

Entry nameiISDA_STAA8
AccessioniPrimary (citable) accession number: Q2FZE9
Secondary accession number(s): Q9KW67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2006
Last sequence update: March 21, 2006
Last modified: November 26, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Expressed in vivo during infection or colonization by S.aureus.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3