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Q6GA85 (ISDA_STAAS) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iron-regulated surface determinant protein A
Alternative name(s):
Fur-regulated protein A
Staphylococcal transferrin-binding protein A
Gene names
Name:isdA
Synonyms:frpA, stbA
Ordered Locus Names:SAS1064
OrganismStaphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]
Taxonomic identifier282459 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transfers its hemin to hemin-free IsdC (apo-IsdC) directly probably through the activated 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. Could play a role in the removal of heme from hemoglobin. 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.

Subunit structure

Monomer. Interacts with IsdC By similarity.

Subcellular location

Secretedcell wall; Peptidoglycan-anchor Probable.

Induction

Repressed by fur in the presence of iron By similarity.

Domain

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.

Sequence similarities

Contains 1 NEAT domain.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   LigandHeme
Iron
Metal-binding
   PTMPeptidoglycan-anchor
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4646 By similarity
Chain47 – 316270Iron-regulated surface determinant protein A
PRO_0000046092
Propeptide317 – 35034Removed by sortase A Potential
PRO_0000046093

Regions

Domain62 – 184123NEAT
Motif313 – 3175LPXTG sorting signal Potential

Sites

Metal binding1661Iron (heme axial ligand) By similarity
Binding site751Heme By similarity
Binding site821Heme By similarity

Amino acid modifications

Modified residue3161Pentaglycyl murein peptidoglycan amidated threonine Potential

Sequences

Sequence LengthMass (Da)Tools
Q6GA85 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 14882D25C0EA3CA6

FASTA35038,746
        10         20         30         40         50         60 
MTKHYLNSKY QSEQRSSAMK KITMGTASII LGSLVYIGAD SQQVNAATEA TNATNNQSTQ 

        70         80         90        100        110        120 
VSQATSQPIN FQVQKDGSSE KSHMDDYMQH PGKVIKQNNK YYFQTVLNNA SFWKEYKFYN 

       130        140        150        160        170        180 
ANNQELATTV VNDNKKADTR TINVAVEPGY KSLTTKVHIV VPQINYNHRY TTHLEFEKAI 

       190        200        210        220        230        240 
PTLADAAKPN NVKPVQPKPA QPKTPTEQTK PVQPKVEKVK PTVTTTSKVE DNHSTKVVST 

       250        260        270        280        290        300 
DTTKDQTKTQ TAHTVKTAQT AQEQNKVQTP VKDVATAKSE SNNQAVSDNK SQQTNKVTKH 

       310        320        330        340        350 
NETPKQASKA KELPKTGLTS VDNFISTVAF ATLALLGSLS LLLFKRKESK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571857 Genomic DNA. Translation: CAG42838.1.
RefSeqYP_043188.1. NC_002953.3.

3D structure databases

ProteinModelPortalQ6GA85.
SMRQ6GA85. Positions 63-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING282459.SAS1064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2864366.
KEGGsas:SAS1064.
PATRIC19551571. VBIStaAur96780_1103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5386.
HOGENOMHOG000107381.
KOK14193.
OMAVNDDKKA.
OrthoDBEOG68SVXG.
ProtClustDBCLSK885153.

Family and domain databases

InterProIPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
IPR006635. NEA_transpt.
[Graphical view]
PfamPF00746. Gram_pos_anchor. 1 hit.
PF05031. NEAT. 1 hit.
[Graphical view]
SMARTSM00725. NEAT. 1 hit.
[Graphical view]
TIGRFAMsTIGR01167. LPXTG_anchor. 1 hit.
PROSITEPS50847. GRAM_POS_ANCHORING. 1 hit.
PS50978. NEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ6GA85.

Entry information

Entry nameISDA_STAAS
AccessionPrimary (citable) accession number: Q6GA85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 19, 2004
Last modified: November 13, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families