ISDB_STAA2
ID ISDB_STAA2 Reviewed; 645 AA.
AC A6U0U6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SaurJH1_1210;
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: 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; CP000736; ABR52064.1; -; Genomic_DNA.
DR RefSeq; WP_001041583.1; NC_009632.1.
DR AlphaFoldDB; A6U0U6; -.
DR BMRB; A6U0U6; -.
DR SMR; A6U0U6; -.
DR KEGG; sah:SaurJH1_1210; -.
DR HOGENOM; CLU_016167_0_0_9; -.
DR OMA; KADNNTY; -.
DR PRO; PR:A6U0U6; -.
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..613
FT /note="Iron-regulated surface determinant protein B"
FT /id="PRO_5000256991"
FT PROPEP 614..645
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000333244"
FT DOMAIN 144..269
FT /note="NEAT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT DOMAIN 341..458
FT /note="NEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 38..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..619
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 610..614
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 41..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
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 440
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 613
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 645 AA; 72162 MW; 524BF70EC0C4F9D8 CRC64;
MNKQQKEFKS FYSIRKSSLG VASVAISTLL LLMSNGEAQA AAEETGGTNT EAQPKTEAVA
SPTTTSEKAP ETKPVANAVS VSNKEVEAPT SETKEAKEVK EVKAPKETKA VKPAAKATNN
TYPILNQELR EAIKNPAIKD KDHSAPNSRP IDFEMKKENG EQQFYHYASS VKPARVIFTD
SKPEIELGLQ SGQFWRKFEV YEGDKKLPIK LVSYDTVKDY AYIRFSVSNG TKAVKIVSST
HFNNKEEKYD YTLMEFAQPI YNSADKFKTE EDYKAEKLLA PYKKAKTLER QVYELNKIQD
KLPEKLKAEY KKKLEDTKKA LDEQVKSAIT EFQNVQPTNE KMTDLQDTKY VVYESVENNE
SMMDTFVKHP IKTGMLNGKK YMVMETTNDD YWKDFMVEGQ RVRTISKDAK NNTRTIIFPY
VEGKTLYDAI VKVHVKTIDY DGQYHVRIVD KEAFTKANTD KSNKKEQQDN SAKKEATPAT
PSKPTPSPVE KESQKQDSQK DDNKQLPSVE KENDASSESG KDKTPATKPT KGEVESSSTT
PTKVVSTTQN VAKPTTASSK TTKDVVQTSA GSSEAKDSAP LQKANIKNTN DGHTQSQNNK
NTQENKAKSL PQTGEESNKD MTLPLMALLA LSSIVAFVLP RKRKN
