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Protein

Iron-regulated surface determinant protein A

Gene

isdA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei75Heme1 Publication1
Binding sitei82Heme1 Publication1
Metal bindingi166Iron (heme axial ligand)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Heme, Iron, Metal-binding

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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Secretedcell wall 1 Publication; Peptidoglycan-anchor 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi83H → A: Does not affect heme-binding. 1 Publication1
Mutagenesisi87Y → A: Decreases heme-binding. 1 Publication1
Mutagenesisi101Y → A: Does not affect heme-binding. 1 Publication1
Mutagenesisi102Y → A: Does not affect heme-binding. 1 Publication1
Mutagenesisi150Y → A: Does not affect heme-binding. 1 Publication1
Mutagenesisi166Y → A: Almost abolishes heme-binding. 1 Publication1
Mutagenesisi170Y → A: Strongly decreases heme-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 46By similarityAdd BLAST46
ChainiPRO_000024796647 – 316Iron-regulated surface determinant protein AAdd BLAST270
PropeptideiPRO_0000247967317 – 350Removed by sortase APROSITE-ProRule annotationAdd BLAST34

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei316Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

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

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi65 – 69Combined sources5
Beta strandi71 – 75Combined sources5
Beta strandi78 – 81Combined sources4
Helixi83 – 87Combined sources5
Beta strandi90 – 97Combined sources8
Beta strandi100 – 109Combined sources10
Helixi110 – 112Combined sources3
Beta strandi113 – 119Combined sources7
Beta strandi128 – 134Combined sources7
Turni135 – 138Combined sources4
Beta strandi139 – 146Combined sources8
Beta strandi152 – 161Combined sources10
Helixi162 – 164Combined sources3
Beta strandi166 – 178Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ2FZE9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini62 – 184NEATPROSITE-ProRule annotationAdd BLAST123

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi313 – 317LPXTG sorting signalPROSITE-ProRule annotation5

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

eggNOGiENOG4106ST0. Bacteria.
COG5386. LUCA.
HOGENOMiHOG000107381.
KOiK14193.
OMAiYYFQAVL.

Family and domain databases

CDDicd06920. NEAT. 1 hit.
InterProiIPR019948. Gram-positive_anchor.
IPR006635. NEAT_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF05031. NEAT. 1 hit.
[Graphical view]
SMARTiSM00725. NEAT. 1 hit.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti105T → A in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti134N → D in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti222T → A in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti225 – 226TT → AP in AAL33768 (PubMed:11952908).Curated2
Sequence conflicti229 – 234VEDNHS → NENRQT in AAL33768 (PubMed:11952908).Curated6
Sequence conflicti240 – 242TDT → SEA in AAL33768 (PubMed:11952908).Curated3
Sequence conflicti247 – 248TK → SQ in AAL33768 (PubMed:11952908).Curated2
Sequence conflicti251 – 253TAH → SAR in AAL33768 (PubMed:11952908).Curated3
Sequence conflicti258A → T in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti263E → D in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti300H → Q in AAL33768 (PubMed:11952908).Curated1
Sequence conflicti303 – 304TP → VH AA sequence (PubMed:11952908).Curated2
Sequence conflicti307A → GPSKD AA sequence (PubMed:11952908).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061874 Genomic DNA. Translation: AAL33768.1.
CP000253 Genomic DNA. Translation: ABD30197.1.
RefSeqiWP_000160859.1. NC_007795.1.
YP_499627.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30197; ABD30197; SAOUHSC_01081.
GeneIDi28381319.
3919243.
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.
RefSeqiWP_000160859.1. NC_007795.1.
YP_499627.1. NC_007795.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi93061.SAOUHSC_01081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD30197; ABD30197; SAOUHSC_01081.
GeneIDi28381319.
3919243.
KEGGisao:SAOUHSC_01081.
PATRICi19579665. VBIStaAur99865_0991.

Phylogenomic databases

eggNOGiENOG4106ST0. Bacteria.
COG5386. LUCA.
HOGENOMiHOG000107381.
KOiK14193.
OMAiYYFQAVL.

Miscellaneous databases

EvolutionaryTraceiQ2FZE9.
PROiQ2FZE9.

Family and domain databases

CDDicd06920. NEAT. 1 hit.
InterProiIPR019948. Gram-positive_anchor.
IPR006635. NEAT_dom.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF05031. NEAT. 1 hit.
[Graphical view]
SMARTiSM00725. NEAT. 1 hit.
[Graphical view]
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
PS50978. NEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 73 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.