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3.A.1.14.20
Heme-iron (hemin) utilization transporter BhuTUV ( Brickman et al., 2006; Vanderpool and Armstrong, 2004).  The crystal structures of BhuUV with or without the periplasmic haem-binding protein BhuT have been solved (Naoe et al. 2016). The TMSs show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of type II importers.

Accession Number:Q7W025
Protein Name:Hemin import ATP-binding protein HmuV
Length:262
Molecular Weight:27800.00
Species:bordetella pertussis [520]
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate ferroheme b

Cross database links:

RefSeq: NP_879216.1   
Entrez Gene ID: 2664027   
Pfam: PF00005   
BioCyc: BPER257313:BP0343-MONOMER   
KEGG: bpe:BP0343   

Gene Ontology

GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0015439 F:heme-transporting ATPase activity
GO:0015886 P:heme transport

References (1)

[1] “Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.”  Parkhill J.et.al.   12910271

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTLQARNLTL ARGGAPILTD VSLTLAPGAL VGLLGANGAG KSTLLAALAG ELAPRSGQVF 
61:	LGDADLATLS ARQLARRRAV LPQKPSLSFD LGVSDVVGMG AYPFPELDPA AVRQLVRDAL 
121:	EQAGVTHLAQ RRYPQLSGGE QQRVQFARVL AQCHAMHAPG QTRYLMLDEP ISNLDPRHQM 
181:	ELLATARALA HEAGMGVLVI VHDINQAARW CDTLALLADG RLAALGPPAD VLTPDHMRRV 
241:	YGIEADVLAH PTLPGRLLVL AR