ISDB_STAA8
ID ISDB_STAA8 Reviewed; 645 AA.
AC Q2FZF0; Q8KQR0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SAOUHSC_01079;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IRON-REGULATED EXPRESSION.
RX PubMed=11952908; DOI=10.1046/j.1365-2958.2002.02850.x;
RA Taylor J.M., Heinrichs D.E.;
RT "Transferrin binding in Staphylococcus aureus: involvement of a cell wall-
RT anchored protein.";
RL Mol. Microbiol. 43:1603-1614(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP REGULATION BY FUR, AND SUBCELLULAR LOCATION.
RX PubMed=11953376; DOI=10.1128/iai.70.5.2399-2407.2002;
RA Morrissey J.A., Cockayne A., Hammacott J., Bishop K., Denman-Johnson A.,
RA Hill P.J., Williams P.;
RT "Conservation, surface exposure, and in vivo expression of the Frp family
RT of iron-regulated cell wall proteins in Staphylococcus aureus.";
RL Infect. Immun. 70:2399-2407(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
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.
CC -!- SIMILARITY: Belongs to the IsdB family. {ECO:0000305}.
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DR EMBL; AY061874; AAL33769.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30196.1; -; Genomic_DNA.
DR RefSeq; WP_001041586.1; NZ_LS483365.1.
DR RefSeq; YP_499626.1; NC_007795.1.
DR PDB; 5D1Q; X-ray; 3.22 A; E=325-442.
DR PDB; 5D1X; X-ray; 3.21 A; E=341-458.
DR PDB; 5D1Z; X-ray; 3.17 A; I/J=115-269.
DR PDB; 6P9H; X-ray; 3.00 A; A/B=341-457.
DR PDBsum; 5D1Q; -.
DR PDBsum; 5D1X; -.
DR PDBsum; 5D1Z; -.
DR PDBsum; 6P9H; -.
DR AlphaFoldDB; Q2FZF0; -.
DR SMR; Q2FZF0; -.
DR STRING; 1280.SAXN108_1124; -.
DR ABCD; Q2FZF0; 3 sequenced antibodies.
DR EnsemblBacteria; ABD30196; ABD30196; SAOUHSC_01079.
DR GeneID; 3919242; -.
DR KEGG; sao:SAOUHSC_01079; -.
DR PATRIC; fig|93061.5.peg.990; -.
DR eggNOG; COG5180; Bacteria.
DR eggNOG; COG5386; Bacteria.
DR HOGENOM; CLU_016167_0_0_9; -.
DR OMA; KADNNTY; -.
DR PHI-base; PHI:4568; -.
DR PRO; PR:Q2FZF0; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Heme; Iron; Metal-binding; Peptidoglycan-anchor;
KW Reference proteome; Repeat; 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_0000292579"
FT PROPEP 614..645
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000292580"
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:0000305"
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..113
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"
FT CONFLICT 39..40
FT /note="QA -> K (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="G -> V (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="P -> PT (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> T (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="T -> AKPVA (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> V (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="S -> T (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="E -> EVKA (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> A (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="V -> E (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="T -> D (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="D -> E (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="T -> A (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="T -> A (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="S -> T (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> T (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="T -> M (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..487
FT /note="PS -> TP (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="L -> S (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 524..526
FT /note="TPA -> MPV (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..532
FT /note="TKG -> AKA (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="K -> E (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="L -> I (in Ref. 1; AAL33769)"
FT /evidence="ECO:0000305"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:6P9H"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:6P9H"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:6P9H"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 426..435
FT /evidence="ECO:0007829|PDB:6P9H"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6P9H"
FT STRAND 440..451
FT /evidence="ECO:0007829|PDB:6P9H"
SQ SEQUENCE 645 AA; 72192 MW; C248D6CF84700B55 CRC64;
MNKQQKEFKS FYSIRKSSLG VASVAISTLL LLMSNGEAQA AAEETGGTNT EAQPKTEAVA
SPTTTSEKAP ETKPVANAVS VSNKEVEAPT SETKEAKEVK EVKAPKETKE VKPAAKATNN
TYPILNQELR EAIKNPAIKD KDHSAPNSRP IDFEMKKKDG TQQFYHYASS 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
