ID   ISDC_STAAB              Reviewed;         227 AA.
AC   Q2YX94;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Iron-regulated surface determinant protein C;
DE   AltName: Full=Staphylococcal iron-regulated protein D;
DE   Flags: Precursor;
GN   Name=isdC; Synonyms=sirD; OrderedLocusNames=SAB0995;
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: Involved in heme (porphyrin) scavenging. Binds hemoglobin and
CC       almost exclusively free-base protoporphyrin IX. Probably has a role as
CC       the central conduit of the isd heme uptake system, i.e. mediates the
CC       transfer of the iron-containing nutrient from IsdABH to the membrane
CC       translocation system IsdDEF. Hemin-free IsdC (apo-IsdC) acquires hemin
CC       from hemin-containing IsdA (holo-IsdA) probably through the activated
CC       holo-IsdA-apo-IsdC complex and due to the higher affinity of apo-IsdC
CC       for the cofactor. The reaction is reversible (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts with IsdA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}; Peptidoglycan-
CC       anchor {ECO:0000250}. Note=Anchored to the cell wall by sortase B (By
CC       similarity). {ECO:0000250|UniProtKB:Q8KQR1}.
CC   -!- INDUCTION: Repressed by fur in the presence of iron. {ECO:0000250}.
CC   -!- DOMAIN: The NEAT domain binds Fe(3+) heme iron. Reduction of the high-
CC       spin Fe(3+) heme iron to high-spin Fe(2+) results in loss of the heme
CC       from the binding site of the protein due to the absence of a proximal
CC       histidine (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IsdC family. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI80683.1; -; Genomic_DNA.
DR   RefSeq; WP_000789826.1; NC_007622.1.
DR   AlphaFoldDB; Q2YX94; -.
DR   SMR; Q2YX94; -.
DR   KEGG; sab:SAB0995; -.
DR   HOGENOM; CLU_092243_1_0_9; -.
DR   OMA; HNYTIRF; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0030492; F:hemoglobin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015886; P:heme transport; IEA:InterPro.
DR   CDD; cd06920; NEAT; 1.
DR   Gene3D; 2.60.40.1850; -; 1.
DR   InterPro; IPR019909; Haem_uptake_protein_IsdC.
DR   InterPro; IPR006635; NEAT_dom.
DR   InterPro; IPR037250; NEAT_dom_sf.
DR   InterPro; IPR017505; Sortase_SrtB_sig_NPQTN.
DR   Pfam; PF05031; NEAT; 1.
DR   SMART; SM00725; NEAT; 1.
DR   SUPFAM; SSF158911; SSF158911; 1.
DR   TIGRFAMs; TIGR03656; IsdC; 1.
DR   TIGRFAMs; TIGR03068; srtB_sig_NPQTN; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..192
FT                   /note="Iron-regulated surface determinant protein C"
FT                   /id="PRO_0000292561"
FT   PROPEP          193..227
FT                   /note="Removed by sortase B"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT                   /id="PRO_0000292562"
FT   DOMAIN          29..150
FT                   /note="NEAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT   REGION          149..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           189..193
FT                   /note="NPQTN sorting signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT   COMPBIAS        165..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT   BINDING         48
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT   BINDING         132
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"
FT   BINDING         136
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT   MOD_RES         192
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KQR1"
SQ   SEQUENCE   227 AA;  24811 MW;  72ABC09F9F8FDDF6 CRC64;
     MKNILKVFNT TILALIIIIA TFSNSANAAD SGTLNYEVYK YNTNDTSIAN DYFNKPAKYI
     KKNGKLYVQI TVNHSHWITG MSIEGHKENI ISKNTAKDER TSEFEVSKLN GKVDGKIDVY
     IDEKVNGKPF KYDHHYNITY KFNGPTDVAG ANAPGKDDKN SASGSDKGSD GATTGQSESN
     SSNKDKVENP QTNAGTPAYI YAIPVASLAL LIAITLFVRK KSKGNVE