ISDA_STAAB
ID ISDA_STAAB Reviewed; 350 AA.
AC Q2YX95;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Iron-regulated surface determinant protein A;
DE AltName: Full=Fur-regulated protein A;
DE AltName: Full=Staphylococcal transferrin-binding protein A;
DE Flags: Precursor;
GN Name=isdA; Synonyms=frpA, stbA; OrderedLocusNames=SAB0994c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: Cell wall-anchored surface receptor that participates in the
CC extraction of heme from oxidized methemoglobin/metHb to enable growth
CC on hemoglobin as a sole iron source (By similarity). Receives heme from
CC IsdB and transfers it to IsdC (By similarity). Also plays a role in the
CC inhibition of host immune response. Protects S.aureus against the
CC bactericidal protease activity of apolactoferrin. Decreases bacterial
CC cellular hydrophobicity, which renders S.aureus resistant to
CC bactericidal human skin fatty acids as well as to beta-defensins and
CC cathelicidin. Also binds fibronectin and chains B-beta and gamma of
CC fibrinogen, promoting clumping of S.aureus with fibrinogen. Involved in
CC adherence of S.aureus to human desquamated nasal epithelial cells and
CC is required for nasal colonization (By similarity).
CC {ECO:0000250|UniProtKB:A6QG31, ECO:0000250|UniProtKB:Q7A152}.
CC -!- SUBUNIT: Monomer. Interacts with IsdC (By similarity). Interacts with
CC IsdB (By similarity). {ECO:0000250|UniProtKB:A6QG31,
CC ECO:0000250|UniProtKB:Q7A152}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:A6QG31}; Peptidoglycan-anchor
CC {ECO:0000250|UniProtKB:A6QG31}. Note=Encodes an LPXTG motif-containing
CC sorting signal that targets to the cell wall, which is catalyzed by
CC sortase A. {ECO:0000250|UniProtKB:A6QG31}.
CC -!- INDUCTION: Repressed by fur in the presence of iron. {ECO:0000250}.
CC -!- DOMAIN: The NEAT domain is responsible for binding Fe(3+) and Fe(2+)
CC heme and fibrinogen. The NEAT domain is an inhibitor of apolactoferrin
CC activity, while the C-domain confers resistance to bovine lactoferricin
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IsdA family. {ECO:0000305}.
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DR EMBL; AJ938182; CAI80682.1; -; Genomic_DNA.
DR RefSeq; WP_000160838.1; NC_007622.1.
DR AlphaFoldDB; Q2YX95; -.
DR SMR; Q2YX95; -.
DR KEGG; sab:SAB0994c; -.
DR HOGENOM; CLU_068057_0_0_9; -.
DR OMA; QTAQDQN; -.
DR PRO; PR:Q2YX95; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06920; NEAT; 1.
DR Gene3D; 2.60.40.1850; -; 1.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR006635; NEAT_dom.
DR InterPro; IPR037250; NEAT_dom_sf.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF05031; NEAT; 1.
DR SMART; SM00725; NEAT; 1.
DR SUPFAM; SSF158911; SSF158911; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS50978; NEAT; 1.
PE 3: Inferred from homology;
KW Cell wall; Heme; Iron; Metal-binding; Peptidoglycan-anchor; Secreted;
KW Signal.
FT SIGNAL 1..46
FT /evidence="ECO:0000250"
FT CHAIN 47..316
FT /note="Iron-regulated surface determinant protein A"
FT /id="PRO_0000284436"
FT PROPEP 317..350
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000284437"
FT DOMAIN 62..184
FT /note="NEAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 187..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 313..317
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 195..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7A655"
FT MOD_RES 316
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 350 AA; 38666 MW; F7E3BFE0BA9A00EE CRC64;
MTKHYLNSKY QSEQRSSAMK KITMGTASII LGSLVYIGAD SQQVNAATEA TNANNNQSAQ
VSQATSQPIN FQVQKDGSSE KSHMDDYMQH PGKVIKQNNK YYFQAVLNNA SFWKEYKFYN
ANNQELATTV VNDDKKADTR TINVAVEPGY KSLTTKVHIV VPQINYNHRY TTHLEFEKAI
PTLADAAKPN NVKPVQPKPA QTKTPTEQTK PVQPKVEKVK PTVTTTSKVE DNHSTKVVST
DTTKDQTKTQ TAHTVKTAQT AQEQNKVQTP VKDVASAKSE SNNQAVSDNK SQQTNKVTKQ
NESPKQASKA KELPKTGLTS VDNFISTVAF ATLALLGSLS LLLFKRKESK
