ISDC_STAA2
ID ISDC_STAA2 Reviewed; 227 AA.
AC A6U0U8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=SaurJH1_1212;
OS Staphylococcus aureus (strain JH1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=359787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JH1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT JH1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000736; ABR52066.1; -; Genomic_DNA.
DR RefSeq; WP_000789821.1; NC_009632.1.
DR AlphaFoldDB; A6U0U8; -.
DR BMRB; A6U0U8; -.
DR SMR; A6U0U8; -.
DR KEGG; sah:SaurJH1_1212; -.
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_5000256993"
FT PROPEP 193..227
FT /note="Removed by sortase B"
FT /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT /id="PRO_0000333250"
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; 24855 MW; 38ABDD96F954B05A CRC64;
MKNILKVFNT TILALIIIIA TFSNSANAAD SGTLNYEVYK YNTNDTSIAN DYFNKPAKYI
KKNGKLYVQI TVNHSHWITG MSIEGHKENI ISKNTAKDER TSEFEVSKLN GKIDGKIDVY
IDEKVNGKPF KYDHHYNITY KFNGPTDVAG ANAPGKDDKN SASGSDKGSD GTTTGQSESN
SSNKDKVENP QTNAGTPAYI YAIPVASLAL LIAITLFVRK KSKGNVE
