#=GF ID Isd_H_B_linker
#=GF AC PF20861.1
#=GF DE Iron-regulated surface determinant protein H/B, linker domain
#=GF AU Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Chuguransky S;0000-0002-0520-0736
#=GF SE ECOD:3796.1.1
#=GF GA 27.00 27.00;
#=GF TC 28.20 28.20;
#=GF NC 24.00 22.70;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 --cpu 4 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RC Paper describing PDB structure 2lhr
#=GF RN [1]
#=GF RM 23132864
#=GF RT Staphylococcus aureus uses a novel multidomain receptor to break
#=GF RT apart human hemoglobin and steal its heme.
#=GF RA Spirig T, Malmirchegini GR, Zhang J, Robson SA, Sjodt M, Liu M,
#=GF RA Krishna Kumar K, Dickson CF, Gell DA, Lei B, Loo JA, Clubb RT;
#=GF RL J Biol Chem. 2013;288:1065-1078.
#=GF RC Paper describing PDB structure 4ij2
#=GF RN [2]
#=GF RM 24425866
#=GF RT Structure of the hemoglobin-IsdH complex reveals the molecular
#=GF RT basis of iron capture by Staphylococcus aureus.
#=GF RA Dickson CF, Kumar KK, Jacques DA, Malmirchegini GR, Spirig T,
#=GF RA Mackay JP, Clubb RT, Guss JM, Gell DA;
#=GF RL J Biol Chem. 2014;289:6728-6738.
#=GF RC Paper describing PDB structure 4xs0
#=GF RN [3]
#=GF RM 26057669
#=GF RT The structure of haemoglobin bound to the haemoglobin receptor
#=GF RT IsdH from Staphylococcus aureus shows disruption of the native
#=GF RT alpha-globin haem pocket.
#=GF RA Dickson CF, Jacques DA, Clubb RT, Guss JM, Gell DA;
#=GF RL Acta Crystallogr D Biol Crystallogr. 2015;71:1295-1306.
#=GF RC Paper describing PDB structure 5vmm
#=GF RN [4]
#=GF RM 29109153
#=GF RT Structure-function analyses reveal key features in
#=GF RT Staphylococcus aureus IsdB-associated unfolding of the
#=GF RT heme-binding pocket of human hemoglobin.
#=GF RA Bowden CFM, Chan ACK, Li EJW, Arrieta AL, Eltis LD, Murphy MEP;
#=GF RL J Biol Chem. 2018;293:177-190.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC The bacterial pathogen Staphylococcus aureus uses two closely
#=GF CC related receptors located on its surface, IsdH and IsdB, to
#=GF CC capture from haemoglobin (Hb) the iron it needs to grow. Both
#=GF CC proteins show conserved near iron transporter (NEAT) domains
#=GF CC (Pfam:PF05031) that function synergistically. These domains,
#=GF CC essential for the arrest of iron, are appropriately positioned
#=GF CC by an alpha-helical linker domain (this entry), which does not
#=GF CC interact itself with the heme group. In IsdH, this linker domain
#=GF CC forms a three-helix bundle structure that is essential for
#=GF CC efficient heme capture [1-4].
#=GF SQ 3
#=GS ISDH_STAA8/471-533 AC Q2FXJ2.1
#=GS A0A178PFC1_MAMLE/450-512 AC A0A178PFC1.1
#=GS ISDB_STAA8/269-331 AC Q2FZF0.1
ISDH_STAA8/471-533 ..DEETYNLQKLLAPYHKAKTLERQVYELEKLQEKLPEKYKAEYKKKLDQTRVELADQVKSAVTE
A0A178PFC1_MAMLE/450-512 sq--SDYKKKKDREKYDNAKTLEDKIRELKKLINKVQDKEKESYTKELQDLENKLDKELKSAVTE
ISDB_STAA8/269-331 ..TEEDYKAEKLLAPYKKAKTLERQVYELNKIQDKLPEKLKAEYKKKLEDTKKALDEQVKSAITE
#=GC seq_cons ..sEEDYKtcKLLAPY+KAKTLERQVYELcKLQ-KLPEKhKAEYKKKL-DT+scLD-QVKSAVTE
//
