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Iron-regulated surface determinant protein B (Fur-regulated protein B) (Staphylococcal iron-regulated protein H) (Staphylococcus aureus surface protein J)

 ISDB_STAAW              Reviewed;         645 AA.
Q8NX66;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 89.
RecName: Full=Iron-regulated surface determinant protein B;
AltName: Full=Fur-regulated protein B;
AltName: Full=Staphylococcal iron-regulated protein H;
AltName: Full=Staphylococcus aureus surface protein J;
Flags: Precursor;
Name=isdB; Synonyms=frpB, sasJ, sirH; OrderedLocusNames=MW1011;
Staphylococcus aureus (strain MW2).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=196620;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MW2;
PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-
acquired MRSA.";
Lancet 359:1819-1827(2002).
[2]
BIOTECHNOLOGY.
PubMed=17075065; DOI=10.1073/pnas.0606863103;
Stranger-Jones Y.K., Bae T., Schneewind O.;
"Vaccine assembly from surface proteins of Staphylococcus aureus.";
Proc. Natl. Acad. Sci. U.S.A. 103:16942-16947(2006).
[3]
FUNCTION IN RESISTANCE TO INNATE HOST DEFENSE, AND INDUCTION.
PubMed=18097052; DOI=10.4049/jimmunol.180.1.500;
Palazzolo-Ballance A.M., Reniere M.L., Braughton K.R.,
Sturdevant D.E., Otto M., Kreiswirth B.N., Skaar E.P., DeLeo F.R.;
"Neutrophil microbicides induce a pathogen survival response in
community-associated methicillin-resistant Staphylococcus aureus.";
J. Immunol. 180:500-509(2008).
-!- FUNCTION: Seems to function as the primary receptor for hemoglobin
since its inactivation inhibits the ability of S.aureus to bind
hemoglobin. Binds hemoglobin in a dose-dependent way. Required for
S.aureus growth using hemoglobin as the sole iron source. Also
required for virulence (By similarity). IsdA and/or IsdB promote
resistance to hydrogen peroxide and killing by neutrophils.
{ECO:0000250, ECO:0000269|PubMed:18097052}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
ProRule:PRU00477}.
-!- INDUCTION: Repressed by fur in the presence of iron (By
similarity). Transcriptionally up-regulated by hydrogen peroxide
and to a lesser extent by hypochlorous acid. Slightly down-
regulated by human neutrophil azurophilic granule proteins.
{ECO:0000250, ECO:0000269|PubMed:18097052}.
-!- BIOTECHNOLOGY: A combined vaccine containing IsdA, IsdB, SdrD and
SdrE afforded significant protection in mice against a lethal
challenge with S.aureus Newman or any of the clinical isolates
NRS252, N315, NRS248, USA100 and USA400. The immune response
elicited by the combined vaccine is greater than the one elicited
by its individual components. {ECO:0000269|PubMed:17075065}.
-!- SIMILARITY: Belongs to the IsdB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BA000033; BAB94876.1; -; Genomic_DNA.
RefSeq; WP_001041586.1; NC_003923.1.
PDB; 2MOQ; NMR; -; A=125-272.
PDBsum; 2MOQ; -.
ProteinModelPortal; Q8NX66; -.
SMR; Q8NX66; -.
EnsemblBacteria; BAB94876; BAB94876; BAB94876.
KEGG; sam:MW1011; -.
HOGENOM; HOG000280077; -.
OMA; KADNNTY; -.
PRO; PR:Q8NX66; -.
Proteomes; UP000000418; Chromosome.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0015232; F:heme transporter activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
CDD; cd06920; NEAT; 1.
InterPro; IPR019948; Gram-positive_anchor.
InterPro; IPR019929; Iron-reg_IsdB.
InterPro; IPR006635; NEAT_dom.
InterPro; IPR037250; NEAT_dom_sf.
InterPro; IPR005877; YSIRK_signal_dom.
Pfam; PF00746; Gram_pos_anchor; 1.
Pfam; PF05031; NEAT; 2.
Pfam; PF04650; YSIRK_signal; 1.
SMART; SM00725; NEAT; 2.
SUPFAM; SSF158911; SSF158911; 2.
TIGRFAMs; TIGR03657; IsdB; 1.
TIGRFAMs; TIGR01168; YSIRK_signal; 1.
PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PROSITE; PS50978; NEAT; 2.
1: Evidence at protein level;
3D-structure; Cell wall; Complete proteome; Iron; Metal-binding;
Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 613 Iron-regulated surface determinant
protein B.
/FTId=PRO_0000292575.
PROPEP 614 645 Removed by sortase A.
{ECO:0000255|PROSITE-ProRule:PRU00477}.
/FTId=PRO_0000292576.
DOMAIN 144 269 NEAT 1. {ECO:0000255|PROSITE-
ProRule:PRU00337}.
DOMAIN 341 458 NEAT 2. {ECO:0000255|PROSITE-
ProRule:PRU00337}.
MOTIF 610 614 LPXTG sorting signal.
{ECO:0000255|PROSITE-ProRule:PRU00477}.
MOD_RES 613 613 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255|PROSITE-
ProRule:PRU00477}.
HELIX 129 132 {ECO:0000244|PDB:2MOQ}.
TURN 136 138 {ECO:0000244|PDB:2MOQ}.
STRAND 148 151 {ECO:0000244|PDB:2MOQ}.
STRAND 153 156 {ECO:0000244|PDB:2MOQ}.
TURN 167 169 {ECO:0000244|PDB:2MOQ}.
STRAND 174 177 {ECO:0000244|PDB:2MOQ}.
STRAND 180 182 {ECO:0000244|PDB:2MOQ}.
STRAND 184 190 {ECO:0000244|PDB:2MOQ}.
TURN 192 194 {ECO:0000244|PDB:2MOQ}.
STRAND 195 202 {ECO:0000244|PDB:2MOQ}.
STRAND 205 207 {ECO:0000244|PDB:2MOQ}.
STRAND 209 215 {ECO:0000244|PDB:2MOQ}.
TURN 216 219 {ECO:0000244|PDB:2MOQ}.
STRAND 220 226 {ECO:0000244|PDB:2MOQ}.
STRAND 231 242 {ECO:0000244|PDB:2MOQ}.
STRAND 245 247 {ECO:0000244|PDB:2MOQ}.
STRAND 253 260 {ECO:0000244|PDB:2MOQ}.
HELIX 264 266 {ECO:0000244|PDB:2MOQ}.
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


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