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1.B.20.1.6
Outer membrane hemagglutinin secretion protein, FhaC. Functionally important conserved motifs have been identified (Delattre et al., 2010).  The x-ray structure reveals a beta-barrel pore obstructed by two structural elements conserved in all two partner secretion systems, an N-terminal α-helix and an extracellular loop.  FhaC goes from the closed to the open state in the presence of the filamentous haemagglutinin adhesin, FHA.  The N-terminal α-helix is displaced into the periplasm during FHA secretion (Guérin et al. 2014).  With two POTRA domains in the periplasm, a transmembrane beta barrel and a large loop harboring a functionally important motif, FhaC epitomizes the conserved features of the superfamily (Jacob-Dubuisson et al. 2009). The conserved secretion domain of FHA interacts with the POTRA domains, specific extracellular loops and strands of FhaC and the inner beta-barrel surface. The interaction map indicates a funnel-like pathway, with conformationally flexible FHA entering the channel in a non-exclusive manner and exiting along a four-stranded beta-sheet at the surface of the FhaC barrel. This sheet of FhaC guides the secretion domain of FHA along discrete steps of translocation and folding (Baud et al. 2014).  The membrane-proximal POTRA domain exists in several conformations, and the binding of FHA displaces this equilibrium (Guérin et al. 2015).

Accession Number:P35077
Protein Name:FhaC
Length:584
Molecular Weight:64446.00
Species:Bordetella pertussis [520]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell outer membrane1
Substrate Hemagglutinin

Cross database links:

HEGENOM: HBG037605
RefSeq: NP_880575.1   
Entrez Gene ID: 2667436   
Pfam: PF08479    PF03865   
BioCyc: BPER257313:BP1884-MONOMER   
KEGG: bpe:BP1884   

Gene Ontology

GO:0009279 C:cell outer membrane
GO:0005886 C:plasma membrane
GO:0046930 C:pore complex
GO:0006811 P:ion transport
GO:0015031 P:protein transport

References (3)

[1] “Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.”  Parkhill J.et.al.   12910271
[2] “Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate.”  Hodak H.et.al.   16771844
[3] “Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily.”  Clantin B.et.al.   17702945
Structure:
2QDZ   3NJT   4QKY   4QL0     

External Searches:

  • Search: DB with
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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTDATNRFRP GLVGRALVRA GLLFAVAACA QAQLLPGARD LNRIDDRQRK EQLQRDIERA 
61:	LTRPPVELNP QSEAAAPARK PDATSGHTVT VHAVDLDFGV EGRLFDPAPL VQDYLNRPLD 
121:	NEQLFLLVKA LSAALYDRGY ATSIVTFVPP GVVDGVLKLK VEWGRIKGWL IDGKPLEGTR 
181:	DRMMVFSAMP GWQDKVLNVF DIDQAIYNIN NGGKTGNITI VPADEYGYSY LDLQLQRRAL 
241:	PRVSLGMDNS GPGTPENGRY KYNASVTAND LLGLNDTLGL YIGNRYYRDA GHDAERNYDL 
301:	MYSVPLGRTR LDLQTGYSTY RNLLKTRYGQ YQSAGNSRSF GLKATRLLYR DTRSQFSVYG 
361:	GLKLRQNKNY LAGTRLDVSS KHYSDVTVGM QYSTQRGANA YFGDLSFTRG VGVNNGKYAA 
421:	YDERGPQGNV SRFNGSLAWT RYMALAGQPI QWASQLGFQY SRQQLLNSYQ ITVGDEYTVR 
481:	GYNLRTSQSG DSGVYLSNTL TVPVQFSLLG KQASVAPFVG ADVGALKSNH PDARTIRMAG 
541:	LAAGVRFDLP YARMSFTYSK PVGAQPGGAP RAPVWLYINA GLSF