ISDC_STAAE
ID ISDC_STAAE Reviewed; 227 AA.
AC A6QG32;
DT 05-FEB-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=NWMN_1042;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP BINDING TO HEME-IRON AND HEMOGLOBIN, IRON-REGULATED EXPRESSION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12574635; DOI=10.1126/science.1081147;
RA Mazmanian S.K., Skaar E.P., Gaspar A.H., Humayun M., Gornicki P.,
RA Jelenska J., Joachmiak A., Missiakas D.M., Schneewind O.;
RT "Passage of heme-iron across the envelope of Staphylococcus aureus.";
RL Science 299:906-909(2003).
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
CC {ECO:0000269|PubMed:12574635}; Peptidoglycan-anchor
CC {ECO:0000269|PubMed:12574635}. Note=Anchored to the cell wall by
CC sortase B (By 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; AP009351; BAF67314.1; -; Genomic_DNA.
DR RefSeq; WP_000789821.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QG32; -.
DR BMRB; A6QG32; -.
DR SMR; A6QG32; -.
DR EnsemblBacteria; BAF67314; BAF67314; NWMN_1042.
DR KEGG; sae:NWMN_1042; -.
DR HOGENOM; CLU_092243_1_0_9; -.
DR OMA; HNYTIRF; -.
DR Proteomes; UP000006386; Chromosome.
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 1: Evidence at protein level;
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_0000317043"
FT PROPEP 193..227
FT /note="Removed by sortase B"
FT /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT /id="PRO_0000317044"
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
