ISDC_STAAW
ID ISDC_STAAW Reviewed; 227 AA.
AC Q7A151;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=MW1013;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP FUNCTION IN ACQUIRING HEMIN FROM ISDA, AND INTERACTION WITH ISDA.
RX PubMed=18184657; DOI=10.1074/jbc.m708372200;
RA Liu M., Tanaka W.N., Zhu H., Xie G., Dooley D.M., Lei B.;
RT "Direct hemin transfer from IsdA to IsdC in the iron-regulated surface
RT determinant (Isd) heme acquisition system of Staphylococcus aureus.";
RL J. Biol. Chem. 283:6668-6676(2008).
RN [3]
RP INDUCTION.
RX PubMed=18097052; DOI=10.4049/jimmunol.180.1.500;
RA Palazzolo-Ballance A.M., Reniere M.L., Braughton K.R., Sturdevant D.E.,
RA Otto M., Kreiswirth B.N., Skaar E.P., DeLeo F.R.;
RT "Neutrophil microbicides induce a pathogen survival response in community-
RT associated methicillin-resistant Staphylococcus aureus.";
RL J. Immunol. 180:500-509(2008).
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 (By similarity). Hemin-free IsdC (apo-IsdC)
CC acquires hemin from hemin-containing IsdA (holo-IsdA) probably through
CC the activated holo-IsdA-apo-IsdC complex and due to the higher affinity
CC of apo-IsdC for the cofactor. The reaction is reversible. {ECO:0000250,
CC ECO:0000269|PubMed:18184657}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with IsdA. {ECO:0000250,
CC ECO:0000269|PubMed:18184657}.
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 (By similarity).
CC Transcriptionally up-regulated by hydrogen peroxide and to a lesser
CC extent by hypochlorous acid. Slightly down-regulated by human
CC neutrophil azurophilic granule proteins. {ECO:0000250,
CC ECO:0000269|PubMed:18097052}.
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; BA000033; BAB94878.1; -; Genomic_DNA.
DR RefSeq; WP_000789821.1; NC_003923.1.
DR PDB; 2K78; NMR; -; A=25-150.
DR PDBsum; 2K78; -.
DR AlphaFoldDB; Q7A151; -.
DR SMR; Q7A151; -.
DR EnsemblBacteria; BAB94878; BAB94878; BAB94878.
DR KEGG; sam:MW1013; -.
DR HOGENOM; CLU_092243_1_0_9; -.
DR OMA; HNYTIRF; -.
DR EvolutionaryTrace; Q7A151; -.
DR Proteomes; UP000000418; 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 3D-structure; Cell wall; Heme; Iron; Metal-binding; Peptidoglycan-anchor;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..192
FT /note="Iron-regulated surface determinant protein C"
FT /id="PRO_0000019454"
FT PROPEP 193..227
FT /note="Removed by sortase B"
FT /evidence="ECO:0000250|UniProtKB:Q8KQR1"
FT /id="PRO_0000019455"
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"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2K78"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2K78"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2K78"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:2K78"
FT STRAND 129..144
FT /evidence="ECO:0007829|PDB:2K78"
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
