ISDB_STAAB
ID ISDB_STAAB Reviewed; 629 AA.
AC Q2YX96;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SAB0993c;
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: 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IsdB family. {ECO:0000305}.
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DR EMBL; AJ938182; CAI80681.1; -; Genomic_DNA.
DR RefSeq; WP_001041593.1; NC_007622.1.
DR AlphaFoldDB; Q2YX96; -.
DR SMR; Q2YX96; -.
DR ABCD; Q2YX96; 3 sequenced antibodies.
DR KEGG; sab:SAB0993c; -.
DR HOGENOM; CLU_016167_0_0_9; -.
DR OMA; KADNNTY; -.
DR PRO; PR:Q2YX96; -.
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 3: Inferred from homology;
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..597
FT /note="Iron-regulated surface determinant protein B"
FT /id="PRO_0000292565"
FT PROPEP 598..629
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000292566"
FT DOMAIN 128..253
FT /note="NEAT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT DOMAIN 325..442
FT /note="NEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 38..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..605
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 594..598
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 38..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346
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 424
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 597
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 629 AA; 70433 MW; D52D3F2FFFDE8245 CRC64;
MNKQQKEFKS FYSIRKSSLG VASVAISTLL LLMSNGEAQA AEETGGTNTE AQPKTEAVAS
PSTTTEKAPE AKSVANAVSV SNKEVEAPTS ETKEVKPAAK SDNNTYPILN QELREAIKNP
AIKDKDHSAP NSRPIDFEMK KENGEQQFYH YASSVKPARV IFTDSKPEIE LGLQSGQFWR
KFEVYEGDKK LPIKLVSYDT VKDYAYIRFS VSNGTKAVKI VSSTHFNNKE EKYDYTLMEF
AQPIYNSADK FKTEEDYKAE KLLAPYKKAK TLERQVYELN KIQDKLPEKL KAEYKKKLEE
TKKALDEQVK SAITEFQNVQ PTNEKMTDLQ DTKYVVYESV ENNESMMDTF VKHPIKTGML
NGKKYMVMET TNDDYWKDFM VEGQRVRTIS KDAKNNTRTI IFPYVEGKTL YDAIVKVHVK
TIDYDGQYHV RIVDKEAFTK ANADKTNKKE QQDNSAKKET TPATPSKPTT PPVEKESQKQ
DSQKDDNKQS PSVEKENDAS SESGKDKTPA TKPAKGEVES SSTTPTKVVS TTQNAAKPTT
ASSETTKDVV QTSAGSSEAK DSAPLQKANI KNTNDGHTQS ENNKNTQENK AKSLPQTGEE
SNKDMTLPLM SLLALSSIIA FVLPRKRKN
