ISDB_STAAR
ID ISDB_STAAR Reviewed; 652 AA.
AC Q6GHV7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Iron-regulated surface determinant protein B;
DE AltName: Full=Fur-regulated protein B;
DE AltName: Full=Staphylococcal iron-regulated protein H;
DE AltName: Full=Staphylococcus aureus surface protein J;
DE Flags: Precursor;
GN Name=isdB; Synonyms=frpB, sasJ, sirH; OrderedLocusNames=SAR1102;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
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: Cell wall-anchored surface receptor that extracts heme from
CC oxidized metHb to enable growth on hemoglobin as a sole iron source.
CC Rapidly extracts heme from hemoglobin and transfers it to IsdA or IsdC,
CC which then relays it to the membrane transporter/IsdEF for
CC internalization. Promotes also resistance to hydrogen peroxide and
CC killing by neutrophils. {ECO:0000250|UniProtKB:A6QG30}.
CC -!- SUBUNIT: Interacts with host HBA; this interaction allows heme
CC extraction as iron source. Interacts with IsdA.
CC {ECO:0000250|UniProtKB:A6QG30}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:A6QG30}; Peptidoglycan-anchor
CC {ECO:0000250|UniProtKB:A6QG30}. Note=Anchored to the cell wall by
CC sortase A. {ECO:0000250|UniProtKB:A6QG30}.
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 and human neutrophil azurophilic granule
CC proteins. {ECO:0000250, ECO:0000269|PubMed:18097052}.
CC -!- SIMILARITY: Belongs to the IsdB family. {ECO:0000305}.
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DR EMBL; BX571856; CAG40104.1; -; Genomic_DNA.
DR RefSeq; WP_001041573.1; NC_002952.2.
DR AlphaFoldDB; Q6GHV7; -.
DR SMR; Q6GHV7; -.
DR TCDB; 9.A.39.1.1; the gram-positive bacterial hemoglobin receptor (isd) family.
DR TCDB; 9.A.39.1.2; the gram-positive bacterial hemoglobin receptor (isd) family.
DR KEGG; sar:SAR1102; -.
DR HOGENOM; CLU_016167_0_0_9; -.
DR OMA; KADNNTY; -.
DR OrthoDB; 962011at2; -.
DR PRO; PR:Q6GHV7; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06920; NEAT; 1.
DR Gene3D; 2.60.40.1850; -; 2.
DR InterPro; IPR019929; Iron-reg_IsdB.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR006635; NEAT_dom.
DR InterPro; IPR037250; NEAT_dom_sf.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF05031; NEAT; 2.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SMART; SM00725; NEAT; 2.
DR SUPFAM; SSF158911; SSF158911; 2.
DR TIGRFAMs; TIGR03657; IsdB; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS50978; NEAT; 2.
PE 2: Evidence at transcript level;
KW Cell wall; Heme; Iron; Metal-binding; Peptidoglycan-anchor; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..620
FT /note="Iron-regulated surface determinant protein B"
FT /id="PRO_0000292569"
FT PROPEP 621..652
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000292570"
FT DOMAIN 151..276
FT /note="NEAT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT DOMAIN 348..465
FT /note="NEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 41..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..23
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:Q2FZF0"
FT MOTIF 617..621
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 41..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
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:Q7A656"
FT BINDING 447
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:Q7A656"
FT MOD_RES 620
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 652 AA; 72999 MW; 28FF303EF6103428 CRC64;
MNKQQKEFKS FYSIRKSSLG VASVAISTLL LLMSNGEAKA AEETGVTNTE AQPKTEAVAS
PTTTTTEKAP EAKPVAKPVA NAVSVSNKEV VAPTTETKEA KEVKAVKEVK APKEAKEEKP
AAKADNNTYP ILNQELREAI KNPAIKDKDH SAPNSRPIDF EMKKKDGTQQ FYHYASSVKP
ARVIFTDSKP EIELGLQSGQ FWRKFEVYEG DKKLPIKLVS YDTVKDYAYI RFSVSNGTKA
VKIVSSTHFN NKEEKYDYTL MEFAQPIYNS ADKFKTEEDY KAEKLLAPYK KAKTLERQVY
ELNKIQDKLP EKLKAEYKKK LEETKKALDE QVKSAITEFQ NVQPTNEKMT DLQDTKYVVY
ESVENNESMM DAFVKHPIKT GMLNGKKYMV METTNDDYWK DFMVEGQRVR TISKDAKNNT
RTIIFPYVEG KTLYDAIVKV HVKTIDYDGQ YHVRIVDKEA FTKANADKTN KKEQQDNSAK
KETTPAMPSK PTTPPVEKES QKQDSQKDDN KQSPSVEKEN DASSESGKDK MPVTKPAKAE
VESSSTTPTK VVSTTQNVAK PTTASSETTK DVVQTSAGSS EAKDSAPLQK ANIKNTNDGH
TQSQNNKNTQ ENKAKSLPQT GEESNKDMTL PLMALIALSS IVAFVLPRKR KN
